| ID | ProtoID | Name | Compartment | ContributesToProcess | EnzymaticActivity | CatalysedReaction | ChainLength | RequiresProcess | MolecularWeight | Annotation | Function |
|---|---|---|---|---|---|---|---|---|---|---|---|
| P04718 | P04718 | Cytoplasm | R_RubiscoC_enzyme R_RubiscoO_enzyme |
R_RubiscoC R_RubiscoO |
NaN |
NaN |
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| Q2RSN9 | Q2RSN9 | Cytoplasm | R_CA_enzyme | R_CA | NaN |
NaN |
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| Q31PL2 | Q31PL2 | Cytoplasm | R_prkA_enzyme | R_prkA | NaN |
NaN |
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| b3981 | b3981 | Protein translocase subunit SecE | Cell_inner_membrane | Secretion | 127 | 13,643 | UniprotID: P0AG96 | FUNCTION: Essential subunit of the protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY. {ECO:0000269|PubMed:15140892}. | |||
| b3300 | b3300 | Protein translocase subunit SecY | Cell_inner_membrane | Secretion | 443 | 48,512 | UniprotID: P0AGA2 |  FUNCTION: The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SecY is required to insert newly synthesized SecY into the inner membrane. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true, overexpression also results in FtsH-mediated degradation of SecY. |
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| b0407 | b0407 | Sec translocon accessory complex subunit YajC | Cell_inner_membrane | Secretion | 110 | 11,887 | UniprotID: P0ADZ7 | FUNCTION: The SecYEG-SecDF-YajC-YidC holo-translocon (HTL) protein secretase/insertase is a supercomplex required for protein secretion, insertion of proteins into membranes, and assembly of membrane protein complexes (PubMed:27435098). The SecYEG complex is essential for assembly of a number of proteins and complexes, assembly is facilitated in the presence of the SecDF-YajC-YidC subcomplex (PubMed:27435098). {ECO:0000269|PubMed:27435098}. |
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| b0408 | b0408 | Protein translocase subunit SecD (Sec translocon accessory complex subunit SecD) | Cell_inner_membrane | Secretion | 615 | 66,632 | UniprotID: P0AG90 | FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. The large periplasmic domain is thought to have a base and head domain joined by a hinge; movement of the hinge may be coupled to both proton transport and protein export, with the head domain capturing substrate, and a conformational change preventing backward movement and driving forward movement. Expression of V.alginolyticus SecD and SecF in E.coli confers Na(+)-dependent protein export, strongly suggesting SecDF functions via cation-coupled protein translocation. {ECO:0000269|PubMed:21562494}. |
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| b3175 | b3175 | Protein-export membrane protein SecG (P12) (Preprotein translocase band 1 subunit) | Cell_inner_membrane | Secretion | 110 | 11,365 | UniprotID: P0AG99 | FUNCTION: Subunit of the protein translocation channel SecYEG. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY. Treatment with antibiotics that block translation elongation such as chloramphenicol also leads to degradation of SecY and SecE but not SecG. |
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| b3705 | b3705 | Membrane protein insertase YidC (Foldase YidC) (Inner membrane protein YidC) (Membrane integrase YidC) (Oxa1Ec) | Cell_inner_membrane | Secretion | 548 | 61,526 | UniprotID: P25714 | FUNCTION: Inner membrane protein required for the insertion and/or proper folding and/or complex formation of integral inner membrane proteins. Involved in integration of membrane proteins that insert dependently and independently of the Sec translocase complex, as well as at least 2 lipoproteins. Its own insertion requires SRP and is Sec translocase-dependent. Essential for the integration of Sec-dependent subunit a of the F(0)ATP synthase, FtsQ and SecE proteins and for Sec-independent subunit c of the F(0)ATP synthase, M13 phage procoat and the N-terminus of leader peptidase Lep. Probably interacts directly with Sec-independent substrates. Sec-dependent protein FtsQ interacts first with SecY then subsequently with YidC. Sec-dependent LacY and MalF require YidC to acquire tertiary structure and stability, a chaperone-like function, but not for membrane insertion. Stable maltose transport copmplex formation (MalFGK(2)) also requires YidC. Partially complements a Streptococcus mutans yidC2 disruption mutant. {ECO:0000269|PubMed:10675323, ECO:0000269|PubMed:10949305, ECO:0000269|PubMed:12724529, ECO:0000269|PubMed:12950181, ECO:0000269|PubMed:15067017, ECO:0000269|PubMed:15140892, ECO:0000269|PubMed:17073462, ECO:0000269|PubMed:18456666}. |
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| b0409 | b0409 | Protein translocase subunit SecF (Sec translocon accessory complex subunit SecF) | Cell_inner_membrane | Secretion | 323 | 35,382 | UniprotID: P0AG93 | FUNCTION: Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA. The large periplasmic domain is thought to have a base and head domain joined by a hinge; movement of the hinge may be coupled to both proton transport and protein export, with the head domain capturing substrate, and a conformational change preventing backward movement and driving forward movement. Expression of V.alginolyticus SecD and SecF in E.coli confers Na(+)-dependent protein export, strongly suggesting SecDF functions via cation-coupled protein translocation. {ECO:0000269|PubMed:21562494}. |
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| b3821 | b3821 | Phospholipase A1 (EC 3.1.1.32) (EC 3.1.1.4) (Detergent-resistant phospholipase A) (DR-phospholipase A) (Outer membrane phospholipase A) (OM PLA) (OMPLA) (Phosphatidylcholine 1-acylhydrolase) | Cell_outer_membrane | R_PLIPA1A120pp_enzyme R_PLIPA1A140pp_enzyme R_PLIPA1A141pp_enzyme R_PLIPA1A160pp_enzyme R_PLIPA1A161pp_enzyme R_PLIPA1A180pp_enzyme R_PLIPA1A181pp_enzyme R_PLIPA1E120pp_enzyme R_PLIPA1E140pp_enzyme R_PLIPA1E141pp_enzyme R_PLIPA1E160pp_enzyme R_PLIPA1E161pp_enzyme R_PLIPA1E180pp_enzyme R_PLIPA1E181pp_enzyme R_PLIPA1G120pp_enzyme R_PLIPA1G140pp_enzyme R_PLIPA1G141pp_enzyme R_PLIPA1G160pp_enzyme R_PLIPA1G161pp_enzyme R_PLIPA1G180pp_enzyme R_PLIPA1G181pp_enzyme R_PLIPA2A120pp_enzyme R_PLIPA2A140pp_enzyme R_PLIPA2A141pp_enzyme R_PLIPA2A160pp_enzyme R_PLIPA2A161pp_enzyme R_PLIPA2A180pp_enzyme R_PLIPA2A181pp_enzyme R_PLIPA2E120pp_enzyme R_PLIPA2E140pp_enzyme R_PLIPA2E141pp_enzyme R_PLIPA2E160pp_enzyme R_PLIPA2E161pp_enzyme R_PLIPA2E180pp_enzyme R_PLIPA2E181pp_enzyme R_PLIPA2G120pp_enzyme R_PLIPA2G140pp_enzyme R_PLIPA2G141pp_enzyme R_PLIPA2G160pp_enzyme R_PLIPA2G161pp_enzyme R_PLIPA2G180pp_enzyme R_PLIPA2G181pp_enzyme |
R_PLIPA1A120pp R_PLIPA1A140pp R_PLIPA1A141pp R_PLIPA1A160pp R_PLIPA1A161pp R_PLIPA1A180pp R_PLIPA1A181pp R_PLIPA1E120pp R_PLIPA1E140pp R_PLIPA1E141pp R_PLIPA1E160pp R_PLIPA1E161pp R_PLIPA1E180pp R_PLIPA1E181pp R_PLIPA1G120pp R_PLIPA1G140pp R_PLIPA1G141pp R_PLIPA1G160pp R_PLIPA1G161pp R_PLIPA1G180pp R_PLIPA1G181pp R_PLIPA2A120pp R_PLIPA2A140pp R_PLIPA2A141pp R_PLIPA2A160pp R_PLIPA2A161pp R_PLIPA2A180pp R_PLIPA2A181pp R_PLIPA2E120pp R_PLIPA2E140pp R_PLIPA2E141pp R_PLIPA2E160pp R_PLIPA2E161pp R_PLIPA2E180pp R_PLIPA2E181pp R_PLIPA2G120pp R_PLIPA2G140pp R_PLIPA2G141pp R_PLIPA2G160pp R_PLIPA2G161pp R_PLIPA2G180pp R_PLIPA2G181pp |
289 | Secretion: 289.0, Translation: 289.0, Folding: 28.9 | 33,163 | UniprotID: P0A921 ECnumber: EC 3.1.1.32; 3.1.1.4 |
FUNCTION: Has broad substrate specificity including hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities. Strong expression leads to outer membrane breakdown and cell death; is dormant in normal growing cells. Required for efficient secretion of bacteriocins. | |
| b2519 | b2519 | Penicillin-binding protein 1C (PBP-1c) (PBP1c) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Transpeptidase-like module | Cell_inner_membrane | R_MPTG_duplicate_3_enzyme R_MPTG2_duplicate_3_enzyme |
R_MPTG_duplicate_3 R_MPTG2_duplicate_3 |
770 | Secretion: 770.0, Translation: 770.0, Folding: 77.0 | 85,067 | UniprotID: P76577 ECnumber: EC 2.4.1.129 |
FUNCTION: Cell wall formation. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a transpeptidase C-terminal domain which may not be functional. {ECO:0000269|PubMed:10542235}. | |
| b2518 | b2518 | Nucleoside diphosphate kinase (NDK) (NDP kinase) (EC 2.7.4.6) (Nucleoside-2-P kinase) | Cytoplasm | 143 | Translation: 143.0, Folding: 14.3 | 15,463 | UniprotID: P0A763 ECnumber: EC 2.7.4.6 |
FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. {ECO:0000255|HAMAP-Rule:MF_00451, ECO:0000269|PubMed:7730286}. | |||
| b3824 | b3824 | Homoserine/homoserine lactone efflux protein | Cell_inner_membrane | R_HOMt2pp_duplicate_2_enzyme | R_HOMt2pp_duplicate_2 | 206 | Secretion: 206.0, Translation: 206.0, Folding: 20.6 | 22,427 | UniprotID: P0AG34 | FUNCTION: Conducts the efflux of homoserine and homoserine lactone. {ECO:0000269|PubMed:10386596}. | |
| b3825 | b3825 | Lysophospholipase L2 (EC 3.1.1.5) (Lecithinase B) | Cell_inner_membrane | R_LPLIPAL2A120_enzyme R_LPLIPAL2A140_enzyme R_LPLIPAL2A141_enzyme R_LPLIPAL2A160_enzyme R_LPLIPAL2A161_enzyme R_LPLIPAL2A180_enzyme R_LPLIPAL2A181_enzyme R_LPLIPAL2ATE120_enzyme R_LPLIPAL2ATE140_enzyme R_LPLIPAL2ATE141_enzyme R_LPLIPAL2ATE160_enzyme R_LPLIPAL2ATE161_enzyme R_LPLIPAL2ATE180_enzyme R_LPLIPAL2ATE181_enzyme R_LPLIPAL2ATG120_enzyme R_LPLIPAL2ATG140_enzyme R_LPLIPAL2ATG141_enzyme R_LPLIPAL2ATG160_enzyme R_LPLIPAL2ATG161_enzyme R_LPLIPAL2ATG180_enzyme R_LPLIPAL2ATG181_enzyme R_LPLIPAL2E120_enzyme R_LPLIPAL2E140_enzyme R_LPLIPAL2E141_enzyme R_LPLIPAL2E160_enzyme R_LPLIPAL2E161_enzyme R_LPLIPAL2E180_enzyme R_LPLIPAL2E181_enzyme R_LPLIPAL2G120_enzyme R_LPLIPAL2G140_enzyme R_LPLIPAL2G141_enzyme R_LPLIPAL2G160_enzyme R_LPLIPAL2G161_enzyme R_LPLIPAL2G180_enzyme R_LPLIPAL2G181_enzyme |
R_LPLIPAL2A120 R_LPLIPAL2A140 R_LPLIPAL2A141 R_LPLIPAL2A160 R_LPLIPAL2A161 R_LPLIPAL2A180 R_LPLIPAL2A181 R_LPLIPAL2ATE120 R_LPLIPAL2ATE140 R_LPLIPAL2ATE141 R_LPLIPAL2ATE160 R_LPLIPAL2ATE161 R_LPLIPAL2ATE180 R_LPLIPAL2ATE181 R_LPLIPAL2ATG120 R_LPLIPAL2ATG140 R_LPLIPAL2ATG141 R_LPLIPAL2ATG160 R_LPLIPAL2ATG161 R_LPLIPAL2ATG180 R_LPLIPAL2ATG181 R_LPLIPAL2E120 R_LPLIPAL2E140 R_LPLIPAL2E141 R_LPLIPAL2E160 R_LPLIPAL2E161 R_LPLIPAL2E180 R_LPLIPAL2E181 R_LPLIPAL2G120 R_LPLIPAL2G140 R_LPLIPAL2G141 R_LPLIPAL2G160 R_LPLIPAL2G161 R_LPLIPAL2G180 R_LPLIPAL2G181 |
340 | Secretion: 340.0, Translation: 340.0, Folding: 34.0 | 38,978 | UniprotID: P07000 ECnumber: EC 3.1.1.5 |
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| b3350 | b3350 | Glutathione-regulated potassium-efflux system protein KefB (K(+)/H(+) antiporter) (NEM-activable K(+)/H(+) antiporter) | Cell_inner_membrane | R_Kt3pp_enzyme | R_Kt3pp | 601 | Secretion: 601.0, Translation: 601.0, Folding: 60.1 | 66,411 | UniprotID: P45522 | FUNCTION: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport. {ECO:0000255|HAMAP-Rule:MF_01412, ECO:0000269|PubMed:3301813, ECO:0000269|PubMed:9023177}. | |
| b3458 | b3458 | Leucine-specific-binding protein (L-BP) (LS-BP) | Periplasm | R_LEUabcpp_duplicate_2_enzyme | R_LEUabcpp_duplicate_2 | 369 | Secretion: 369.0, Translation: 369.0, Folding: 36.9 | 39,379 | UniprotID: P04816 | FUNCTION: This protein is a component of the leucine-specific transport system, which is one of the two periplasmic binding protein-dependent transport systems of the high-affinity transport of the branched-chain amino acids in E.coli. | |
| b3829 | b3829 | 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase (EC 2.1.1.14) (Cobalamin-independent methionine synthase) (Methionine synthase, vitamin-B12 independent isozyme) | Cytoplasm | R_METS_duplicate_2_enzyme | R_METS_duplicate_2 | 753 | Translation: 753.0, Folding: 75.3 | 84,674 | UniprotID: P25665 ECnumber: EC 2.1.1.14 |
FUNCTION: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. | |
| b2515 | b2515 | 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (EC 1.17.7.3) (1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase) (Protein GcpE) (Protein E) | Cytoplasm | R_MECDPDH5_enzyme R_MECDPDH5_duplicate_2_enzyme |
R_MECDPDH5 R_MECDPDH5_duplicate_2 |
372 | Translation: 372.0, Folding: 37.2 | 40,684 | UniprotID: P62620 ECnumber: EC 1.17.7.3 |
FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate, using flavodoxin as the reducing agent. {ECO:0000255|HAMAP-Rule:MF_00159, ECO:0000269|PubMed:15978585, ECO:0000269|PubMed:16268586}. | |
| b3359 | b3359 | Acetylornithine/succinyldiaminopimelate aminotransferase (ACOAT) (DapATase) (Succinyldiaminopimelate transferase) (EC 2.6.1.11) (EC 2.6.1.17) | Cytoplasm | R_ACOTA_duplicate_2_enzyme R_SDPTA_enzyme |
R_ACOTA_duplicate_2 R_SDPTA |
406 | Translation: 406.0, Folding: 40.6 | 43,767 | UniprotID: P18335 ECnumber: EC 2.6.1.11; 2.6.1.17 |
FUNCTION: Involved in both the arginine and lysine biosynthetic pathways. {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:10074354}. | |
| b3823 | b3823 | Threonine efflux protein | Cell_inner_membrane | R_THRt2pp_duplicate_2_enzyme | R_THRt2pp_duplicate_2 | 206 | Secretion: 206.0, Translation: 206.0, Folding: 20.6 | 22,474 | UniprotID: P0AG38 | FUNCTION: Conducts the efflux of threonine. {ECO:0000269|PubMed:10386596}. | |
| b3826 | b3826 | Pyridoxal phosphate phosphatase YigL (EC 3.1.3.74) (PLP phosphatase) (Sugar phosphatase) (EC 3.1.3.23) | Cytoplasm | R_PYDXPP_enzyme | R_PYDXPP | 266 | Translation: 266.0, Folding: 26.6 | 29,708 | UniprotID: P27848 ECnumber: EC 3.1.3.74; 3.1.3.23 |
FUNCTION: Catalyzes Strongly the dephosphorylation of pyridoxal-phosphate (PLP) and moderately the dephosphorylation of 2-deoxyglucose 6-phosphate (2bGLU6P) and beta-glucose 6-phosphate (bGlu6P). Also hydrolyzes both purines (GMP and IMP) and pyrimidines as secondary substrates. {ECO:0000269|PubMed:16990279}. | |
| b2199 | b2199 | Heme exporter protein C (Cytochrome c-type biogenesis protein CcmC) | Cell_inner_membrane | R_PHEMEabcpp_enzyme | R_PHEMEabcpp | 245 | Secretion: 245.0, Translation: 245.0, Folding: 24.5 | 27,885 | UniprotID: P0ABM1 | FUNCTION: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes. | |
| b2198 | b2198 | Heme exporter protein D (Cytochrome c-type biogenesis protein CcmD) | Cell_inner_membrane | R_PHEMEabcpp_enzyme | R_PHEMEabcpp | 69 | Secretion: 69.0, Translation: 69.0, Folding: 6.9 | 7,745 | UniprotID: P0ABM5 | FUNCTION: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes. {ECO:0000305}. | |
| b2197 | b2197 | Cytochrome c-type biogenesis protein CcmE (Cytochrome c maturation protein E) (Heme chaperone CcmE) | Cell_inner_membrane | R_PHEMEabcpp_enzyme | R_PHEMEabcpp | 159 | Secretion: 159.0, Translation: 159.0, Folding: 15.9 | 17,698 | UniprotID: P69490 | FUNCTION: Heme chaperone required for the biogenesis of c-type cytochromes. Transiently binds heme delivered by CcmC and transfers the heme to apo-cytochromes in a process facilitated by CcmF and CcmH. | |
| b2925 | b2925 | Fructose-bisphosphate aldolase class 2 (FBP aldolase) (FBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase) (Fructose-bisphosphate aldolase class II) | Cytoplasm | R_FBA_duplicate_3_enzyme R_FBA3_enzyme |
R_FBA_duplicate_3 R_FBA3 |
359 | Translation: 359.0, Folding: 35.9 | 39,147 | UniprotID: P0AB71 ECnumber: EC 4.1.2.13 |
FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis. {ECO:0000269|PubMed:10712619}. | |
| b3734 | b3734 | ATP synthase subunit alpha (EC 3.6.3.14) (ATP synthase F1 sector subunit alpha) (F-ATPase subunit alpha) | Cell_inner_membrane | R_ATPS4rpp_enzyme R_ATPS4rpp_duplicate_2_enzyme |
R_ATPS4rpp R_ATPS4rpp_duplicate_2 |
513 | Secretion: 513.0, Translation: 513.0, Folding: 51.3 | 55,222 | UniprotID: P0ABB0 ECnumber: EC 3.6.3.14 |
FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. | |
| b3735 | b3735 | ATP synthase subunit delta (ATP synthase F(1) sector subunit delta) (F-type ATPase subunit delta) (F-ATPase subunit delta) | Cell_inner_membrane | R_ATPS4rpp_enzyme R_ATPS4rpp_duplicate_2_enzyme |
R_ATPS4rpp R_ATPS4rpp_duplicate_2 |
177 | Secretion: 177.0, Translation: 177.0, Folding: 17.7 | 19,332 | UniprotID: P0ABA4 | FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.; FUNCTION: This protein is part of the stalk that links CF(0) to CF(1). It either transmits conformational changes from CF(0) to CF(1) or is implicated in proton conduction. |
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| b3736 | b3736 | ATP synthase subunit b (ATP synthase F(0) sector subunit b) (ATPase subunit I) (F-type ATPase subunit b) (F-ATPase subunit b) | Cell_inner_membrane | R_ATPS4rpp_enzyme R_ATPS4rpp_duplicate_2_enzyme |
R_ATPS4rpp R_ATPS4rpp_duplicate_2 |
156 | Secretion: 156.0, Translation: 156.0, Folding: 15.6 | 17,264 | UniprotID: P0ABA0 | FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-Rule:MF_01398}.; FUNCTION: Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-Rule:MF_01398}. |
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| b3737 | b3737 | ATP synthase subunit c (ATP synthase F(0) sector subunit c) (Dicyclohexylcarbodiimide-binding protein) (F-type ATPase subunit c) (F-ATPase subunit c) (Lipid-binding protein) | Cell_inner_membrane | R_ATPS4rpp_enzyme R_ATPS4rpp_duplicate_2_enzyme |
R_ATPS4rpp R_ATPS4rpp_duplicate_2 |
79 | Secretion: 79.0, Translation: 79.0, Folding: 7.9 | 8,256 | UniprotID: P68699 | FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.; FUNCTION: Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of 10 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. |
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| b3730 | b3730 | Bifunctional protein GlmU [Includes: UDP-N-acetylglucosamine pyrophosphorylase (EC 2.7.7.23) (N-acetylglucosamine-1-phosphate uridyltransferase); Glucosamine-1-phosphate N-acetyltransferase (EC 2.3.1.157) | Cytoplasm | R_G1PACT_enzyme R_UAGDP_enzyme |
R_G1PACT R_UAGDP |
456 | Translation: 456.0, Folding: 45.6 | 49,190 | UniprotID: P0ACC7 ECnumber: EC 2.7.7.23; 2.3.1.157 |
FUNCTION: Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain. {ECO:0000255|HAMAP-Rule:MF_01631, ECO:0000269|PubMed:10428949, ECO:0000269|PubMed:21984832, ECO:0000269|PubMed:22297115, ECO:0000269|PubMed:8083170, ECO:0000269|PubMed:8555230}. |
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| b3731 | b3731 | ATP synthase epsilon chain (ATP synthase F1 sector epsilon subunit) (F-ATPase epsilon subunit) | Cell_inner_membrane | R_ATPS4rpp_enzyme R_ATPS4rpp_duplicate_2_enzyme |
R_ATPS4rpp R_ATPS4rpp_duplicate_2 |
139 | Secretion: 139.0, Translation: 139.0, Folding: 13.9 | 15,068 | UniprotID: P0A6E6 | FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. | |
| b3732 | b3732 | ATP synthase subunit beta (EC 3.6.3.14) (ATP synthase F1 sector subunit beta) (F-ATPase subunit beta) | Cell_inner_membrane | R_ATPS4rpp_enzyme R_ATPS4rpp_duplicate_2_enzyme |
R_ATPS4rpp R_ATPS4rpp_duplicate_2 |
460 | Secretion: 460.0, Translation: 460.0, Folding: 46.0 | 50,325 | UniprotID: P0ABB4 ECnumber: EC 3.6.3.14 |
FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits. | |
| b3733 | b3733 | ATP synthase gamma chain (ATP synthase F1 sector gamma subunit) (F-ATPase gamma subunit) | Cell_inner_membrane | R_ATPS4rpp_enzyme R_ATPS4rpp_duplicate_2_enzyme |
R_ATPS4rpp R_ATPS4rpp_duplicate_2 |
287 | Secretion: 287.0, Translation: 287.0, Folding: 28.7 | 31,577 | UniprotID: P0ABA6 | FUNCTION: Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex. | |
| b3738 | b3738 | ATP synthase subunit a (ATP synthase F0 sector subunit a) (F-ATPase subunit 6) | Cell_inner_membrane | R_ATPS4rpp_enzyme R_ATPS4rpp_duplicate_2_enzyme |
R_ATPS4rpp R_ATPS4rpp_duplicate_2 |
271 | Secretion: 271.0, Translation: 271.0, Folding: 27.1 | 30,303 | UniprotID: P0AB98 | FUNCTION: Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. | |
| b3739 | b3739 | ATP synthase protein I | Cell_inner_membrane | R_ATPS4rpp_enzyme | R_ATPS4rpp | 126 | Secretion: 126.0, Translation: 126.0, Folding: 12.6 | 13,632 | UniprotID: P0ABC0 | FUNCTION: A possible function for this protein is to guide the assembly of the membrane sector of the ATPase enzyme complex. | |
| b2601 | b2601 | Phospho-2-dehydro-3-deoxyheptonate aldolase, Tyr-sensitive (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase) (DAHP synthase) (Phospho-2-keto-3-deoxyheptonate aldolase) | Cytoplasm | R_DDPA_duplicate_2_enzyme | R_DDPA_duplicate_2 | 356 | Translation: 356.0, Folding: 35.6 | 38,804 | UniprotID: P00888 ECnumber: EC 2.5.1.54 |
FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). | |
| b2600 | b2600 | T-protein [Includes: Chorismate mutase (CM) (EC 5.4.99.5); Prephenate dehydrogenase (PDH) (EC 1.3.1.12) | Cytoplasm | R_CHORM_duplicate_2_enzyme R_PPND_enzyme |
R_CHORM_duplicate_2 R_PPND |
373 | Translation: 373.0, Folding: 37.3 | 42,043 | UniprotID: P07023 ECnumber: EC 5.4.99.5; 1.3.1.12 |
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| b2174 | b2174 | Lipid A 1-diphosphate synthase (EC 2.7.4.29) (Kdo(2)-lipid A phosphotransferase) (Undecaprenyl pyrophosphate:lipid A 1-phosphate phosphotransferase) | Cell_inner_membrane | R_COLIPAKpp_enzyme | R_COLIPAKpp | 237 | Secretion: 237.0, Translation: 237.0, Folding: 23.7 | 26,759 | UniprotID: P76445 ECnumber: EC 2.7.4.29 |
FUNCTION: Involved in the modification of the lipid A domain of lipopolysaccharides (LPS). Transfers a phosphate group from undecaprenyl pyrophosphate (C55-PP) to lipid A to form lipid A 1-diphosphate. Contributes to the recycling of undecaprenyl phosphate (C55-P) (PubMed:18047581). In vitro, has low undecaprenyl-diphosphate phosphatase activity (PubMed:17660416). {ECO:0000269|PubMed:17660416, ECO:0000269|PubMed:18047581}. |
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| b2170 | b2170 | Sugar efflux transporter B | Cell_inner_membrane | R_LCTSt3ipp_duplicate_2_enzyme | R_LCTSt3ipp_duplicate_2 | 393 | Secretion: 393.0, Translation: 393.0, Folding: 39.3 | 42,746 | UniprotID: P33026 | FUNCTION: Involved in the efflux of sugars. The physiological role may be the detoxification of non-metabolizable sugar analogs. Can transport lactose and glucose. | |
| b2997 | b2997 | Hydrogenase-2 small chain (HYD2) (EC 1.12.99.6) (Membrane-bound hydrogenase 2 small subunit) (NiFe hydrogenase) | Cell_inner_membrane | R_HYD1pp_enzyme R_HYD2pp_duplicate_2_enzyme R_HYD3pp_duplicate_2_enzyme |
R_HYD1pp R_HYD2pp_duplicate_2 R_HYD3pp_duplicate_2 |
372 | Secretion: 372.0, Translation: 372.0, Folding: 37.2 | 39,652 | UniprotID: P69741 ECnumber: EC 1.12.99.6 |
FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake. | |
| b2996 | b2996 | Hydrogenase-2 operon protein HybA | Periplasm | R_HYD1pp_enzyme R_HYD2pp_duplicate_2_enzyme R_HYD3pp_duplicate_2_enzyme |
R_HYD1pp R_HYD2pp_duplicate_2 R_HYD3pp_duplicate_2 |
328 | Secretion: 328.0, Translation: 328.0, Folding: 32.8 | 36,003 | UniprotID: P0AAJ8 | FUNCTION: Participates in the periplasmic electron-transferring activity of hydrogenase 2 during its catalytic turnover. | |
| b2995 | b2995 | Probable Ni/Fe-hydrogenase 2 b-type cytochrome subunit | Cell_inner_membrane | R_HYD1pp_enzyme R_HYD2pp_duplicate_2_enzyme R_HYD3pp_duplicate_2_enzyme |
R_HYD1pp R_HYD2pp_duplicate_2 R_HYD3pp_duplicate_2 |
392 | Secretion: 392.0, Translation: 392.0, Folding: 39.2 | 43,602 | UniprotID: P37180 | FUNCTION: Probable b-type cytochrome. | |
| b2994 | b2994 | Hydrogenase-2 large chain (HYD2) (EC 1.12.99.6) (Membrane-bound hydrogenase 2 large subunit) (NiFe hydrogenase) | Cell_inner_membrane | R_HYD1pp_enzyme R_HYD2pp_duplicate_2_enzyme R_HYD3pp_duplicate_2_enzyme |
R_HYD1pp R_HYD2pp_duplicate_2 R_HYD3pp_duplicate_2 |
567 | Secretion: 567.0, Translation: 567.0, Folding: 56.7 | 62,491 | UniprotID: P0ACE0 ECnumber: EC 1.12.99.6 |
FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake. | |
| b3918 | b3918 | CDP-diacylglycerol pyrophosphatase (EC 3.6.1.26) (CDP-diacylglycerol phosphatidylhydrolase) (CDP-diglyceride hydrolase) | Cell_inner_membrane | R_CDAPPA120 R_CDAPPA140 R_CDAPPA141 R_CDAPPA160 R_CDAPPA161 R_CDAPPA180 R_CDAPPA181 |
251 | Secretion: 251.0, Translation: 251.0, Folding: 25.1 | 28,451 | UniprotID: P06282 ECnumber: EC 3.6.1.26 |
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| b3919 | b3919 | Triosephosphate isomerase (TIM) (TPI) (EC 5.3.1.1) (Triose-phosphate isomerase) | Cytoplasm | R_TPI_enzyme | R_TPI | 255 | Translation: 255.0, Folding: 25.5 | 26,972 | UniprotID: P0A858 ECnumber: EC 5.3.1.1 |
FUNCTION: Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:9442062}. | |
| b1897 | b1897 | Trehalose-6-phosphate phosphatase (TPP) (EC 3.1.3.12) (Osmoregulatory trehalose synthesis protein B) (Trehalose 6-phosphate phosphatase) (Trehalose-phosphatase) | Cytoplasm | R_TRE6PP_enzyme | R_TRE6PP | 266 | Translation: 266.0, Folding: 26.6 | 29,175 | UniprotID: P31678 ECnumber: EC 3.1.3.12 |
FUNCTION: Removes the phosphate from trehalose 6-phosphate (Tre6P) to produce free trehalose. Also catalyzes the dephosphorylation of glucose-6-phosphate (Glu6P) and 2-deoxyglucose-6-phosphate (2dGlu6P). {ECO:0000269|PubMed:1310094, ECO:0000269|PubMed:16990279}. | |
| b3915 | b3915 | Ferrous-iron efflux pump FieF | Cell_inner_membrane | R_CD2t3pp R_COBALT2t3pp_duplicate_2 R_FE2t3pp R_HG2t3pp R_MN2t3pp R_NI2t3pp R_ZN2t3pp |
300 | Secretion: 300.0, Translation: 300.0, Folding: 30.0 | 32,927 | UniprotID: P69380 | FUNCTION: Iron-efflux transporter responsible for iron detoxification. Also able to transport Zn(2+) in a proton-dependent manner. {ECO:0000269|PubMed:15549269}. | ||
| b3916 | b3916 | ATP-dependent 6-phosphofructokinase isozyme 1 (ATP-PFK 1) (Phosphofructokinase 1) (EC 2.7.1.11) (6-phosphofructokinase isozyme I) (Phosphohexokinase 1) | Cytoplasm | 320 | Translation: 320.0, Folding: 32.0 | 34,842 | UniprotID: P0A796 ECnumber: EC 2.7.1.11 |
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000255|HAMAP-Rule:MF_00339}. | |||
| b2514 | b2514 | Histidine--tRNA ligase (EC 6.1.1.21) (Histidyl-tRNA synthetase) (HisRS) | Cytoplasm | R_HISTRS_enzyme | R_HISTRS | 424 | Translation: 424.0, Folding: 42.4 | 47,029 | UniprotID: P60906 ECnumber: EC 6.1.1.21 |
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| b1096 | b1096 | Aminodeoxychorismate lyase (EC 4.1.3.38) (4-amino-4-deoxychorismate lyase) (ADC lyase) (ADCL) | Cytoplasm | R_ADCL_enzyme | R_ADCL | 269 | Translation: 269.0, Folding: 26.9 | 29,715 | UniprotID: P28305 ECnumber: EC 4.1.3.38 |
FUNCTION: Involved in the biosynthesis of p-aminobenzoate (PABA), a precursor of tetrahydrofolate. Converts 4-amino-4-deoxychorismate into 4-aminobenzoate (PABA) and pyruvate. {ECO:0000269|PubMed:1644759, ECO:0000269|PubMed:2251281}. | |
| b1095 | b1095 | 3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC 2.3.1.179) (3-oxoacyl-[acyl-carrier-protein] synthase II) (Beta-ketoacyl-ACP synthase II) (KAS II) | Cytoplasm | 413 | Translation: 413.0, Folding: 41.3 | 43,046 | UniprotID: P0AAI5 ECnumber: EC 2.3.1.179 |
FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Has a preference for short chain acid substrates and may function to supply the octanoic substrates for lipoic acid biosynthesis. {ECO:0000269|PubMed:6988423, ECO:0000269|PubMed:9013860}. | |||
| b1094 | b1094 | Acyl carrier protein (ACP) (Cytosolic-activating factor) (CAF) (Fatty acid synthase acyl carrier protein) | Cytoplasm | R_AACPS1_enzyme R_AACPS2_enzyme R_AACPS3_enzyme R_AACPS4_enzyme R_AACPS5_enzyme R_AACPS6_enzyme R_AACPS7_enzyme R_AACPS8_enzyme R_AACPS9_enzyme R_ACOATA_enzyme R_ACPPAT120_enzyme R_ACPPAT140_enzyme R_ACPPAT141_enzyme R_ACPPAT160_enzyme R_ACPPAT161_enzyme R_ACPPAT180_enzyme R_ACPPAT181_enzyme R_G3PAT120_enzyme R_G3PAT140_enzyme R_G3PAT141_enzyme R_G3PAT160_enzyme R_G3PAT161_enzyme R_G3PAT180_enzyme R_G3PAT181_enzyme R_MCOATA_enzyme R_UAGAAT_enzyme |
78 | Translation: 78.0, Folding: 7.8 | 8,640 | UniprotID: P0A6A8 | FUNCTION: Carrier of the growing fatty acid chain in fatty acid biosynthesis. | ||
| b1093 | b1093 | 3-oxoacyl-[acyl-carrier-protein] reductase FabG (EC 1.1.1.100) (3-ketoacyl-acyl carrier protein reductase) (Beta-Ketoacyl-acyl carrier protein reductase) (Beta-ketoacyl-ACP reductase) | Cytoplasm | 244 | Translation: 244.0, Folding: 24.4 | 25,560 | UniprotID: P0AEK2 ECnumber: EC 1.1.1.100 |
FUNCTION: Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis. {ECO:0000269|PubMed:14996818, ECO:0000269|PubMed:8631920}. | |||
| b1092 | b1092 | Malonyl CoA-acyl carrier protein transacylase (MCT) (EC 2.3.1.39) | Cytoplasm | R_MCOATA_enzyme | R_MCOATA | 309 | Translation: 309.0, Folding: 30.9 | 32,417 | UniprotID: P0AAI9 ECnumber: EC 2.3.1.39 |
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| b1091 | b1091 | 3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC 2.3.1.180) (3-oxoacyl-[acyl-carrier-protein] synthase III) (Beta-ketoacyl-ACP synthase III) (KAS III) (EcFabH) | Cytoplasm | R_ACOATA_enzyme R_KAS15_enzyme R_OGMEACPS_enzyme |
R_ACOATA R_KAS15 R_OGMEACPS |
317 | Translation: 317.0, Folding: 31.7 | 33,515 | UniprotID: P0A6R0 ECnumber: EC 2.3.1.180 |
FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain. |
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| b1090 | b1090 | Phosphate acyltransferase (EC 2.3.1.n2) (Acyl-ACP phosphotransacylase) (Acyl-[acyl-carrier-protein]--phosphate acyltransferase) (Phosphate-acyl-ACP acyltransferase) | Cytoplasm | R_ACPPAT120 R_ACPPAT140 R_ACPPAT141 R_ACPPAT160 R_ACPPAT161 R_ACPPAT180 R_ACPPAT181 |
356 | Translation: 356.0, Folding: 35.6 | 38,214 | UniprotID: P27247 ECnumber: EC 2.3.1.n2 |
FUNCTION: Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00019, ECO:0000269|PubMed:17645809}. | ||
| b1098 | b1098 | Thymidylate kinase (EC 2.7.4.9) (Thymidine monophosphate kinase) (dTMP kinase) (TMPK) | Cytoplasm | R_DTMPK_enzyme | R_DTMPK | 213 | Translation: 213.0, Folding: 21.3 | 23,783 | UniprotID: P0A720 ECnumber: EC 2.7.4.9 |
FUNCTION: Catalyzes the reversible phosphorylation of deoxythymidine monophosphate (dTMP) to deoxythymidine diphosphate (dTDP), using ATP as its preferred phosphoryl donor. Situated at the junction of both de novo and salvage pathways of deoxythymidine triphosphate (dTTP) synthesis, is essential for DNA synthesis and cellular growth. | |
| b2779 | b2779 | Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) | Cytoplasm | R_ENO_enzyme | R_ENO | 432 | Translation: 432.0, Folding: 43.2 | 45,655 | UniprotID: P0A6P9 ECnumber: EC 4.2.1.11 |
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation. {ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:14981237, ECO:0000269|PubMed:15522087, ECO:0000269|PubMed:4942326}. |
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| b1270 | b1270 | Cob(I)yrinic acid a,c-diamide adenosyltransferase (EC 2.5.1.17) (Cob(I)alamin adenosyltransferase) (Corrinoid adenosyltransferase) | Cytoplasm | R_CBIAT_enzyme R_CBLAT_enzyme |
R_CBIAT R_CBLAT |
196 | Translation: 196.0, Folding: 19.6 | 21,999 | UniprotID: P0A9H5 ECnumber: EC 2.5.1.17 |
FUNCTION: Required for both de novo synthesis of the corrin ring for the assimilation of exogenous corrinoids. Participates in the adenosylation of a variety of incomplete and complete corrinoids (By similarity). {ECO:0000250}. | |
| b1277 | b1277 | GTP cyclohydrolase-2 (EC 3.5.4.25) (GTP cyclohydrolase II) | Cytoplasm | R_GTPCII2_enzyme | R_GTPCII2 | 196 | Translation: 196.0, Folding: 19.6 | 21,836 | UniprotID: P0A7I7 ECnumber: EC 3.5.4.25 |
FUNCTION: Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5-phosphate (DARP), formate and pyrophosphate. {ECO:0000269|PubMed:235552}. | |
| b1276 | b1276 | Aconitate hydratase A (ACN) (Aconitase) (EC 4.2.1.3) (Iron-responsive protein-like) (IRP-like) (RNA-binding protein) (Stationary phase enzyme) | Cytoplasm | R_ACONTa_duplicate_2_enzyme R_ACONTb_duplicate_2_enzyme |
R_ACONTa_duplicate_2 R_ACONTb_duplicate_2 |
891 | Translation: 891.0, Folding: 89.1 | 97,677 | UniprotID: P25516 ECnumber: EC 4.2.1.3 |
FUNCTION: Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role as a maintenance or survival enzyme during nutritional or oxidative stress. During oxidative stress inactive AcnA apo-enzyme without iron sulfur clusters binds the acnA mRNA 3 UTRs (untranslated regions), stabilizes acnA mRNA and increases AcnA synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnA also enhances the stability of the sodA transcript. {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:10589714, ECO:0000269|PubMed:11932448, ECO:0000269|PubMed:12486059, ECO:0000269|PubMed:1838390, ECO:0000269|PubMed:9421904}. |
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| b1278 | b1278 | Phosphatidylglycerophosphatase B (EC 3.1.3.27) (Diacylglycerol pyrophosphate phosphatase) (DGPP phosphatase) (EC 3.1.3.81) (Phosphatidate phosphatase) (EC 3.1.3.4) (Undecaprenyl pyrophosphate phosphatase) (EC 3.6.1.27) (Undecaprenyl-diphosphatase) | Cell_inner_membrane | R_PAPA120_enzyme R_PAPA120pp_enzyme R_PAPA140_enzyme R_PAPA140pp_enzyme R_PAPA141_enzyme R_PAPA141pp_enzyme R_PAPA160_enzyme R_PAPA160pp_enzyme R_PAPA161_enzyme R_PAPA161pp_enzyme R_PAPA180_enzyme R_PAPA180pp_enzyme R_PAPA181_enzyme R_PAPA181pp_enzyme R_PGPP120_enzyme R_PGPP120pp_duplicate_2_enzyme R_PGPP140_enzyme R_PGPP140pp_duplicate_2_enzyme R_PGPP141_enzyme R_PGPP141pp_duplicate_2_enzyme R_PGPP160_duplicate_2_enzyme R_PGPP160pp_duplicate_2_enzyme R_PGPP161_enzyme R_PGPP161pp_duplicate_2_enzyme R_PGPP180_duplicate_2_enzyme R_PGPP180pp_duplicate_2_enzyme R_PGPP181_enzyme R_PGPP181pp_duplicate_2_enzyme R_UDCPDP_enzyme R_UDCPDPpp_duplicate_2_enzyme |
R_PAPA120 R_PAPA120pp R_PAPA140 R_PAPA140pp R_PAPA141 R_PAPA141pp R_PAPA160 R_PAPA160pp R_PAPA161 R_PAPA161pp R_PAPA180 R_PAPA180pp R_PAPA181 R_PAPA181pp R_PGPP120 R_PGPP120pp_duplicate_2 R_PGPP140 R_PGPP140pp_duplicate_2 R_PGPP141 R_PGPP141pp_duplicate_2 R_PGPP160_duplicate_2 R_PGPP160pp_duplicate_2 R_PGPP161 R_PGPP161pp_duplicate_2 R_PGPP180_duplicate_2 R_PGPP180pp_duplicate_2 R_PGPP181 R_PGPP181pp_duplicate_2 R_UDCPDP R_UDCPDPpp_duplicate_2 |
254 | Secretion: 254.0, Translation: 254.0, Folding: 25.4 | 29,021 | UniprotID: P0A924 ECnumber: EC 3.1.3.27; 3.1.3.81; 3.1.3.4; 3.6.1.27 |
FUNCTION: Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. The pattern of activities varies according to subcellular location, PGP phosphatase activity is higher in the cytoplasmic membrane, whereas PA and LPA phosphatase activities are higher in the outer membrane. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide. {ECO:0000269|PubMed:15778224, ECO:0000269|PubMed:18411271, ECO:0000269|PubMed:21148555, ECO:0000269|PubMed:8940025}. |
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| b4358 | b4358 | L-galactonate-5-dehydrogenase (EC 1.1.1.-) | Cytoplasm | R_GALCTLO_enzyme | R_GALCTLO | 340 | Translation: 340.0, Folding: 34.0 | 36,448 | UniprotID: P39400 ECnumber: EC 1.1.1.- |
FUNCTION: Catalyzes the oxidation of L-galactonate to D-tagaturonate. Required for growth on L-galactonate as the sole carbon source. In vitro, can also use L-gulonate. {ECO:0000269|PubMed:17088549, ECO:0000269|PubMed:24861318}. | |
| b4356 | b4356 | Probable L-galactonate transporter (Galactonate:H(+) symporter) | Cell_inner_membrane | R_GALCTNLt2pp_enzyme | R_GALCTNLt2pp | 453 | Secretion: 453.0, Translation: 453.0, Folding: 45.3 | 49,440 | UniprotID: P39398 | FUNCTION: Probably responsible for the transport of L-galactonate from the periplasm across the inner membrane. Is essential for growth on L-galactonate as the sole carbon source. {ECO:0000269|PubMed:17088549}. | |
| b1651 | b1651 | Lactoylglutathione lyase (EC 4.4.1.5) (Aldoketomutase) (Glyoxalase I) (Glx I) (Ketone-aldehyde mutase) (Methylglyoxalase) (S-D-lactoylglutathione methylglyoxal lyase) | Cytoplasm | R_LGTHL_enzyme | R_LGTHL | 135 | Translation: 135.0, Folding: 13.5 | 14,920 | UniprotID: P0AC81 ECnumber: EC 4.4.1.5 |
FUNCTION: Catalyzes the isomerization of the hemithioacetal formed spontaneously from methylglyoxal and glutathione, to S-lactoylglutathione, which is then hydrolyzed by a type II glyoxalase (GloB or GloC). Is involved in methylglyoxal (MG) detoxification. {ECO:0000269|PubMed:10913283, ECO:0000305|PubMed:25670698}. | |
| b0709 | b0709 | Dipeptide permease D | Cell_inner_membrane | R_LALADGLUtpp_duplicate_4_enzyme R_LALALGLUtpp_duplicate_4_enzyme |
R_LALADGLUtpp_duplicate_4 R_LALALGLUtpp_duplicate_4 |
493 | Secretion: 493.0, Translation: 493.0, Folding: 49.3 | 54,159 | UniprotID: P75742 | FUNCTION: Probable proton-dependent permease that transports dipeptides. {ECO:0000250}. | |
| b1876 | b1876 | Arginine--tRNA ligase (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) | Cytoplasm | R_ARGTRS_enzyme | R_ARGTRS | 577 | Translation: 577.0, Folding: 57.7 | 64,683 | UniprotID: P11875 ECnumber: EC 6.1.1.19 |
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| b1654 | b1654 | Glutaredoxin 4 (Grx4) (Monothiol glutaredoxin) | Cytoplasm | R_GRXR R_PAPSR2 R_RNDR1b R_RNDR2b_duplicate_4 R_RNDR3b R_RNDR4b_duplicate_4 |
115 | Translation: 115.0, Folding: 11.5 | 12,879 | UniprotID: P0AC69 | FUNCTION: Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. {ECO:0000305}. | ||
| b1873 | b1873 | Cytochrome c-type protein TorY | Cell_inner_membrane | R_DMSOR1pp_enzyme R_DMSOR2pp_enzyme R_TMAOR1pp_duplicate_2_enzyme R_TMAOR2pp_duplicate_2_enzyme |
R_DMSOR1pp R_DMSOR2pp R_TMAOR1pp_duplicate_2 R_TMAOR2pp_duplicate_2 |
366 | Secretion: 366.0, Translation: 366.0, Folding: 36.6 | 40,286 | UniprotID: P52005 | FUNCTION: Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase TorZ. Required for electron transfer to the TorZ terminal enzyme. | |
| b1872 | b1872 | Trimethylamine-N-oxide reductase 2 (TMAO reductase 2) (Trimethylamine oxidase 2) (EC 1.7.2.3) | Periplasm | R_DMSOR1pp_enzyme R_DMSOR2pp_enzyme R_TMAOR1pp_duplicate_2_enzyme R_TMAOR2pp_duplicate_2_enzyme |
R_DMSOR1pp R_DMSOR2pp R_TMAOR1pp_duplicate_2 R_TMAOR2pp_duplicate_2 |
809 | Secretion: 809.0, Translation: 809.0, Folding: 80.9 | 88,964 | UniprotID: P46923 ECnumber: EC 1.7.2.3 |
FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. Can also reduce other N- and S-oxide compounds such as 4-methylmorpholine-N-oxide and biotin sulfoxide (BSO), but with a lower catalytic efficiency. | |
| b0875 | b0875 | Aquaporin Z (Bacterial nodulin-like intrinsic protein) | Cell_inner_membrane | R_H2Otpp_duplicate_2_enzyme | R_H2Otpp_duplicate_2 | 231 | Secretion: 231.0, Translation: 231.0, Folding: 23.1 | 23,703 | UniprotID: P60844 | FUNCTION: Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. {ECO:0000269|PubMed:10400575, ECO:0000269|PubMed:10518952, ECO:0000269|PubMed:11493683}. | |
| b0870 | b0870 | Low specificity L-threonine aldolase (Low specificity L-TA) (EC 4.1.2.48) | Cytoplasm | R_ALATA_D2_duplicate_2_enzyme R_ALATA_L2_enzyme R_THRA2_duplicate_2_enzyme R_THRA_duplicate_2_enzyme |
R_ALATA_D2_duplicate_2 R_ALATA_L2 R_THRA2_duplicate_2 R_THRA_duplicate_2 |
333 | Translation: 333.0, Folding: 33.3 | 36,495 | UniprotID: P75823 ECnumber: EC 4.1.2.48 |
FUNCTION: Catalyzes the cleavage of L-allo-threonine and L-threonine to glycine and acetaldehyde. L-threo-phenylserine and L-erythro-phenylserine are also good substrates. | |
| b0871 | b0871 | Pyruvate dehydrogenase [ubiquinone] (EC 1.2.5.1) (Pyruvate oxidase) (POX) [Cleaved into: Alpha-peptide | Cell_inner_membrane | R_POX_enzyme | R_POX | 572 | Secretion: 572.0, Translation: 572.0, Folding: 57.2 | 62,011 | UniprotID: P07003 ECnumber: EC 1.2.5.1 |
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| b4136 | b4136 | Thiol:disulfide interchange protein DsbD (EC 1.8.1.8) (C-type cytochrome biogenesis protein CycZ) (Inner membrane copper tolerance protein) (Protein-disulfide reductase) (Disulfide reductase) | Cell_inner_membrane | R_DSBDR_enzyme R_DSBDR_duplicate_2_enzyme R_TDSR1_enzyme R_TDSR2_enzyme |
R_DSBDR R_DSBDR_duplicate_2 R_TDSR1 R_TDSR2 |
565 | Secretion: 565.0, Translation: 565.0, Folding: 56.5 | 61,795 | UniprotID: P36655 ECnumber: EC 1.8.1.8 |
FUNCTION: Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm, thereby maintaining the active site of DsbC, DsbE and DsbG in a reduced state. This transfer involves a cascade of disulfide bond formation and reduction steps. |
|
| b4132 | b4132 | Probable cadaverine/lysine antiporter | Cell_inner_membrane | R_CADVtpp_enzyme | R_CADVtpp | 444 | Secretion: 444.0, Translation: 444.0, Folding: 44.4 | 46,665 | UniprotID: P0AAE8 | FUNCTION: Probable cadaverine/lysine antiporter or part of it. | |
| b4131 | b4131 | Inducible lysine decarboxylase (LDC) (EC 4.1.1.18) | Cytoplasm | R_LYSDC_duplicate_2_enzyme | R_LYSDC_duplicate_2 | 715 | Translation: 715.0, Folding: 71.5 | 81,260 | UniprotID: P0A9H3 ECnumber: EC 4.1.1.18 |
FUNCTION: Plays a role in pH homeostasis by consuming protons and neutralizing the acidic by-products of carbohydrate fermentation. | |
| b4130 | b4130 | Dipeptide and tripeptide permease C (Dipeptide/tripeptide:H(+) symporter DtpC) | Cell_inner_membrane | R_LALADGLUtpp_enzyme R_LALALGLUtpp_enzyme |
R_LALADGLUtpp R_LALALGLUtpp |
485 | Secretion: 485.0, Translation: 485.0, Folding: 48.5 | 53,055 | UniprotID: P39276 | FUNCTION: Proton-dependent permease that transports di- and tripeptides. Shows significantly higher specificity towards dipeptides than tripeptides. Has a preference for dipeptides with a C-terminal Lys residue. Can bind Ala-Lys, Lys-Ala, Ala-Ala. Can also transport alanine and trialanine. {ECO:0000269|PubMed:19703419, ECO:0000269|PubMed:21933132, ECO:0000269|PubMed:22940668, ECO:0000269|PubMed:24440353}. |
|
| b4139 | b4139 | Aspartate ammonia-lyase (Aspartase) (EC 4.3.1.1) | Cytoplasm | R_ASPT_enzyme | R_ASPT | 478 | Translation: 478.0, Folding: 47.8 | 52,356 | UniprotID: P0AC38 ECnumber: EC 4.3.1.1 |
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| b4138 | b4138 | Anaerobic C4-dicarboxylate transporter DcuA | Cell_inner_membrane | 433 | Secretion: 433.0, Translation: 433.0, Folding: 43.3 | 45,751 | UniprotID: P0ABN5 | FUNCTION: Responsible for the transport of C4-dicarboxylates from the periplasm across the inner membrane. | |||
| b1479 | b1479 | NAD-dependent malic enzyme (NAD-ME) (EC 1.1.1.38) | Cytoplasm | R_ME1_enzyme | R_ME1 | 565 | Translation: 565.0, Folding: 56.5 | 63,197 | UniprotID: P26616 ECnumber: EC 1.1.1.38 |
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| b1478 | b1478 | Alcohol dehydrogenase, propanol-preferring (EC 1.1.1.1) | Cytoplasm | R_ALCD2x_duplicate_2_enzyme | R_ALCD2x_duplicate_2 | 336 | Translation: 336.0, Folding: 33.6 | 35,380 | UniprotID: P39451 ECnumber: EC 1.1.1.1 |
FUNCTION: Preferred specificity is towards 1-propanol. | |
| b1473 | b1473 | Aromatic amino acid exporter YddG | Cell_inner_membrane | R_PHEt2rpp_duplicate_2_enzyme R_TRPt2rpp_enzyme R_TYRt2rpp_duplicate_2_enzyme |
R_PHEt2rpp_duplicate_2 R_TRPt2rpp R_TYRt2rpp_duplicate_2 |
293 | Secretion: 293.0, Translation: 293.0, Folding: 29.3 | 31,539 | UniprotID: P46136 | FUNCTION: Probable efflux pump. Overexpression confers resistance to phenylalanine and increases export of phenylalanine, tyrosine and tryptophan. {ECO:0000269|PubMed:17784858}. | |
| b1475 | b1475 | Formate dehydrogenase, nitrate-inducible, iron-sulfur subunit (Anaerobic formate dehydrogenase iron-sulfur subunit) (Formate dehydrogenase-N subunit beta) (FDH-N subunit beta) | Cell_inner_membrane | R_FDH4pp_duplicate_2_enzyme R_FDH5pp_enzyme |
R_FDH4pp_duplicate_2 R_FDH5pp |
294 | Secretion: 294.0, Translation: 294.0, Folding: 29.4 | 32,239 | UniprotID: P0AAJ3 | FUNCTION: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The beta subunit FdnH is an electron transfer unit containing 4 iron-sulfur clusters; it serves as a conduit for electrons that are transferred from the formate oxidation site in the alpha subunit (FdnG) to the menaquinone associated with the gamma subunit (FdnI) of formate dehydrogenase-N. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). {ECO:0000269|PubMed:11884747}. |
|
| b1474 | b1474 | Formate dehydrogenase, nitrate-inducible, major subunit (EC 1.17.5.3) (Anaerobic formate dehydrogenase major subunit) (Formate dehydrogenase-N subunit alpha) (FDH-N subunit alpha) | Periplasm | R_FDH4pp_duplicate_2_enzyme R_FDH5pp_enzyme |
R_FDH4pp_duplicate_2 R_FDH5pp |
1015 | Secretion: 1014.0, Translation: 1014.0, Folding: 101.4 | 112,963 | UniprotID: P24183 ECnumber: EC 1.17.5.3 |
FUNCTION: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. The alpha subunit FdnG contains the formate oxidation site. Electrons are transferred from formate to menaquinone in the gamma subunit (FdnI), through the 4Fe-4S clusters in the beta subunit (FdnH). Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). {ECO:0000269|PubMed:11884747}. |
|
| b1476 | b1476 | Formate dehydrogenase, nitrate-inducible, cytochrome b556(Fdn) subunit (Anaerobic formate dehydrogenase cytochrome b556 subunit) (Formate dehydrogenase-N subunit gamma) (FDH-N subunit gamma) | Cell_inner_membrane | R_FDH4pp_duplicate_2_enzyme R_FDH5pp_enzyme |
R_FDH4pp_duplicate_2 R_FDH5pp |
217 | Secretion: 217.0, Translation: 217.0, Folding: 21.7 | 25,368 | UniprotID: P0AEK7 | FUNCTION: Formate dehydrogenase allows E.coli to use formate as major electron donor during anaerobic respiration, when nitrate is used as electron acceptor. Subunit gamma is the cytochrome b556 component of the formate dehydrogenase-N, and also contains a menaquinone reduction site that receives electrons from the beta subunit (FdnH), through its hemes. Formate dehydrogenase-N is part of a system that generates proton motive force, together with the dissimilatory nitrate reductase (Nar). {ECO:0000269|PubMed:11884747}. |
|
| b0674 | b0674 | Asparagine synthetase B [glutamine-hydrolyzing] (AS-B) (EC 6.3.5.4) | Cytoplasm | R_ASNS1_enzyme | R_ASNS1 | 554 | Translation: 554.0, Folding: 55.4 | 62,659 | UniprotID: P22106 ECnumber: EC 6.3.5.4 |
FUNCTION: Catalyzes the ATP-dependent conversion of aspartate into asparagine, using glutamine as a source of nitrogen. Can also use ammonia as the nitrogen source in vitro, albeit with lower efficiency. As nucleotide substrates, ATP and dATP are utilized at a similar rate in both the glutamine- and ammonia-dependent reactions, whereas GTP utilization is only 15% that of ATP, and CTP, UTP, ITP and XTP are very poor or not substrates. Also exhibits glutaminase activity. {ECO:0000269|PubMed:20853825, ECO:0000269|PubMed:6102982, ECO:0000269|PubMed:7907328}. |
|
| b0677 | b0677 | N-acetylglucosamine-6-phosphate deacetylase (GlcNAc 6-P deacetylase) (EC 3.5.1.25) | Cytoplasm | R_AGDC_enzyme | R_AGDC | 382 | Translation: 382.0, Folding: 38.2 | 40,949 | UniprotID: P0AF18 ECnumber: EC 3.5.1.25 |
FUNCTION: Involved in the first step in the biosynthesis of amino-sugar-nucleotides. Catalyzes the hydrolysis of the N-acetyl group of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to yield glucosamine 6-phosphate and acetate. In vitro, can also hydrolyze substrate analogs such as N-thioacetyl-D-glucosamine-6-phosphate, N-trifluoroacetyl-D-glucosamine-6-phosphate, N-acetyl-D-glucosamine-6-sulfate, N-acetyl-D-galactosamine-6-phosphate, and N-formyl-D-glucosamine-6-phosphate. {ECO:0000269|PubMed:16630633, ECO:0000269|PubMed:17567047, ECO:0000269|PubMed:17567048, ECO:0000269|PubMed:2190615, ECO:0000269|PubMed:4861885, ECO:0000269|PubMed:9143339}. |
|
| b0678 | b0678 | Glucosamine-6-phosphate deaminase (EC 3.5.99.6) (GlcN6P deaminase) (GNPDA) (Glucosamine-6-phosphate isomerase) | Cytoplasm | R_G6PDA_enzyme | R_G6PDA | 266 | Translation: 266.0, Folding: 26.6 | 29,774 | UniprotID: P0A759 ECnumber: EC 3.5.99.6 |
FUNCTION: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion. | |
| b0679 | b0679 | PTS system N-acetylglucosamine-specific EIICBA component (EIICBA-Nag) (EII-Nag) [Includes: N-acetylglucosamine permease IIC component (PTS system N-acetylglucosamine-specific EIIC component); N-acetylglucosamine-specific phosphotransferase enzyme IIB component (EC 2.7.1.193) (PTS system N-acetylglucosamine-specific EIIB component); N-acetylglucosamine-specific phosphotransferase enzyme IIA component (EC 2.7.1.193) (PTS system N-acetylglucosamine-specific EIIA component) |
Cell_inner_membrane | R_ACGAptspp_duplicate_2_enzyme | R_ACGAptspp_duplicate_2 | 648 | Secretion: 648.0, Translation: 648.0, Folding: 64.8 | 68,347 | UniprotID: P09323 ECnumber: EC 2.7.1.193; 2.7.1.193 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:4919472). This system is involved in N-acetylglucosamine transport (PubMed:4919472). It can also transport and phosphorylate the antibiotic streptozotocin (PubMed:161156). Could play a significant role in the recycling of peptidoglycan (PubMed:19617367). {ECO:0000269|PubMed:161156, ECO:0000269|PubMed:19617367, ECO:0000269|PubMed:4919472, ECO:0000305|PubMed:3056518}. |
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| b4006 | b4006 | Bifunctional purine biosynthesis protein PurH [Includes: Phosphoribosylaminoimidazolecarboxamide formyltransferase (EC 2.1.2.3) (AICAR transformylase); IMP cyclohydrolase (EC 3.5.4.10) (ATIC) (IMP synthase) (Inosinicase) | Cytoplasm | R_AICART_enzyme R_IMPC_enzyme |
R_AICART R_IMPC |
529 | Translation: 529.0, Folding: 52.9 | 57,329 | UniprotID: P15639 ECnumber: EC 2.1.2.3; 3.5.4.10 |
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| b4005 | b4005 | Phosphoribosylamine--glycine ligase (EC 6.3.4.13) (GARS) (Glycinamide ribonucleotide synthetase) (Phosphoribosylglycinamide synthetase) | Cytoplasm | R_PRAGSr_enzyme | R_PRAGSr | 429 | Translation: 429.0, Folding: 42.9 | 45,940 | UniprotID: P15640 ECnumber: EC 6.3.4.13 |
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| b0052 | b0052 | 4-hydroxythreonine-4-phosphate dehydrogenase (EC 1.1.1.262) (4-(phosphohydroxy)-L-threonine dehydrogenase) | Cytoplasm | R_PDX5PS_enzyme | R_PDX5PS | 329 | Translation: 329.0, Folding: 32.9 | 35,114 | UniprotID: P19624 ECnumber: EC 1.1.1.262 |
FUNCTION: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphohydroxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphohydroxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP). {ECO:0000255|HAMAP-Rule:MF_00536, ECO:0000269|PubMed:15026039, ECO:0000269|Ref.5}. | |
| b0907 | b0907 | Phosphoserine aminotransferase (EC 2.6.1.52) (Phosphohydroxythreonine aminotransferase) (PSAT) | Cytoplasm | R_OHPBAT_enzyme R_PSERT_enzyme |
R_OHPBAT R_PSERT |
362 | Translation: 362.0, Folding: 36.2 | 39,783 | UniprotID: P23721 ECnumber: EC 2.6.1.52 |
FUNCTION: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine. Is involved in both pyridoxine and serine biosynthesis. {ECO:0000269|PubMed:2121717, ECO:0000269|PubMed:8706854}. | |
| b0904 | b0904 | Probable formate transporter 1 (Formate channel 1) | Cell_inner_membrane | R_FORt2pp_enzyme R_FORtppi_enzyme |
R_FORt2pp R_FORtppi |
285 | Secretion: 285.0, Translation: 285.0, Folding: 28.5 | 30,991 | UniprotID: P0AC23 | FUNCTION: Involved in the bidirectional transport of formate. | |
| b0902 | b0902 | Pyruvate formate-lyase 1-activating enzyme (EC 1.97.1.4) (Formate-C-acetyltransferase-activating enzyme 1) (PFL-activating enzyme 1) | Cytoplasm | R_OBTFL R_OBTFL_duplicate_2 R_OBTFL_duplicate_3 R_PFL_duplicate_2 R_PFL_duplicate_3 R_PFL_duplicate_4 |
246 | Translation: 246.0, Folding: 24.6 | 28,204 | UniprotID: P0A9N4 ECnumber: EC 1.97.1.4 |
FUNCTION: Activation of pyruvate formate-lyase 1 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5-deoxy-adenosine. | ||
| b0903 | b0903 | Formate acetyltransferase 1 (EC 2.3.1.54) (Pyruvate formate-lyase 1) | Cytoplasm | R_OBTFL_enzyme R_OBTFL_duplicate_2_enzyme R_PFL_duplicate_2_enzyme R_PFL_duplicate_4_enzyme |
R_OBTFL R_OBTFL_duplicate_2 R_PFL_duplicate_2 R_PFL_duplicate_4 |
760 | Translation: 760.0, Folding: 76.0 | 85,357 | UniprotID: P09373 ECnumber: EC 2.3.1.54 |
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| b0459 | b0459 | Maltose O-acetyltransferase (EC 2.3.1.79) (Maltose transacetylase) | Cytoplasm | R_GLCATr_enzyme R_MALTATr_enzyme |
R_GLCATr R_MALTATr |
183 | Translation: 183.0, Folding: 18.3 | 20,096 | UniprotID: P77791 ECnumber: EC 2.3.1.79 |
FUNCTION: Acetylates maltose and other sugars. | |
| b0908 | b0908 | 3-phosphoshikimate 1-carboxyvinyltransferase (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPS) | Cytoplasm | R_PSCVT_enzyme | R_PSCVT | 427 | Translation: 427.0, Folding: 42.7 | 46,096 | UniprotID: P0A6D3 ECnumber: EC 2.5.1.19 |
FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000269|PubMed:12430021, ECO:0000269|PubMed:13129913, ECO:0000269|PubMed:16225867, ECO:0000269|PubMed:17855366, ECO:0000269|PubMed:17958399, ECO:0000269|PubMed:19211556, ECO:0000269|PubMed:6229418}. |
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| b3035 | b3035 | Outer membrane protein TolC (Multidrug efflux pump subunit TolC) (Outer membrane factor TolC) | Cell_outer_membrane | R_CMtpp_enzyme R_CMtpp_duplicate_2_enzyme R_DOXRBCNtpp_enzyme R_DOXRBCNtpp_duplicate_2_enzyme R_FEENTERtex_enzyme R_FUSAtpp_enzyme R_FUSAtpp_duplicate_2_enzyme R_INDOLEt2pp_enzyme R_MINCYCtpp_enzyme R_MINCYCtpp_duplicate_2_enzyme R_NOVBCNtpp_enzyme R_NOVBCNtpp_duplicate_2_enzyme R_RFAMPtpp_enzyme R_RFAMPtpp_duplicate_2_enzyme R_TTRCYCtpp_enzyme R_TTRCYCtpp_duplicate_2_enzyme |
493 | Secretion: 493.0, Translation: 493.0, Folding: 49.3 | 53,741 | UniprotID: P02930 | FUNCTION: Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells. {ECO:0000269|PubMed:11274125, ECO:0000269|PubMed:15228545, ECO:0000269|PubMed:18955484, ECO:0000269|PubMed:23176499, ECO:0000269|PubMed:6337123}. |
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| b3034 | b3034 | ADP-ribose pyrophosphatase (EC 3.6.1.13) (ADP-ribose diphosphatase) (ADP-ribose phosphohydrolase) (ASPPase) (Adenosine diphosphoribose pyrophosphatase) (ADPR-PPase) | Cytoplasm | R_ADPRDP_duplicate_2_enzyme | R_ADPRDP_duplicate_2 | 209 | Translation: 209.0, Folding: 20.9 | 23,667 | UniprotID: Q93K97 ECnumber: EC 3.6.1.13 |
FUNCTION: Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process. {ECO:0000269|PubMed:11416161}. | |
| b2938 | b2938 | Biosynthetic arginine decarboxylase (ADC) (EC 4.1.1.19) | Periplasm | R_ARGDCpp_enzyme | R_ARGDCpp | 658 | Secretion: 658.0, Translation: 658.0, Folding: 65.8 | 73,898 | UniprotID: P21170 ECnumber: EC 4.1.1.19 |
FUNCTION: Catalyzes the biosynthesis of agmatine from arginine. {ECO:0000250}. | |
| b3583 | b3583 | L-ribulose-5-phosphate 4-epimerase SgbE (EC 5.1.3.4) (Phosphoribulose isomerase) | Cytoplasm | R_RBP4E_enzyme | R_RBP4E | 231 | Translation: 231.0, Folding: 23.1 | 25,561 | UniprotID: P37680 ECnumber: EC 5.1.3.4 |
FUNCTION: Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. May be involved in the utilization of 2,3-diketo-L-gulonate. {ECO:0000269|PubMed:10913097, ECO:0000269|PubMed:11741871}. | |
| b3581 | b3581 | 3-keto-L-gulonate-6-phosphate decarboxylase SgbH (KGPDC) (EC 4.1.1.85) (3-dehydro-L-gulonate-6-phosphate decarboxylase) | Cytoplasm | R_KG6PDC_duplicate_2_enzyme | R_KG6PDC_duplicate_2 | 220 | Translation: 220.0, Folding: 22.0 | 23,445 | UniprotID: P37678 ECnumber: EC 4.1.1.85 |
FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. May be involved in the utilization of 2,3-diketo-L-gulonate. {ECO:0000269|PubMed:11741871}. | |
| b3580 | b3580 | L-xylulose/3-keto-L-gulonate kinase (L-xylulokinase) (EC 2.7.1.-) (EC 2.7.1.53) (3-dehydro-L-gulonate kinase) | Cytoplasm | R_3KGK_enzyme R_XYLK2_duplicate_2_enzyme |
R_3KGK R_XYLK2_duplicate_2 |
498 | Translation: 498.0, Folding: 49.8 | 55,155 | UniprotID: P37677 ECnumber: EC 2.7.1.-; 2.7.1.53 |
FUNCTION: Catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. Is involved in L-lyxose utilization via xylulose, and may also be involved in the utilization of 2,3-diketo-L-gulonate. {ECO:0000269|PubMed:11741871, ECO:0000269|PubMed:7961955}. | |
| b3588 | b3588 | Aldehyde dehydrogenase B (EC 1.2.1.-) | Cytoplasm | R_ALDD2y_enzyme R_ALDD3y_enzyme |
R_ALDD2y R_ALDD3y |
512 | Translation: 512.0, Folding: 51.2 | 56,306 | UniprotID: P37685 ECnumber: EC 1.2.1.- |
FUNCTION: Catalyzes the NADP-dependent oxidation of diverse aldehydes such as chloroacetaldehyde, acetaldehyde, propionaldehyde, benzaldehyde, mafosfamide, 4-hydroperoxycyclophosphamide. Its preferred substrates are acetaldehyde and chloroacetaldehyde. | |
| b0353 | b0353 | 3-(3-hydroxy-phenyl)propionate transporter (3HPP transporter) (3-(3-hydroxy-phenyl)propionate:H(+) symporter) (3HPP:H(+) symporter) | Cell_inner_membrane | R_HCINNMt2rpp_enzyme R_HPPPNt2rpp_enzyme |
R_HCINNMt2rpp R_HPPPNt2rpp |
403 | Secretion: 403.0, Translation: 403.0, Folding: 40.3 | 41,551 | UniprotID: P77589 | FUNCTION: Uptake of 3-(3-hydroxyphenyl)propionate (3HPP) across the cytoplasmic membrane. Transport is driven by the proton motive force. Does not transport benzoate, 3-hydroxybenzoate or gentisate. {ECO:0000269|PubMed:23934492}. | |
| b1896 | b1896 | Trehalose-6-phosphate synthase (TPS) (EC 2.4.1.15) (Alpha,alpha-trehalose-phosphate synthase [UDP-forming]) (Osmoregulatory trehalose synthesis protein A) (OtsA) (UDP-glucose-glucosephosphate glucosyltransferase) | Cytoplasm | R_TRE6PS_enzyme | R_TRE6PS | 474 | Translation: 474.0, Folding: 47.4 | 53,611 | UniprotID: P31677 ECnumber: EC 2.4.1.15 |
FUNCTION: Catalyzes the transfer of glucose from UDP-glucose (UDP-Glc) to D-glucose 6-phosphate (Glc-6-P) to form trehalose-6-phosphate. Acts with retention of the anomeric configuration of the UDP-sugar donor. Essential for viability of the cells at low temperatures and at elevated osmotic strength. {ECO:0000269|PubMed:12105274, ECO:0000269|PubMed:1310094, ECO:0000269|PubMed:20077550, ECO:0000269|PubMed:3131312}. |
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| b3917 | b3917 | Sulfate-binding protein (Sulfate starvation-induced protein 2) (SSI2) | Periplasm | R_MOBDabcpp_enzyme R_SULabcpp_duplicate_3_enzyme R_TSULabcpp_duplicate_2_enzyme |
R_MOBDabcpp R_SULabcpp_duplicate_3 R_TSULabcpp_duplicate_2 |
329 | Secretion: 329.0, Translation: 329.0, Folding: 32.9 | 36,659 | UniprotID: P0AG78 | FUNCTION: This protein specifically binds sulfate and is involved in its transmembrane transport. | |
| b3091 | b3091 | Altronate dehydratase (EC 4.2.1.7) (D-altronate hydro-lyase) | Cytoplasm | R_ALTRH_enzyme | R_ALTRH | 495 | Translation: 495.0, Folding: 49.5 | 54,093 | UniprotID: P42604 ECnumber: EC 4.2.1.7 |
FUNCTION: Catalyzes the dehydration of D-altronate. {ECO:0000269|PubMed:3038546}. | |
| b3093 | b3093 | Hexuronate transporter | Cell_inner_membrane | R_GALURt2rpp_enzyme R_GLCURt2rpp_duplicate_2_enzyme |
R_GALURt2rpp R_GLCURt2rpp_duplicate_2 |
432 | Secretion: 432.0, Translation: 432.0, Folding: 43.2 | 46,892 | UniprotID: P0AA78 | FUNCTION: Aldohexuronate transport system. | |
| b3360 | b3360 | Aminodeoxychorismate synthase component 2 (ADC synthase) (ADCS) (EC 2.6.1.85) (4-amino-4-deoxychorismate synthase component 2) (Aminodeoxychorismate synthase, glutamine amidotransferase component) | Cytoplasm | R_ADCS_enzyme | R_ADCS | 187 | Translation: 187.0, Folding: 18.7 | 20,772 | UniprotID: P00903 ECnumber: EC 2.6.1.85 |
FUNCTION: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. {ECO:0000269|PubMed:4914080}. |
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| b3367 | b3367 | Nitrite transporter NirC | Cell_inner_membrane | R_NO2t2rpp_enzyme | R_NO2t2rpp | 268 | Secretion: 268.0, Translation: 268.0, Folding: 26.8 | 28,563 | UniprotID: P0AC26 | FUNCTION: Catalyzes nitrite uptake and nitrite export across the cytoplasmic membrane. Is up to 10-fold more active than NarK or NarU in nitrite uptake for subsequent reduction in the cytoplasm by the NirB/NirD nitrite reductase. {ECO:0000269|PubMed:11967075, ECO:0000269|PubMed:15667293, ECO:0000269|PubMed:18691156}. | |
| b3366 | b3366 | Nitrite reductase (NADH) small subunit (EC 1.7.1.15) | Cytoplasm | R_NTRIR2x_enzyme | R_NTRIR2x | 108 | Translation: 108.0, Folding: 10.8 | 12,284 | UniprotID: P0A9I8 ECnumber: EC 1.7.1.15 |
FUNCTION: Required for activity of the reductase. {ECO:0000269|PubMed:1435259}. | |
| b3365 | b3365 | Nitrite reductase (NADH) large subunit (EC 1.7.1.15) | Cytoplasm | R_NTRIR2x_enzyme | R_NTRIR2x | 847 | Translation: 847.0, Folding: 84.7 | 93,121 | UniprotID: P08201 ECnumber: EC 1.7.1.15 |
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| b3368 | b3368 | Siroheme synthase [Includes: Uroporphyrinogen-III C-methyltransferase (Urogen III methylase) (EC 2.1.1.107) (SUMT) (Uroporphyrinogen III methylase) (UROM); Precorrin-2 dehydrogenase (EC 1.3.1.76); Sirohydrochlorin ferrochelatase (EC 4.99.1.4) | Cytoplasm | R_SHCHD2_enzyme R_SHCHF_enzyme R_UPP3MT_duplicate_2_enzyme |
R_SHCHD2 R_SHCHF R_UPP3MT_duplicate_2 |
457 | Translation: 457.0, Folding: 45.7 | 49,951 | UniprotID: P0AEA8 ECnumber: EC 2.1.1.107; 1.3.1.76; 4.99.1.4 |
FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme. {ECO:0000255|HAMAP-Rule:MF_01646, ECO:0000269|PubMed:2407234, ECO:0000269|PubMed:2407558, ECO:0000269|PubMed:8243665, ECO:0000269|PubMed:8573073, ECO:0000269|PubMed:9461500}. |
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| b3693 | b3693 | 2-dehydro-3-deoxygalactonokinase (EC 2.7.1.58) (2-keto-3-deoxy-galactonokinase) (2-oxo-3-deoxygalactonate kinase) | Cytoplasm | R_DDGALK_enzyme | R_DDGALK | 292 | Translation: 292.0, Folding: 29.2 | 31,374 | UniprotID: P31459 ECnumber: EC 2.7.1.58 |
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| b3691 | b3691 | D-galactonate transporter | Cell_inner_membrane | R_GALCTNt2pp_enzyme | R_GALCTNt2pp | 430 | Secretion: 430.0, Translation: 430.0, Folding: 43.0 | 47,077 | UniprotID: P0AA76 | FUNCTION: Intake of galactonate into the cell. | |
| b3213 | b3213 | Glutamate synthase [NADPH] small chain (EC 1.4.1.13) (Glutamate synthase subunit beta) (GLTS beta chain) (NADPH-GOGAT) | Cytoplasm | R_GLUSy_enzyme | R_GLUSy | 472 | Translation: 472.0, Folding: 47.2 | 52,015 | UniprotID: P09832 ECnumber: EC 1.4.1.13 |
FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. {ECO:0000269|PubMed:4565085}. | |
| b3212 | b3212 | Glutamate synthase [NADPH] large chain (EC 1.4.1.13) (Glutamate synthase subunit alpha) (GLTS alpha chain) (NADPH-GOGAT) | Cytoplasm | R_GLUSy_enzyme | R_GLUSy | 1486 | Translation: 1486.0, Folding: 148.6 | 163,297 | UniprotID: P09831 ECnumber: EC 1.4.1.13 |
FUNCTION: Catalyzes the conversion of L-glutamine and 2-oxoglutarate into two molecules of L-glutamate. {ECO:0000269|PubMed:4565085}. | |
| b3747 | b3747 | Low affinity potassium transport system protein kup (Kup system potassium uptake protein) | Cell_inner_membrane | R_Kt2pp_duplicate_4_enzyme | R_Kt2pp_duplicate_4 | 622 | Secretion: 622.0, Translation: 622.0, Folding: 62.2 | 69,294 | UniprotID: P63183 | FUNCTION: Responsible for the low-affinity transport of potassium into the cell, with the probable concomitant uptake of protons (symport system). Can also transport cesium. {ECO:0000269|PubMed:10214935, ECO:0000269|PubMed:11682179, ECO:0000269|PubMed:2649491}. | |
| b3749 | b3749 | Ribose import ATP-binding protein RbsA (EC 3.6.3.17) | Cell_inner_membrane | R_RIBabcpp_enzyme | R_RIBabcpp | 501 | Secretion: 501.0, Translation: 501.0, Folding: 50.1 | 55,042 | UniprotID: P04983 ECnumber: EC 3.6.3.17 |
FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000269|PubMed:25533465, ECO:0000269|PubMed:6327617, ECO:0000269|PubMed:8762140}. | |
| b3748 | b3748 | D-ribose pyranase (EC 5.4.99.62) | Cytoplasm | R_RIBabcpp_enzyme | R_RIBabcpp | 139 | Translation: 139.0, Folding: 13.9 | 15,292 | UniprotID: P04982 ECnumber: EC 5.4.99.62 |
FUNCTION: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose. It also catalyzes the conversion between beta-allofuranose and beta-allopyranose. {ECO:0000269|PubMed:15060078}. | |
| b2344 | b2344 | Long-chain fatty acid transport protein (Outer membrane FadL protein) (Outer membrane flp protein) | Cell_outer_membrane | R_DDCAtexi R_HDCAtexi R_HDCEAtexi R_OCDCAtexi R_OCDCEAtexi R_TTDCAtexi R_TTDCEAtexi |
446 | Secretion: 446.0, Translation: 446.0, Folding: 44.6 | 48,542 | UniprotID: P10384 | FUNCTION: Involved in translocation of long-chain fatty acids across the outer membrane. It is a receptor for the bacteriophage T2. FadL may form a specific channel. | ||
| b2342 | b2342 | 3-ketoacyl-CoA thiolase FadI (EC 2.3.1.16) (ACSs) (Acetyl-CoA acyltransferase) (Acyl-CoA ligase) (Beta-ketothiolase) (Fatty acid oxidation complex subunit beta) | Cytoplasm | 436 | Translation: 436.0, Folding: 43.6 | 46,531 | UniprotID: P76503 ECnumber: EC 2.3.1.16 |
FUNCTION: Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. {ECO:0000269|PubMed:12270828, ECO:0000269|PubMed:12535077}. |
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| b2615 | b2615 | NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase) | Cytoplasm | R_NADK_enzyme | R_NADK | 292 | Translation: 292.0, Folding: 29.2 | 32,566 | UniprotID: P0A7B3 ECnumber: EC 2.7.1.23 |
FUNCTION: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (UTP, CTP, GTP, dATP, TTP) as phosphoryl donors, while nucleoside mono- or diphosphates and poly(P) can not. {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:11488932, ECO:0000269|PubMed:15855156, ECO:0000269|PubMed:3025169}. |
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| b2341 | b2341 | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) | Cytoplasm | R_ECOAH1_duplicate_2_enzyme R_ECOAH2_duplicate_2_enzyme R_ECOAH3_duplicate_2_enzyme R_ECOAH4_duplicate_2_enzyme R_ECOAH5_duplicate_2_enzyme R_ECOAH6_duplicate_2_enzyme R_ECOAH7_duplicate_2_enzyme R_ECOAH8_duplicate_2_enzyme R_HACD1_duplicate_2_enzyme R_HACD2_duplicate_2_enzyme R_HACD3_duplicate_2_enzyme R_HACD4_duplicate_2_enzyme R_HACD5_duplicate_2_enzyme R_HACD6_duplicate_2_enzyme R_HACD7_duplicate_2_enzyme R_HACD8_duplicate_2_enzyme |
R_ECOAH1_duplicate_2 R_ECOAH2_duplicate_2 R_ECOAH3_duplicate_2 R_ECOAH4_duplicate_2 R_ECOAH5_duplicate_2 R_ECOAH6_duplicate_2 R_ECOAH7_duplicate_2 R_ECOAH8_duplicate_2 R_HACD1_duplicate_2 R_HACD2_duplicate_2 R_HACD3_duplicate_2 R_HACD4_duplicate_2 R_HACD5_duplicate_2 R_HACD6_duplicate_2 R_HACD7_duplicate_2 R_HACD8_duplicate_2 |
714 | Translation: 714.0, Folding: 71.4 | 77,072 | UniprotID: P77399 ECnumber: EC 4.2.1.17; 5.1.2.3; 1.1.1.35 |
FUNCTION: Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities. Strongly involved in the anaerobic degradation of long and medium-chain fatty acids in the presence of nitrate and weakly involved in the aerobic degradation of long-chain fatty acids. {ECO:0000269|PubMed:12270828, ECO:0000269|PubMed:12535077}. |
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| b2167 | b2167 | PTS system fructose-specific EIIBBC component (EIIBBC-Fru) [Includes: PTS system fructose-specific EIIB component (EC 2.7.1.202) (EIII-Fru) (Fructose-specific phosphotransferase enzyme IIB component); PTS system fructose-specific EIIC component (Fructose permease IIC component) | Cell_inner_membrane | R_FRUptspp_enzyme | R_FRUptspp | 563 | Secretion: 563.0, Translation: 563.0, Folding: 56.3 | 57,519 | UniprotID: P20966 ECnumber: EC 2.7.1.202 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport. {ECO:0000269|PubMed:3510127, ECO:0000269|PubMed:8626640, ECO:0000305|PubMed:3076173}. |
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| b2162 | b2162 | Pyrimidine-specific ribonucleoside hydrolase RihB (EC 3.2.2.8) (Cytidine/uridine-specific hydrolase) | Cytoplasm | R_CYTDH_duplicate_2_enzyme R_URIH_duplicate_2_enzyme |
R_CYTDH_duplicate_2 R_URIH_duplicate_2 |
313 | Translation: 313.0, Folding: 31.3 | 33,748 | UniprotID: P33022 ECnumber: EC 3.2.2.8 |
FUNCTION: Hydrolyzes cytidine or uridine to ribose and cytosine or uracil, respectively. Has a clear preference for cytidine over uridine. Strictly specific for ribonucleosides. Has a low but significant activity for the purine nucleoside xanthosine. | |
| b2877 | b2877 | Molybdenum cofactor cytidylyltransferase (MoCo cytidylyltransferase) (EC 2.7.7.76) (CTP:molybdopterin cytidylyltransferase) (Mo-MPT cytidylyltransferase) (Molybdopterin cytidylyltransferase) (Molybdopterin-cytosine dinucleotide synthase) (MCD synthase) | Cytoplasm | R_MOCDS_enzyme | R_MOCDS | 192 | Translation: 192.0, Folding: 19.2 | 21,514 | UniprotID: Q46810 ECnumber: EC 2.7.7.76 |
FUNCTION: Transfers a CMP moiety from CTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor. Is specific for CTP; other nucleotides such as ATP and GTP cannot be utilized. Is also able to convert MPT to MCD in the absence of molybdate, however, with only one catalytic turnover. {ECO:0000269|PubMed:19542235}. | |
| b2168 | b2168 | 1-phosphofructokinase (EC 2.7.1.56) (Fructose 1-phosphate kinase) | Cytoplasm | R_FRUK_enzyme | R_FRUK | 312 | Translation: 312.0, Folding: 31.2 | 33,756 | UniprotID: P0AEW9 ECnumber: EC 2.7.1.56 |
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| b2169 | b2169 | Multiphosphoryl transfer protein (MTP) (Diphosphoryl transfer protein) (DTP) (Phosphotransferase FPr protein) (Pseudo-HPr) [Includes: Phosphocarrier protein HPr (Protein H); PTS system fructose-specific EIIA component (EC 2.7.1.202) (EIIA-Fru) (EIII-Fru) (Fructose-specific phosphotransferase enzyme IIA component) | Cytoplasm | R_FRUptspp_enzyme | R_FRUptspp | 376 | Translation: 376.0, Folding: 37.6 | 39,648 | UniprotID: P69811 ECnumber: EC 2.7.1.202 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II FruAB PTS system is involved in fructose transport. {ECO:0000269|PubMed:3510127, ECO:0000305|PubMed:8013873}. | |
| b2987 | b2987 | Probable low-affinity inorganic phosphate transporter 2 | Cell_inner_membrane | R_PIt2rpp_enzyme | R_PIt2rpp | 499 | Secretion: 499.0, Translation: 499.0, Folding: 49.9 | 53,809 | UniprotID: P43676 | FUNCTION: Low-affinity inorganic phosphate transport. {ECO:0000250}. | |
| b2988 | b2988 | Bifunctional glutathionylspermidine synthetase/amidase (GspSA) [Includes: Glutathionylspermidine amidase (Gsp amidase) (EC 3.5.1.78) (Glutathionylspermidine amidohydrolase [spermidine-forming]); Glutathionylspermidine synthetase (Gsp synthetase) (EC 6.3.1.8) (Glutathione:spermidine ligase [ADP-forming]) (Gsp synthase) | Cytoplasm | R_GSPMDA_enzyme R_GSPMDS_enzyme |
R_GSPMDA R_GSPMDS |
619 | Translation: 619.0, Folding: 61.9 | 70,532 | UniprotID: P0AES0 ECnumber: EC 3.5.1.78; 6.3.1.8 |
FUNCTION: Catalyzes the formation of an amide bond between glutathione (GSH) and spermidine coupled with hydrolysis of ATP; also catalyzes the opposing reaction, i.e. the hydrolysis of glutathionylspermidine (Gsp) back to glutathione and spermidine. The amidase active site can also hydrolyze Gsp-disulfide (Gsp-S-S-Gsp) to Gsp-SG and Gsp S-thiolated proteins (GspSSPs) to GSH S-thiolated protein (GSSPs). Likely acts synergistically with glutaredoxin to regulate the redox environment of E.coli and defend against oxidative damage. In vitro, the amidase active site also catalyzes hydrolysis of amide and ester derivatives of glutathione (e.g. glutathione ethyl ester and glutathione amide) but lacks activity toward acetylspermidine (N1 and N8) and acetylspermine (N1). {ECO:0000269|PubMed:20530482, ECO:0000269|PubMed:23097746, ECO:0000269|PubMed:7775463, ECO:0000269|PubMed:8999955}. |
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| b3960 | b3960 | Argininosuccinate lyase (ASAL) (EC 4.3.2.1) (Arginosuccinase) | Cytoplasm | R_ARGSL_enzyme | R_ARGSL | 457 | Translation: 457.0, Folding: 45.7 | 50,318 | UniprotID: P11447 ECnumber: EC 4.3.2.1 |
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| b3962 | b3962 | Soluble pyridine nucleotide transhydrogenase (STH) (EC 1.6.1.1) (NAD(P)(+) transhydrogenase [B-specific]) | Cytoplasm | R_NADTRHD_enzyme | R_NADTRHD | 466 | Translation: 466.0, Folding: 46.6 | 51,560 | UniprotID: P27306 ECnumber: EC 1.6.1.1 |
FUNCTION: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation. | |
| b3967 | b3967 | Glutamate racemase (EC 5.1.1.3) | Cytoplasm | R_GLUR_enzyme | R_GLUR | 285 | Translation: 285.0, Folding: 28.5 | 31,002 | UniprotID: P22634 ECnumber: EC 5.1.1.3 |
FUNCTION: Provides the (R)-glutamate required for cell wall biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00258, ECO:0000269|PubMed:1355768, ECO:0000269|PubMed:8098327, ECO:0000305|PubMed:17568739}. | |
| b3966 | b3966 | Vitamin B12 transporter BtuB (Cobalamin receptor) (Outer membrane cobalamin translocator) | Cell_outer_membrane | R_ADOCBLtonex_enzyme R_CBItonex_enzyme R_CBL1tonex_enzyme |
R_ADOCBLtonex R_CBItonex R_CBL1tonex |
614 | Secretion: 614.0, Translation: 614.0, Folding: 61.4 | 68,407 | UniprotID: P06129 | FUNCTION: Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. {ECO:0000269|PubMed:10485884, ECO:0000269|PubMed:2687240, ECO:0000269|PubMed:2982793}. |
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| b1927 | b1927 | Cytoplasmic alpha-amylase (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) | Cytoplasm | R_AAMYL_enzyme | R_AAMYL | 495 | Translation: 495.0, Folding: 49.5 | 56,639 | UniprotID: P26612 ECnumber: EC 3.2.1.1 |
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| b2507 | b2507 | GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (GMPS) (Glutamine amidotransferase) | Cytoplasm | R_GMPS2_enzyme | R_GMPS2 | 525 | Translation: 525.0, Folding: 52.5 | 58,679 | UniprotID: P04079 ECnumber: EC 6.3.5.2 |
FUNCTION: Catalyzes the synthesis of GMP from XMP. | |
| b2500 | b2500 | Phosphoribosylglycinamide formyltransferase (EC 2.1.2.2) (5-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART) | Cytoplasm | R_GARFT_enzyme | R_GARFT | 212 | Translation: 212.0, Folding: 21.2 | 23,238 | UniprotID: P08179 ECnumber: EC 2.1.2.2 |
FUNCTION: Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate. {ECO:0000255|HAMAP-Rule:MF_01930, ECO:0000269|PubMed:2185839, ECO:0000269|PubMed:350869}. | |
| b2501 | b2501 | Polyphosphate kinase (EC 2.7.4.1) (ATP-polyphosphate phosphotransferase) (Polyphosphoric acid kinase) | Cell_inner_membrane | R_PPK2_enzyme R_PPK_enzyme |
R_PPK2 R_PPK |
688 | Secretion: 688.0, Translation: 688.0, Folding: 68.8 | 80,432 | UniprotID: P0A7B1 ECnumber: EC 2.7.4.1 |
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP). Can form linear polymers of orthophosphate with chain lengths up to 1000 or more. Can use GTP instead of ATP, but the efficiency of GTP is 5% that of ATP. Also exhibits several other enzymatic activities, which include: ATP synthesis from polyP in the presence of excess ADP, general nucleoside-diphosphate kinase activity, linear guanosine 5-tetraphosphate (ppppG) synthesis and autophosphorylation. {ECO:0000269|PubMed:10660553, ECO:0000269|PubMed:8962061}. |
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| b2502 | b2502 | Exopolyphosphatase (ExopolyPase) (EC 3.6.1.11) (Metaphosphatase) | Cell_inner_membrane | R_PPA_duplicate_3_enzyme R_PPA2_enzyme |
R_PPA_duplicate_3 R_PPA2 |
513 | Secretion: 513.0, Translation: 513.0, Folding: 51.3 | 58,136 | UniprotID: P0AFL6 ECnumber: EC 3.6.1.11 |
FUNCTION: Degradation of inorganic polyphosphates (polyP). Releases orthophosphate processively from the ends of the polyP chain. Has a strong preference for long-chain polyphosphates and has only weak affinity for smaller size polyP of about 15 residues. {ECO:0000269|PubMed:16905100, ECO:0000269|PubMed:8380170, ECO:0000269|PubMed:9143103}. | |
| b2508 | b2508 | Inosine-5-monophosphate dehydrogenase (IMP dehydrogenase) (IMPD) (IMPDH) (EC 1.1.1.205) | Cytoplasm | R_IMPD_enzyme | R_IMPD | 488 | Translation: 488.0, Folding: 48.8 | 52,022 | UniprotID: P0ADG7 ECnumber: EC 1.1.1.205 |
FUNCTION: Catalyzes the conversion of inosine 5-phosphate (IMP) to xanthosine 5-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. {ECO:0000255|HAMAP-Rule:MF_01964, ECO:0000269|PubMed:9341229}. | |
| b0038 | b0038 | L-carnitine CoA-transferase (EC 2.8.3.21) (Crotonobetainyl-CoA:carnitine CoA-transferase) | Cytoplasm | R_CRNBTCT_enzyme R_CRNCBCT_enzyme |
R_CRNBTCT R_CRNCBCT |
405 | Translation: 405.0, Folding: 40.5 | 45,127 | UniprotID: P31572 ECnumber: EC 2.8.3.21 |
FUNCTION: Catalyzes the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA to L-carnitine to generate L-carnitinyl-CoA and gamma-butyrobetaine. Is also able to catalyze the reversible transfer of the CoA moiety from gamma-butyrobetainyl-CoA or L-carnitinyl-CoA to crotonobetaine to generate crotonobetainyl-CoA. {ECO:0000255|HAMAP-Rule:MF_01050, ECO:0000269|PubMed:11551212}. | |
| b2762 | b2762 | Phosphoadenosine phosphosulfate reductase (EC 1.8.4.8) (3-phosphoadenylylsulfate reductase) (PAPS reductase, thioredoxin dependent) (PAPS sulfotransferase) (PAdoPS reductase) | Cytoplasm | R_PAPSR R_PAPSR_duplicate_2 R_PAPSR2 R_PAPSR2_duplicate_2 R_PAPSR2_duplicate_3 R_PAPSR2_duplicate_4 |
244 | Translation: 244.0, Folding: 24.4 | 27,976 | UniprotID: P17854 ECnumber: EC 1.8.4.8 |
FUNCTION: Reduction of activated sulfate into sulfite. | ||
| b2763 | b2763 | Sulfite reductase [NADPH] hemoprotein beta-component (SiR-HP) (SiRHP) (EC 1.8.1.2) | Cytoplasm | R_FADRx2_enzyme R_FLVR_duplicate_2_enzyme R_FMNRx2_duplicate_3_enzyme R_SULR_enzyme |
R_FADRx2 R_FLVR_duplicate_2 R_FMNRx2_duplicate_3 R_SULR |
570 | Translation: 570.0, Folding: 57.0 | 63,998 | UniprotID: P17846 ECnumber: EC 1.8.1.2 |
FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. {ECO:0000255|HAMAP-Rule:MF_01540}. | |
| b2764 | b2764 | Sulfite reductase [NADPH] flavoprotein alpha-component (SiR-FP) (EC 1.8.1.2) | Cytoplasm | R_FADRx2_enzyme R_FLVR_duplicate_2_enzyme R_FMNRx2_duplicate_3_enzyme R_SULR_enzyme |
R_FADRx2 R_FLVR_duplicate_2 R_FMNRx2_duplicate_3 R_SULR |
599 | Translation: 599.0, Folding: 59.9 | 66,270 | UniprotID: P38038 ECnumber: EC 1.8.1.2 |
FUNCTION: Component of the sulfite reductase complex that catalyzes the 6-electron reduction of sulfite to sulfide. This is one of several activities required for the biosynthesis of L-cysteine from sulfate. The flavoprotein component catalyzes the electron flow from NADPH -> FAD -> FMN to the hemoprotein component. {ECO:0000255|HAMAP-Rule:MF_01541}. | |
| b2765 | b2765 | 6-carboxy-5,6,7,8-tetrahydropterin synthase (CPH4 synthase) (EC 4.1.2.50) (Queuosine biosynthesis protein QueD) | Cytoplasm | R_CPH4S_enzyme | R_CPH4S | 121 | Translation: 121.0, Folding: 12.1 | 13,773 | UniprotID: P65870 ECnumber: EC 4.1.2.50 |
FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) and acetaldehyde. Can also convert 6-pyruvoyltetrahydropterin (PPH4) and sepiapterin to CPH4; these 2 compounds are probably intermediates in the reaction from H2NTP. {ECO:0000269|PubMed:19231875}. | |
| b1264 | b1264 | Anthranilate synthase component 1 (AS) (ASI) (EC 4.1.3.27) | Cytoplasm | R_ANS_enzyme | R_ANS | 520 | Translation: 520.0, Folding: 52.0 | 57,494 | UniprotID: P00895 ECnumber: EC 4.1.3.27 |
FUNCTION: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. {ECO:0000269|PubMed:4567790, ECO:0000269|PubMed:4886289, ECO:0000269|PubMed:5333199}. |
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| b1260 | b1260 | Tryptophan synthase alpha chain (EC 4.2.1.20) | Cytoplasm | R_TRPS1_enzyme R_TRPS2_enzyme R_TRPS3_enzyme |
R_TRPS1 R_TRPS2 R_TRPS3 |
268 | Translation: 268.0, Folding: 26.8 | 28,724 | UniprotID: P0A877 ECnumber: EC 4.2.1.20 |
FUNCTION: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. | |
| b1261 | b1261 | Tryptophan synthase beta chain (EC 4.2.1.20) | Cytoplasm | R_TRPS1_enzyme R_TRPS2_enzyme R_TRPS3_enzyme |
R_TRPS1 R_TRPS2 R_TRPS3 |
397 | Translation: 397.0, Folding: 39.7 | 42,983 | UniprotID: P0A879 ECnumber: EC 4.2.1.20 |
FUNCTION: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. | |
| b1262 | b1262 | Tryptophan biosynthesis protein TrpCF [Includes: Indole-3-glycerol phosphate synthase (IGPS) (EC 4.1.1.48); N-(5-phospho-ribosyl)anthranilate isomerase (PRAI) (EC 5.3.1.24) | Cytoplasm | R_IGPS_enzyme R_PRAIi_enzyme |
R_IGPS R_PRAIi |
453 | Translation: 453.0, Folding: 45.3 | 49,492 | UniprotID: P00909 ECnumber: EC 4.1.1.48; 5.3.1.24 |
FUNCTION: Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. | |
| b1263 | b1263 | Bifunctional protein TrpGD [Includes: Anthranilate synthase component 2 (AS) (ASII) (EC 4.1.3.27) (Anthranilate synthase glutamine amidotransferase component); Anthranilate phosphoribosyltransferase (EC 2.4.2.18) | Cytoplasm | R_ANPRT_enzyme R_ANS_enzyme |
R_ANPRT R_ANS |
531 | Translation: 531.0, Folding: 53.1 | 56,870 | UniprotID: P00904 ECnumber: EC 4.1.3.27; 2.4.2.18 |
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| b1528 | b1528 | Sugar efflux transporter | Cell_inner_membrane | R_ARBt3ipp_enzyme R_LCTSt3ipp_duplicate_3_enzyme R_MELIBt3ipp_enzyme |
R_ARBt3ipp R_LCTSt3ipp_duplicate_3 R_MELIBt3ipp |
396 | Secretion: 396.0, Translation: 396.0, Folding: 39.6 | 42,538 | UniprotID: P31122 | FUNCTION: Involved in the efflux of sugars. The physiological role may be the reduction of the intracellular concentration of toxic sugars or sugar metabolites. Transports L-arabinose and to a lesser extent IPTG. Seems to contribute to the control of the arabinose regulon. | |
| b1866 | b1866 | Aspartate--tRNA ligase (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) | Cytoplasm | R_ASPTRS_enzyme | R_ASPTRS | 590 | Translation: 590.0, Folding: 59.0 | 65,913 | UniprotID: P21889 ECnumber: EC 6.1.1.12 |
FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). Also mischarges tRNA(Asp) with D-aspartate, although it is a poor substrate (PubMed:10918062). {ECO:0000255|HAMAP-Rule:MF_00044, ECO:0000269|PubMed:10918062}. | |
| b0849 | b0849 | Glutaredoxin 1 (Grx1) | Cytoplasm | 85 | Translation: 85.0, Folding: 8.5 | 9,685 | UniprotID: P68688 | FUNCTION: The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase. | |||
| b1865 | b1865 | Dihydroneopterin triphosphate diphosphatase (EC 3.6.1.67) (Dihydroneopterin triphosphate pyrophosphatase) (dATP pyrophosphohydrolase) | Cytoplasm | R_DNTPPA_duplicate_2_enzyme R_NTPP5_duplicate_2_enzyme |
R_DNTPPA_duplicate_2 R_NTPP5_duplicate_2 |
150 | Translation: 150.0, Folding: 15.0 | 17,306 | UniprotID: P0AFC0 ECnumber: EC 3.6.1.67 |
FUNCTION: Catalyzes the hydrolysis of dihydroneopterin triphosphate to dihydroneopterin monophosphate and pyrophosphate. Required for efficient folate biosynthesis. Can also hydrolyze nucleoside triphosphates with a preference for dATP. {ECO:0000269|PubMed:17698004, ECO:0000269|PubMed:8798731}. | |
| b1646 | b1646 | Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (Bacteriocuprein) | Periplasm | R_SPODMpp_enzyme | R_SPODMpp | 173 | Secretion: 173.0, Translation: 173.0, Folding: 17.3 | 17,681 | UniprotID: P0AGD1 ECnumber: EC 1.15.1.1 |
FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | |
| b0842 | b0842 | Multidrug transporter MdfA (Chloramphenicol resistance pump Cmr) | Cell_inner_membrane | R_Kt3pp_duplicate_3_enzyme R_NAt3pp_enzyme |
R_Kt3pp_duplicate_3 R_NAt3pp |
410 | Secretion: 410.0, Translation: 410.0, Folding: 41.0 | 44,321 | UniprotID: P0AEY8 | FUNCTION: Efflux pump driven by the proton motive force. Confers resistance to a broad spectrum of chemically unrelated drugs. Confers resistance to a diverse group of cationic or zwitterionic lipophilic compounds such as ethidium bromide, tetraphenylphosphonium, rhodamine, daunomycin, benzalkonium, rifampicin, tetracycline, puromycin, and to chemically unrelated, clinically important antibiotics such as chloramphenicol, erythromycin, and certain aminoglycosides and fluoroquinolones. Overexpression results in isopropyl-beta-D-thiogalactopyranoside (IPTG) exclusion and spectinomycin sensitivity. Transport of neutral substrates is electrogenic, whereas transport of cationic substrates is electroneutral. In addition to its role in multidrug resistance, confers extreme alkaline pH resistance, allowing the growth under conditions that are close to those used normally by alkaliphiles. This activity requires Na(+) or K(+). {ECO:0000269|PubMed:12578981, ECO:0000269|PubMed:15371593, ECO:0000269|PubMed:9079913, ECO:0000269|PubMed:9644262, ECO:0000269|PubMed:9811673}. |
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| b0841 | b0841 | Putative undecaprenyl-diphosphatase YbjG (EC 3.6.1.27) (Undecaprenyl pyrophosphate phosphatase) | Cell_inner_membrane | R_UDCPDP_duplicate_2_enzyme R_UDCPDPpp_duplicate_3_enzyme |
R_UDCPDP_duplicate_2 R_UDCPDPpp_duplicate_3 |
198 | Secretion: 198.0, Translation: 198.0, Folding: 19.8 | 22,399 | UniprotID: P75806 ECnumber: EC 3.6.1.27 |
FUNCTION: Overexpression leads to increased undecaprenyl diphosphatase activity and to increased resistance to bacitracin. May have a preferred substrate other than undecaprenyl diphosphate in vivo. {ECO:0000269|PubMed:15778224}. | |
| b4120 | b4120 | Melibiose carrier protein (Melibiose permease) (Melibiose transporter) (Na+ (Li+)/melibiose symporter) (Thiomethylgalactoside permease II) | Cell_inner_membrane | R_MELIBt2pp_enzyme | R_MELIBt2pp | 473 | Secretion: 473.0, Translation: 473.0, Folding: 47.3 | 52,636 | UniprotID: P02921 | FUNCTION: Responsible for melibiose and other galactoside transport. It is capable of using hydrogen, sodium, and lithium cations as coupling cations for cotransport, depending on the particular sugar transported (symport system). | |
| b4122 | b4122 | Fumarate hydratase class I, anaerobic (EC 4.2.1.2) (D-tartrate dehydratase) (EC 4.2.1.81) (Fumarase B) | Cytoplasm | R_DTARTD_enzyme R_FUM_enzyme |
R_DTARTD R_FUM |
548 | Translation: 548.0, Folding: 54.8 | 60,105 | UniprotID: P14407 ECnumber: EC 4.2.1.2; 4.2.1.81 |
FUNCTION: Catalyzes the reversible hydration of fumarate to (S)-malate. Functions in the generation of fumarate for use as an anaerobic electron acceptor. To a lesser extent, also displays D-tartrate dehydratase activity, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Is required for anaerobic growth on D-tartrate. {ECO:0000269|PubMed:17643228, ECO:0000269|PubMed:23405168, ECO:0000269|PubMed:3282546, ECO:0000269|Ref.6}. |
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| b4123 | b4123 | Anaerobic C4-dicarboxylate transporter DcuB | Cell_inner_membrane | 446 | Secretion: 446.0, Translation: 446.0, Folding: 44.6 | 47,935 | UniprotID: P0ABN9 | FUNCTION: Responsible for the transport of C4-dicarboxylates from the periplasm across the inner membrane. | |||
| b0118 | b0118 | Aconitate hydratase B (ACN) (Aconitase) (EC 4.2.1.3) ((2R,3S)-2-methylisocitrate dehydratase) ((2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase) (2-methyl-cis-aconitate hydratase) (EC 4.2.1.99) (Iron-responsive protein-like) (IRP-like) (RNA-binding protein) | Cytoplasm | R_ACONTa_enzyme R_ACONTb_enzyme R_MICITDr_enzyme |
R_ACONTa R_ACONTb R_MICITDr |
865 | Translation: 865.0, Folding: 86.5 | 93,498 | UniprotID: P36683 ECnumber: EC 4.2.1.3; 4.2.1.99 |
FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnB functions as a RNA-binding regulatory protein. During oxidative stress inactive AcnB apo-enzyme without iron sulfur clusters binds the acnB mRNA 3 UTRs (untranslated regions), stabilizes acnB mRNA and increases AcnB synthesis, thus mediating a post-transcriptional positive autoregulatory switch. AcnB also decreases the stability of the sodA transcript. {ECO:0000269|PubMed:10585860, ECO:0000269|PubMed:10589714, ECO:0000269|PubMed:11932448, ECO:0000269|PubMed:12473114, ECO:0000269|PubMed:15882410, ECO:0000269|PubMed:8000525, ECO:0000269|PubMed:8932712}. |
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| b0115 | b0115 | Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.12) (Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex) (E2) | Cytoplasm | R_PDH_enzyme | R_PDH | 630 | Translation: 630.0, Folding: 63.0 | 66,096 | UniprotID: P06959 ECnumber: EC 2.3.1.12 |
FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3). | |
| b0114 | b0114 | Pyruvate dehydrogenase E1 component (PDH E1 component) (EC 1.2.4.1) | Cytoplasm | R_PDH_enzyme | R_PDH | 887 | Translation: 887.0, Folding: 88.7 | 99,668 | UniprotID: P0AFG8 ECnumber: EC 1.2.4.1 |
FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). | |
| b0116 | b0116 | Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide dehydrogenase) (E3 component of pyruvate and 2-oxoglutarate dehydrogenases complexes) (Glycine cleavage system L protein) | Cytoplasm | R_AKGDH_enzyme R_GLYCL_enzyme R_PDH_enzyme |
R_AKGDH R_GLYCL R_PDH |
474 | Translation: 474.0, Folding: 47.4 | 50,688 | UniprotID: P0A9P0 ECnumber: EC 1.8.1.4 |
FUNCTION: Lipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. | |
| b0110 | b0110 | 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD (EC 3.5.1.28) (N-acetylmuramoyl-L-alanine amidase) | Cytoplasm | R_AGM3PA_enzyme R_AGM4PA_enzyme R_AM3PA_enzyme R_AM4PA_enzyme |
R_AGM3PA R_AGM4PA R_AM3PA R_AM4PA |
183 | Translation: 183.0, Folding: 18.3 | 20,536 | UniprotID: P13016 ECnumber: EC 3.5.1.28 |
FUNCTION: Involved in both cell wall peptidoglycans recycling and beta-lactamase induction. Specifically cleaves the amide bond between the lactyl group of N-acetylmuramic acid and the alpha-amino group of the L-alanine in degradation products containing an anhydro N-acetylmuramyl moiety (By similarity). {ECO:0000250}. | |
| b0112 | b0112 | Aromatic amino acid transport protein AroP (General aromatic amino acid permease) | Cell_inner_membrane | R_HISt2rpp_enzyme R_PHEt2rpp_enzyme R_TRPt2rpp_duplicate_4_enzyme R_TYRt2rpp_enzyme |
R_HISt2rpp R_PHEt2rpp R_TRPt2rpp_duplicate_4 R_TYRt2rpp |
457 | Secretion: 457.0, Translation: 457.0, Folding: 45.7 | 49,690 | UniprotID: P15993 | FUNCTION: Permease that is involved in the transport across the cytoplasmic membrane of the aromatic amino acids (phenylalanine, tyrosine, and tryptophan). | |
| b1468 | b1468 | Respiratory nitrate reductase 2 alpha chain (EC 1.7.99.4) | Cell_inner_membrane | R_NO3R1pp_enzyme R_NO3R2pp_enzyme |
R_NO3R1pp R_NO3R2pp |
1246 | Secretion: 1246.0, Translation: 1246.0, Folding: 124.6 | 140,227 | UniprotID: P19319 ECnumber: EC 1.7.99.4 |
FUNCTION: This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth.; FUNCTION: The alpha chain is the actual site of nitrate reduction. | |
| b1469 | b1469 | Nitrate/nitrite transporter NarU (Nitrite extrusion protein 2) (Nitrite facilitator 2) | Cell_inner_membrane | R_NO3t7pp_duplicate_2_enzyme | R_NO3t7pp_duplicate_2 | 462 | Secretion: 462.0, Translation: 462.0, Folding: 46.2 | 49,890 | UniprotID: P37758 | FUNCTION: Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane. May function as a nitrate/H(+) and nitrite/H(+) channel. Could confer a selective advantage during severe nutrient starvation or slow growth. {ECO:0000269|PubMed:11967075, ECO:0000269|PubMed:15667293, ECO:0000269|PubMed:16804183, ECO:0000269|PubMed:18691156}. | |
| b1463 | b1463 | N-hydroxyarylamine O-acetyltransferase (EC 2.3.1.118) (Arylamine N-acetyltransferase) (Arylhydroxamate N,O-acetyltransferase) | Cytoplasm | R_ACANTHAT_enzyme | R_ACANTHAT | 281 | Translation: 281.0, Folding: 28.1 | 32,275 | UniprotID: P77567 ECnumber: EC 2.3.1.118 |
FUNCTION: Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O-acetyltransferase activity. {ECO:0000269|PubMed:10806332, ECO:0000305|PubMed:12222687, ECO:0000305|PubMed:23452042}. |
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| b1466 | b1466 | Probable nitrate reductase molybdenum cofactor assembly chaperone NarW (Redox enzyme maturation protein NarW) | Cytoplasm | R_NO3R1pp_enzyme R_NO3R2pp_enzyme |
R_NO3R1pp R_NO3R2pp |
231 | Translation: 231.0, Folding: 23.1 | 26,161 | UniprotID: P19317 | FUNCTION: Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 2. {ECO:0000250}. | |
| b1467 | b1467 | Respiratory nitrate reductase 2 beta chain (EC 1.7.99.4) | Cell_inner_membrane | R_NO3R1pp_enzyme R_NO3R2pp_enzyme |
R_NO3R1pp R_NO3R2pp |
514 | Secretion: 514.0, Translation: 514.0, Folding: 51.4 | 58,558 | UniprotID: P19318 ECnumber: EC 1.7.99.4 |
FUNCTION: This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit. |
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| b1465 | b1465 | Respiratory nitrate reductase 2 gamma chain (EC 1.7.99.4) | Cell_inner_membrane | R_NO3R1pp_enzyme R_NO3R2pp_enzyme |
R_NO3R1pp R_NO3R2pp |
226 | Secretion: 226.0, Translation: 226.0, Folding: 22.6 | 26,018 | UniprotID: P0AF32 ECnumber: EC 1.7.99.4 |
FUNCTION: This is a second nitrate reductase enzyme which can substitute for the NRA enzyme and allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. | |
| b0591 | b0591 | Enterobactin exporter EntS (Protein p43) | Cell_inner_membrane | R_FEENTERtpp_enzyme | R_FEENTERtpp | 416 | Secretion: 416.0, Translation: 416.0, Folding: 41.6 | 43,282 | UniprotID: P24077 | FUNCTION: Exports the siderophore enterobactin out of the cell. {ECO:0000269|PubMed:12068807}. | |
| b0590 | b0590 | Ferric enterobactin transport system permease protein FepD | Cell_inner_membrane | R_FE3DHBZSabcpp_enzyme R_FEENTERabcpp_enzyme |
R_FE3DHBZSabcpp R_FEENTERabcpp |
334 | Secretion: 334.0, Translation: 334.0, Folding: 33.4 | 33,871 | UniprotID: P23876 | FUNCTION: Part of the binding-protein-dependent transport system for ferric enterobactin. Probably responsible for the translocation of the substrate across the membrane. | |
| b0593 | b0593 | Isochorismate synthase EntC (EC 5.4.4.2) (Isochorismate mutase) | Cytoplasm | R_ICHORS_copy2_enzyme | R_ICHORS_copy2 | 391 | Translation: 391.0, Folding: 39.1 | 42,932 | UniprotID: P0AEJ2 ECnumber: EC 5.4.4.2 |
FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine). Catalyzes the reversible conversion of chorismate to isochorismate. {ECO:0000269|PubMed:17243787, ECO:0000269|PubMed:20079748, ECO:0000269|PubMed:2139795, ECO:0000269|PubMed:2536681, ECO:0000269|PubMed:8655506, ECO:0000269|PubMed:9795253}. | |
| b0592 | b0592 | Ferrienterobactin-binding periplasmic protein | Periplasm | R_FE3DHBZSabcpp_enzyme R_FEENTERabcpp_enzyme |
R_FE3DHBZSabcpp R_FEENTERabcpp |
318 | Secretion: 318.0, Translation: 318.0, Folding: 31.8 | 34,283 | UniprotID: P0AEL6 | FUNCTION: Binds ferrienterobactin; part of the binding-protein-dependent transport system for uptake of ferrienterobactin. | |
| b0595 | b0595 | Enterobactin synthase component B (EC 6.3.2.14) (Enterobactin biosynthesis bifunctional protein EntB) (Enterochelin synthase B) [Includes: Isochorismatase (EC 3.3.2.1) (2 3-dihydro-2 3-dihydroxybenzoate synthase) (Isochorismate lyase); Aryl carrier protein (ArCP) | Cytoplasm | R_ICHORT_enzyme | R_ICHORT | 285 | Translation: 285.0, Folding: 28.5 | 32,554 | |||
| b0594 | b0594 | Enterobactin synthase component E (EC 6.3.2.14) (2,3-dihydroxybenzoate-AMP ligase) (DHB-AMP ligase) (2,3-dihydroxybenzoate-AMP synthase) (EC 2.7.7.58) (Dihydroxybenzoic acid-activating enzyme) (Enterochelin synthase E) (S-dihydroxybenzoyltransferase) (EC 2.5.1.-) | Cell_inner_membrane | R_DHBS_enzyme | R_DHBS | 536 | Secretion: 536.0, Translation: 536.0, Folding: 53.6 | 59,112 | UniprotID: P10378 ECnumber: EC 6.3.2.14; 2.7.7.58; 2.5.1.- |
FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. EntE proccesses via a two-step adenylation-ligation reaction (bi-uni-uni-bi ping-pong mechanism). First, it catalyzes the activation of the carboxylate group of 2,3-dihydroxy-benzoate (DHB), via a reversible ATP-dependent pyrophosphate exchange reactions to yield the acyladenylate intermediate 2,3-dihydroxybenzoyl-AMP. It can also transfer AMP to salicylate, 2,4-dihydroxybenzoate, gentisate and 2,3,4-trihydroxybenzoate. In the second step, DHB is transferred from 2,3-dihydroxybenzoyl-AMP onto the phosphopantetheinylated EntB (holo-EntB) to form DHB-holo-EntB. Then this product will serve in the formation of the amide bond between 2,3-dihydroxybenzoate (DHB) and L-serine. It can also transfer adenylated salicylate to holo-EntB. {ECO:0000269|PubMed:10688898, ECO:0000269|PubMed:16567620, ECO:0000269|PubMed:16632253, ECO:0000269|PubMed:19699210, ECO:0000269|PubMed:19852513, ECO:0000269|PubMed:20359185, ECO:0000269|PubMed:20845982, ECO:0000269|PubMed:21166461, ECO:0000269|PubMed:2531000, ECO:0000269|PubMed:9214294}. |
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| b0596 | b0596 | 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (DiDHB-DH) (EC 1.3.1.28) (Trans-2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase) | Cytoplasm | R_DHBD_enzyme | R_DHBD | 248 | Translation: 248.0, Folding: 24.8 | 26,250 | UniprotID: P15047 ECnumber: EC 1.3.1.28 |
FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. Catalyzes the reversible NAD-dependent oxidation of the C3-hydroxyl group of 2,3-dihydro-2,3-dihydroxybenzoate (2,3-diDHB), producing the transient intermediate 2-hydroxy-3-oxo-4,6-cyclohexadiene-1-carboxylate, which undergoes rapid aromatization to the final product, 2,3-dihydroxybenzoate (2,3-DHB). Only the compounds with a C3-hydroxyl group such as methyl 2,3-dihydro-2,3-dihydroxybenzoate, methyl-3-hydroxy-1,4-cyclohexadiene-1-carboxylate, trans-3-hydroxy-2-cyclohexene-1-carboxylate, cis-3-hydroxy-4-cyclohexene-1-carboxylate, cis-3-hydroxycyclohexane-1-carboxylic acid are oxidized to the corresponding ketone products. The stereospecificity of the C3 allylic alcohol group oxidation is 3R in a 1R,3R dihydro substrate. It can also increase the DHB-AMP ligase activity of EntE by interaction EntE. {ECO:0000269|PubMed:21166461, ECO:0000269|PubMed:2144454, ECO:0000269|PubMed:2521622}. |
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| b0604 | b0604 | Thiol:disulfide interchange protein DsbG | Periplasm | R_DSBGGT_enzyme R_TDSR2_enzyme |
R_DSBGGT R_TDSR2 |
248 | Secretion: 248.0, Translation: 248.0, Folding: 24.8 | 27,495 | UniprotID: P77202 | FUNCTION: Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro. {ECO:0000269|PubMed:19965429}. |
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| b0029 | b0029 | 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) (EC 1.17.7.4) (1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase) | Cytoplasm | R_DMPPS_enzyme R_IPDPS_enzyme |
R_DMPPS R_IPDPS |
316 | Translation: 316.0, Folding: 31.6 | 34,775 | UniprotID: P62623 ECnumber: EC 1.17.7.4 |
FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis (PubMed:11818558, PubMed:11418107, PubMed:12706830, PubMed:19569147, PubMed:22137895). In vitro, can also hydrate acetylenes to aldehydes and ketones via anti-Markovnikov/Markovnikov addition (PubMed:22948824). {ECO:0000269|PubMed:11418107, ECO:0000269|PubMed:11818558, ECO:0000269|PubMed:12706830, ECO:0000269|PubMed:19569147, ECO:0000269|PubMed:22137895, ECO:0000269|PubMed:22948824}. |
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| b4019 | b4019 | Methionine synthase (EC 2.1.1.13) (5-methyltetrahydrofolate--homocysteine methyltransferase) (Methionine synthase, vitamin-B12-dependent) (MS) | Cytoplasm | R_METS_enzyme | R_METS | 1227 | Translation: 1227.0, Folding: 122.7 | 135,997 | UniprotID: P13009 ECnumber: EC 2.1.1.13 |
FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. | |
| b4014 | b4014 | Malate synthase A (MSA) (EC 2.3.3.9) | Cytoplasm | 533 | Translation: 533.0, Folding: 53.3 | 60,274 | UniprotID: P08997 ECnumber: EC 2.3.3.9 |
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| b4015 | b4015 | Isocitrate lyase (ICL) (EC 4.1.3.1) (Isocitrase) (Isocitratase) | Cytoplasm | 434 | Translation: 434.0, Folding: 43.4 | 47,522 | UniprotID: P0A9G6 ECnumber: EC 4.1.3.1 |
FUNCTION: Involved in the metabolic adaptation in response to environmental changes. Catalyzes the reversible formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle during growth on fatty acid substrates. {ECO:0000269|PubMed:15748982, ECO:0000269|PubMed:3281659, ECO:0000269|PubMed:3291954, ECO:0000269|PubMed:7826335, ECO:0000269|Ref.9}. |
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| b0025 | b0025 | Riboflavin biosynthesis protein RibF [Includes: Riboflavin kinase (EC 2.7.1.26) (Flavokinase); FMN adenylyltransferase (EC 2.7.7.2) (FAD pyrophosphorylase) (FAD synthase) | Cytoplasm | R_FMNAT_enzyme R_RBFK_enzyme |
R_FMNAT R_RBFK |
313 | Translation: 313.0, Folding: 31.3 | 34,734 | UniprotID: P0AG40 ECnumber: EC 2.7.1.26; 2.7.7.2 |
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| b1519 | b1519 | Trans-aconitate 2-methyltransferase (EC 2.1.1.144) | Cytoplasm | R_ACONMT_enzyme | R_ACONMT | 252 | Translation: 252.0, Folding: 25.2 | 29,006 | UniprotID: P76145 ECnumber: EC 2.1.1.144 |
FUNCTION: Catalyzes the S-adenosylmethionine monomethyl esterification of trans-aconitate at high affinity and of cis-aconitate, isocitrate, and citrate at lower velocities and affinities. | |
| b0933 | b0933 | Aliphatic sulfonates import ATP-binding protein SsuB (EC 3.6.3.-) | Cell_inner_membrane | R_BUTSO3abcpp_enzyme R_ETHSO3abcpp_enzyme R_ISETACabcpp_duplicate_2_enzyme R_MSO3abcpp_enzyme R_SULFACabcpp_enzyme |
R_BUTSO3abcpp R_ETHSO3abcpp R_ISETACabcpp_duplicate_2 R_MSO3abcpp R_SULFACabcpp |
255 | Secretion: 255.0, Translation: 255.0, Folding: 25.5 | 27,738 | UniprotID: P0AAI1 ECnumber: EC 3.6.3.- |
FUNCTION: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system (Probable). {ECO:0000305|PubMed:10506196, ECO:0000305|PubMed:10781534}. | |
| b0932 | b0932 | Aminopeptidase N (EC 3.4.11.2) (Alpha-aminoacylpeptide hydrolase) | Cell_inner_membrane | R_AMPTASECG_duplicate_3_enzyme R_AMPTASEPG_duplicate_4_enzyme |
R_AMPTASECG_duplicate_3 R_AMPTASEPG_duplicate_4 |
870 | Secretion: 870.0, Translation: 870.0, Folding: 87.0 | 98,919 | UniprotID: P04825 ECnumber: EC 3.4.11.2 |
FUNCTION: Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation. {ECO:0000269|PubMed:16885166, ECO:0000269|PubMed:18416562, ECO:0000269|PubMed:19622865, ECO:0000305|PubMed:20067529}. | |
| b0931 | b0931 | Nicotinate phosphoribosyltransferase (NAPRTase) (EC 6.3.4.21) | Cytoplasm | R_NAMNPP_enzyme | R_NAMNPP | 400 | Translation: 400.0, Folding: 40.0 | 45,897 | UniprotID: P18133 ECnumber: EC 6.3.4.21 |
FUNCTION: Catalyzes the synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate at the expense of ATP. {ECO:0000255|HAMAP-Rule:MF_00570, ECO:0000269|PubMed:2211655}. | |
| b0930 | b0930 | Asparagine--tRNA ligase (EC 6.1.1.22) (Asparaginyl-tRNA synthetase) (AsnRS) | Cytoplasm | R_ASNTRS_enzyme | R_ASNTRS | 466 | Translation: 466.0, Folding: 46.6 | 52,570 | UniprotID: P0A8M0 ECnumber: EC 6.1.1.22 |
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| b0937 | b0937 | FMN reductase (NADPH) (EC 1.5.1.38) (FMN reductase) (Sulfate starvation-induced protein 4) (SSI4) | Cytoplasm | R_FMNRx_enzyme R_FMNRx2_enzyme |
R_FMNRx R_FMNRx2 |
191 | Translation: 191.0, Folding: 19.1 | 21,253 | UniprotID: P80644 ECnumber: EC 1.5.1.38 |
FUNCTION: Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin. | |
| b0936 | b0936 | Putative aliphatic sulfonates-binding protein | Periplasm | R_BUTSO3abcpp_enzyme R_ETHSO3abcpp_enzyme R_ISETACabcpp_duplicate_2_enzyme R_MSO3abcpp_enzyme R_SULFACabcpp_enzyme |
R_BUTSO3abcpp R_ETHSO3abcpp R_ISETACabcpp_duplicate_2 R_MSO3abcpp R_SULFACabcpp |
319 | Secretion: 319.0, Translation: 319.0, Folding: 31.9 | 34,558 | UniprotID: P75853 | FUNCTION: Part of a binding-protein-dependent transport system for aliphatic sulfonates. Putative binding protein. | |
| b0935 | b0935 | Alkanesulfonate monooxygenase (EC 1.14.14.5) (FMNH2-dependent aliphatic sulfonate monooxygenase) (Sulfate starvation-induced protein 6) (SSI6) | Cytoplasm | R_FDMO_enzyme R_FDMO2_enzyme R_FDMO3_enzyme R_FDMO4_enzyme R_FDMO6_enzyme |
R_FDMO R_FDMO2 R_FDMO3 R_FDMO4 R_FDMO6 |
381 | Translation: 381.0, Folding: 38.1 | 41,736 | UniprotID: P80645 ECnumber: EC 1.14.14.5 |
FUNCTION: Involved in desulfonation of aliphatic sulfonates. Catalyzes the conversion of pentanesulfonic acid to sulfite and pentaldehyde and is able to desulfonate a wide range of sulfonated substrates including C-2 to C-10 unsubstituted linear alkanesulfonates, substituted ethanesulfonic acids and sulfonated buffers. | |
| b0934 | b0934 | Putative aliphatic sulfonates transport permease protein SsuC | Cell_inner_membrane | R_BUTSO3abcpp_enzyme R_ETHSO3abcpp_enzyme R_ISETACabcpp_duplicate_2_enzyme R_MSO3abcpp_enzyme R_SULFACabcpp_enzyme |
R_BUTSO3abcpp R_ETHSO3abcpp R_ISETACabcpp_duplicate_2 R_MSO3abcpp R_SULFACabcpp |
263 | Secretion: 263.0, Translation: 263.0, Folding: 26.3 | 28,925 | UniprotID: P75851 | FUNCTION: Part of a binding-protein-dependent transport system for aliphatic sulfonates. Probably responsible for the translocation of the substrate across the membrane. | |
| b0334 | b0334 | 2-methylcitrate dehydratase (2-MC dehydratase) (EC 4.2.1.79) ((2S,3S)-2-methylcitrate dehydratase) (Aconitate hydratase) (ACN) (Aconitase) (EC 4.2.1.3) | Cytoplasm | R_MCITD_enzyme | R_MCITD | 483 | Translation: 483.0, Folding: 48.3 | 53,952 | UniprotID: P77243 ECnumber: EC 4.2.1.79; 4.2.1.3 |
FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the stereospecific dehydration of (2S,3S)-2-methylcitrate (2-MC) to yield the cis isomer of 2-methyl-aconitate. It is also able to catalyze the dehydration of citrate and the hydration of cis-aconitate at a lower rate. Due to its broad substrate specificity, it seems to be responsible for the residual aconitase activity of the acnAB-null mutant. {ECO:0000269|PubMed:11782506, ECO:0000269|PubMed:12473114}. |
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| b0337 | b0337 | Cytosine deaminase (CD) (CDA) (CDase) (EC 3.5.4.1) (Cytosine aminohydrolase) (Isoguanine deaminase) (EC 3.5.4.-) | Cytoplasm | R_CSND_enzyme | R_CSND | 427 | Translation: 427.0, Folding: 42.7 | 47,591 | UniprotID: P25524 ECnumber: EC 3.5.4.1; 3.5.4.- |
FUNCTION: Catalyzes the hydrolytic deamination of cytosine to uracil. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis. Is also able to catalyze deamination of isoguanine, a mutagenic oxidation product of adenine in DNA, and of isocytosine. To a lesser extent, also catalyzes the conversion of 5-fluorocytosine (5FC) to 5-fluorouracil (5FU); this activity allows the formation of a cytotoxic chemotherapeutic agent from a non-cytotoxic precursor. {ECO:0000269|PubMed:15381761, ECO:0000269|PubMed:21545144, ECO:0000269|PubMed:21604715, ECO:0000269|PubMed:8226944}. |
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| b0336 | b0336 | Cytosine permease | Cell_inner_membrane | R_CSNt2pp_enzyme | R_CSNt2pp | 419 | Secretion: 419.0, Translation: 419.0, Folding: 41.9 | 43,650 | UniprotID: P0AA82 | FUNCTION: Required for cytosine transport into the cell. | |
| b0331 | b0331 | 2-methylisocitrate lyase (2-MIC) (MICL) (EC 4.1.3.30) ((2R,3S)-2-methylisocitrate lyase) | Cytoplasm | R_MCITL2_enzyme | R_MCITL2 | 296 | Translation: 296.0, Folding: 29.6 | 32,135 | UniprotID: P77541 ECnumber: EC 4.1.3.30 |
FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the thermodynamically favored C-C bond cleavage of (2R,3S)-2-methylisocitrate to yield pyruvate and succinate via an alpha-carboxy-carbanion intermediate. {ECO:0000255|HAMAP-Rule:MF_01939, ECO:0000269|PubMed:11422389, ECO:0000269|PubMed:15723538}. | |
| b0333 | b0333 | 2-methylcitrate synthase (2-MCS) (MCS) (EC 2.3.3.5) ((2S,3S)-2-methylcitrate synthase) (Citrate synthase) (EC 2.3.3.16) | Cytoplasm | R_MCITS_enzyme | R_MCITS | 389 | Translation: 389.0, Folding: 38.9 | 43,102 | UniprotID: P31660 ECnumber: EC 2.3.3.5; 2.3.3.16 |
FUNCTION: Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and via the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the Claisen condensation of propionyl-CoA and oxaloacetate (OAA) to yield (2S,3S)-2-methylcitrate (2-MC) and CoA. Also catalyzes the condensation of oxaloacetate with acetyl-CoA to yield citrate but with a lower specificity. {ECO:0000269|PubMed:8508809, ECO:0000269|PubMed:9325432, ECO:0000269|PubMed:9579066}. |
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| b0339 | b0339 | Carbonic anhydrase 1 (EC 4.2.1.1) (Carbonate dehydratase 1) | Cytoplasm | R_HCO3E_duplicate_2_enzyme | R_HCO3E_duplicate_2 | 219 | Translation: 219.0, Folding: 21.9 | 23,764 | UniprotID: P0ABE9 ECnumber: EC 4.2.1.1 |
FUNCTION: Reversible hydration of carbon dioxide. Carbon dioxide formed in the bicarbonate-dependent decomposition of cyanate by cyanase (CynS) diffuses out of the cell faster than it would be hydrated to bicarbonate, so the apparent function of this enzyme is to catalyze the hydration of carbon dioxide and thus prevent depletion of cellular bicarbonate. {ECO:0000269|PubMed:1740425}. | |
| b3028 | b3028 | Modulator of drug activity B | Cytoplasm | R_NADPHQR2_enzyme R_NADPHQR3_enzyme R_NADPHQR4_enzyme |
R_NADPHQR2 R_NADPHQR3 R_NADPHQR4 |
193 | Translation: 193.0, Folding: 19.3 | 21,891 | UniprotID: P0AEY5 | ||
| b3029 | b3029 | Probable quinol monooxygenase YgiN (QuMo) (EC 1.-.-.-) | Cytoplasm | R_QMO2_enzyme R_QMO3_enzyme |
R_QMO2 R_QMO3 |
104 | Translation: 104.0, Folding: 10.4 | 11,532 | UniprotID: P0ADU2 ECnumber: EC 1.-.-.- |
FUNCTION: Can oxidize menadiol to menadione. {ECO:0000269|PubMed:15613473}. | |
| b3591 | b3591 | L-seryl-tRNA(Sec) selenium transferase (EC 2.9.1.1) (Selenocysteine synthase) (Sec synthase) (Selenocysteinyl-tRNA(Sec) synthase) | Cytoplasm | R_SELCYSS_enzyme | R_SELCYSS | 463 | Translation: 463.0, Folding: 46.3 | 50,607 | UniprotID: P0A821 ECnumber: EC 2.9.1.1 |
FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. Requires selenophosphate as the selenium-donor molecule. {ECO:0000269|PubMed:2007584, ECO:0000269|PubMed:2007585}. | |
| b3599 | b3599 | PTS system mannitol-specific EIICBA component (EIICBA-Mtl) (EII-Mtl) [Includes: Mannitol permease IIC component (PTS system mannitol-specific EIIC component); Mannitol-specific phosphotransferase enzyme IIB component (EC 2.7.1.197) (PTS system mannitol-specific EIIB component); Mannitol-specific phosphotransferase enzyme IIA component (EC 2.7.1.197) (PTS system mannitol-specific EIIA component) |
Cell_inner_membrane | R_MNLptspp_enzyme | R_MNLptspp | 637 | Secretion: 637.0, Translation: 637.0, Folding: 63.7 | 67,972 | UniprotID: P00550 ECnumber: EC 2.7.1.197; 2.7.1.197 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in D-mannitol transport (PubMed:368051, PubMed:6427236, PubMed:2123863). Also able to use D-mannonic acid (PubMed:6427236). {ECO:0000269|PubMed:2123863, ECO:0000269|PubMed:368051, ECO:0000269|PubMed:6427236}. |
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| b4032 | b4032 | Maltose transport system permease protein MalG | Cell_inner_membrane | R_14GLUCANabcpp R_MALTHXabcpp R_MALTPTabcpp R_MALTTRabcpp R_MALTTTRabcpp R_MALTabcpp |
296 | Secretion: 296.0, Translation: 296.0, Folding: 29.6 | 32,225 | UniprotID: P68183 | FUNCTION: Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. | ||
| b3114 | b3114 | PFL-like enzyme TdcE (Keto-acid formate acetyltransferase) (Keto-acid formate-lyase) (Ketobutyrate formate-lyase) (KFL) (EC 2.3.1.-) (Pyruvate formate-lyase) (PFL) (EC 2.3.1.54) | Cytoplasm | R_OBTFL_duplicate_3_enzyme R_PFL_duplicate_3_enzyme |
R_OBTFL_duplicate_3 R_PFL_duplicate_3 |
764 | Translation: 764.0, Folding: 76.4 | 85,936 | UniprotID: P42632 ECnumber: EC 2.3.1.-; 2.3.1.54 |
FUNCTION: Catalyzes the cleavage of 2-ketobutyrate to propionyl-CoA and formate. It can also use pyruvate as substrate. {ECO:0000269|PubMed:9484901}. | |
| b3115 | b3115 | Propionate kinase (EC 2.7.2.15) | Cytoplasm | R_ACKr_duplicate_2_enzyme R_PPAKr_enzyme |
R_ACKr_duplicate_2 R_PPAKr |
402 | Translation: 402.0, Folding: 40.2 | 43,384 | UniprotID: P11868 ECnumber: EC 2.7.2.15 |
FUNCTION: Catalyzes the conversion of propionyl phosphate and ADP to propionate and ATP. It can also use acetyl phosphate as phosphate group acceptor. {ECO:0000255|HAMAP-Rule:MF_01881, ECO:0000269|PubMed:9484901}. | |
| b3116 | b3116 | Threonine/serine transporter TdcC (H(+)/threonine-serine symporter) | Cell_inner_membrane | R_SERt2rpp_duplicate_2_enzyme R_THRt2rpp_enzyme |
R_SERt2rpp_duplicate_2 R_THRt2rpp |
443 | Secretion: 443.0, Translation: 443.0, Folding: 44.3 | 48,879 | UniprotID: P0AAD8 | FUNCTION: Involved in the import of threonine and serine into the cell, with the concomitant import of a proton (symport system). {ECO:0000255|HAMAP-Rule:MF_01583, ECO:0000269|PubMed:9498571}. | |
| b3117 | b3117 | L-threonine dehydratase catabolic TdcB (EC 4.3.1.19) (L-serine dehydratase) (EC 4.3.1.17) (Threonine deaminase) | Cytoplasm | R_THRD_L_enzyme | R_THRD_L | 329 | Translation: 329.0, Folding: 32.9 | 35,232 | UniprotID: P0AGF6 ECnumber: EC 4.3.1.19; 4.3.1.17 |
FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. TdcB also dehydrates serine to yield pyruvate via analogous enamine/imine intermediates. {ECO:0000269|PubMed:10388709, ECO:0000269|PubMed:13405870, ECO:0000269|PubMed:15390404}. |
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| b3374 | b3374 | Fructoselysine 6-kinase (EC 2.7.1.218) | Cytoplasm | R_FRULYSK_enzyme | R_FRULYSK | 261 | Translation: 261.0, Folding: 26.1 | 28,332 | UniprotID: P45543 ECnumber: EC 2.7.1.218 |
FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructoselysine to fructoselysine 6-phosphate (PubMed:12147680). Functions in a fructoselysine degradation pathway that allows E.coli to grow on fructoselysine or psicoselysine (PubMed:12147680, PubMed:14641112). To a much lesser extenst, is also able to phosphorylate psicoselysine (PubMed:14641112). {ECO:0000269|PubMed:12147680, ECO:0000269|PubMed:14641112}. |
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| b3370 | b3370 | Probable fructoselysine/psicoselysine transporter FrlA | Cell_inner_membrane | R_FRULYSt2pp_enzyme R_PSCLYSt2pp_enzyme |
R_FRULYSt2pp R_PSCLYSt2pp |
445 | Secretion: 445.0, Translation: 445.0, Folding: 44.5 | 47,577 | UniprotID: P45539 | FUNCTION: Is likely involved in the transport of fructoselysine and psicoselysine to the cytoplasm, where they are degraded. {ECO:0000305|PubMed:12147680, ECO:0000305|PubMed:14641112}. | |
| b3371 | b3371 | Fructoselysine 6-phosphate deglycase (EC 3.5.-.-) | Cytoplasm | R_FRULYSDG_enzyme | R_FRULYSDG | 340 | Translation: 340.0, Folding: 34.0 | 38,569 | UniprotID: P0AC00 ECnumber: EC 3.5.-.- |
FUNCTION: Catalyzes the reversible conversion of fructoselysine 6-phosphate to glucose 6-phosphate and lysine (PubMed:12147680). Functions in a fructoselysine degradation pathway that allows E.coli to grow on fructoselysine or psicoselysine (PubMed:14641112). {ECO:0000269|PubMed:12147680, ECO:0000269|PubMed:14641112}. | |
| b3752 | b3752 | Ribokinase (RK) (EC 2.7.1.15) | Cytoplasm | R_RBK_enzyme | R_RBK | 309 | Translation: 309.0, Folding: 30.9 | 32,291 | UniprotID: P0A9J6 ECnumber: EC 2.7.1.15 |
FUNCTION: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway. {ECO:0000255|HAMAP-Rule:MF_01987, ECO:0000269|PubMed:11563694, ECO:0000269|PubMed:3011794}. | |
| b3201 | b3201 | Lipopolysaccharide export system ATP-binding protein LptB (EC 3.6.3.-) | Cytoplasm | 241 | Translation: 241.0, Folding: 24.1 | 26,801 | UniprotID: P0A9V1 ECnumber: EC 3.6.3.- |
FUNCTION: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system. {ECO:0000269|PubMed:16765569, ECO:0000269|PubMed:17056748, ECO:0000269|PubMed:18424520}. | |||
| b3750 | b3750 | Ribose import permease protein RbsC | Cell_inner_membrane | R_RIBabcpp_enzyme | R_RIBabcpp | 321 | Secretion: 321.0, Translation: 321.0, Folding: 32.1 | 33,452 | UniprotID: P0AGI1 | FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:25533465, ECO:0000269|PubMed:6327617}. | |
| b2378 | b2378 | Lipid A biosynthesis palmitoleoyltransferase (EC 2.3.1.242) (Kdo(2)-lipid IV(A) palmitoleoyltransferase) | Cell_inner_membrane | R_EDTXS3_enzyme | R_EDTXS3 | 306 | Secretion: 306.0, Translation: 306.0, Folding: 30.6 | 35,493 | UniprotID: P0ACV2 ECnumber: EC 2.3.1.242 |
FUNCTION: Catalyzes the transfer of palmitoleate from palmitoleoyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(palmitoleoyl)-lipid IV(A). Required for the biosynthesis of a distinct molecular species of lipid A, which is present only in cells grown at low temperatures. It may confer a selective advantage to cells growing at lower temperatures by making the outer membrane a more effective barrier to harmful chemicals. {ECO:0000269|PubMed:10092655, ECO:0000269|PubMed:11830594}. |
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| b2373 | b2373 | Oxalyl-CoA decarboxylase (EC 4.1.1.8) | Cytoplasm | R_OXCDC_enzyme | R_OXCDC | 564 | Translation: 564.0, Folding: 56.4 | 60,581 | UniprotID: P0AFI0 ECnumber: EC 4.1.1.8 |
FUNCTION: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the decarboxylation of oxalyl-CoA to yield carbon dioxide and formyl-CoA. {ECO:0000269|PubMed:20553497}. | |
| b2374 | b2374 | Formyl-CoA:oxalate CoA-transferase (FCOCT) (EC 2.8.3.16) (Formyl-coenzyme A transferase) (Formyl-CoA transferase) | Cytoplasm | R_FORCT_enzyme | R_FORCT | 416 | Translation: 416.0, Folding: 41.6 | 45,828 | UniprotID: P69902 ECnumber: EC 2.8.3.16 |
FUNCTION: Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl-CoA to oxalate. It can also use succinate as an acceptor. {ECO:0000269|PubMed:12844490, ECO:0000269|PubMed:18245280, ECO:0000269|PubMed:23335415}. | |
| b2153 | b2153 | GTP cyclohydrolase 1 (EC 3.5.4.16) (GTP cyclohydrolase I) (GTP-CH-I) | Cytoplasm | R_GTPCI_enzyme | R_GTPCI | 222 | Translation: 222.0, Folding: 22.2 | 24,831 | UniprotID: P0A6T5 ECnumber: EC 3.5.4.16 |
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| b4219 | b4219 | Peptide methionine sulfoxide reductase MsrA (Protein-methionine-S-oxide reductase) (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (Peptide Met(O) reductase) | Cytoplasm | R_METSOXR1_duplicate_2_enzyme R_METSOXR1_duplicate_3_enzyme |
R_METSOXR1_duplicate_2 R_METSOXR1_duplicate_3 |
212 | Translation: 212.0, Folding: 21.2 | 23,315 | UniprotID: P0A744 ECnumber: EC 1.8.4.11 |
FUNCTION: Could have an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. | |
| b2156 | b2156 | Lysine-specific permease | Cell_inner_membrane | R_LYSt2pp_enzyme | R_LYSt2pp | 489 | Secretion: 489.0, Translation: 489.0, Folding: 48.9 | 53,576 | UniprotID: P25737 | FUNCTION: Permease that is involved in the transport across the cytoplasmic membrane of lysine. | |
| b2155 | b2155 | Colicin I receptor | Cell_outer_membrane | R_FE3DHBZStonex_duplicate_2_enzyme | R_FE3DHBZStonex_duplicate_2 | 663 | Secretion: 663.0, Translation: 663.0, Folding: 66.3 | 73,896 | UniprotID: P17315 | FUNCTION: Not yet known. Postulated to participate in iron transport. Outer membrane receptor for colicins IA and IB. | |
| b2154 | b2154 | S-formylglutathione hydrolase YeiG (FGH) (EC 3.1.2.12) | Cytoplasm | R_SFGTHi_enzyme | R_SFGTHi | 278 | Translation: 278.0, Folding: 27.8 | 31,259 | UniprotID: P33018 ECnumber: EC 3.1.2.12 |
FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids. {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16567800}. | |
| b2407 | b2407 | Purine nucleoside phosphorylase 2 (EC 2.4.2.1) (Inosine-guanosine phosphorylase) (Purine nucleoside phosphorylase II) (PNP II) (Xanthosine phosphorylase) | Cytoplasm | R_PUNP3_enzyme R_PUNP4_enzyme R_PUNP5_enzyme R_PUNP6_enzyme R_PUNP7_enzyme |
R_PUNP3 R_PUNP4 R_PUNP5 R_PUNP6 R_PUNP7 |
277 | Translation: 277.0, Folding: 27.7 | 29,835 | UniprotID: P45563 ECnumber: EC 2.4.2.1 |
FUNCTION: The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. This protein can degrade all purine nucleosides including xanthosine, inosine and guanosine, but cannot cleave adenosine, deoxyadenosine or hypoxanthine arabinoside. Has a preference for the neutral over the monoanionic form of xanthosine. {ECO:0000269|PubMed:15808857, ECO:0000269|PubMed:3042752, ECO:0000269|PubMed:7007808, ECO:0000269|PubMed:7007809}. |
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| b2406 | b2406 | Xanthosine permease (Xanthosine transporter) | Cell_inner_membrane | R_ADNt2pp_copy2 R_CYTDt2pp_copy2 R_INSt2pp_copy2 R_THMDt2pp_copy2 R_URIt2pp_copy2 R_XTSNt2rpp |
418 | Secretion: 418.0, Translation: 418.0, Folding: 41.8 | 46,140 | UniprotID: P45562 | FUNCTION: Uptake of xanthosine. Driven by a proton motive force. Can also transport other nucleosides such as inosine, adenosine, cytidine, uridine and thymidine. {ECO:0000269|PubMed:7559336}. | ||
| b2400 | b2400 | Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase) (GluRS) | Cytoplasm | R_GLUTRS_enzyme | R_GLUTRS | 471 | Translation: 471.0, Folding: 47.1 | 53,816 | UniprotID: P04805 ECnumber: EC 6.1.1.17 |
FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). {ECO:0000269|PubMed:14764088, ECO:0000269|PubMed:6280993, ECO:0000269|PubMed:6986385, ECO:0000269|PubMed:7797500, ECO:0000269|PubMed:8218204}.; FUNCTION: Phosphorylation of GltX by HipA prevents it from being charged, leading to an increase in uncharged tRNA(Glu). This induces amino acid starvation and the stringent response via RelA/SpoT and increased (p)ppGpp levels, which inhibits replication, transcription, translation and cell wall synthesis, reducing growth and leading to multidrug resistance and persistence (PubMed:24095282, PubMed:24343429). Overexpression of GltX prevents HipA-induced growth arrest, persister formation and increases in (p)ppGpp levels (PubMed:24343429, PubMed:28430938). {ECO:0000269|PubMed:24095282, ECO:0000269|PubMed:24343429, ECO:0000269|PubMed:28430938}. |
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| b2979 | b2979 | Glycolate oxidase subunit GlcD | Cytoplasm | R_GLYCTO2_enzyme R_GLYCTO3_enzyme R_GLYCTO4_enzyme |
R_GLYCTO2 R_GLYCTO3 R_GLYCTO4 |
499 | Translation: 499.0, Folding: 49.9 | 53,812 | UniprotID: P0AEP9 | ||
| b2975 | b2975 | Glycolate permease GlcA | Cell_inner_membrane | R_D_LACt2pp_duplicate_2_enzyme R_GLYCLTt2rpp_duplicate_2_enzyme R_L_LACt2rpp_duplicate_2_enzyme |
R_D_LACt2pp_duplicate_2 R_GLYCLTt2rpp_duplicate_2 R_L_LACt2rpp_duplicate_2 |
560 | Secretion: 560.0, Translation: 560.0, Folding: 56.0 | 58,920 | UniprotID: Q46839 | FUNCTION: Transports glycolate across the membrane. Can also transport L-lactate and D-lactate. Seems to be driven by a proton motive force. | |
| b2976 | b2976 | Malate synthase G (MSG) (EC 2.3.3.9) | Cytoplasm | 723 | Translation: 723.0, Folding: 72.3 | 80,489 | UniprotID: P37330 ECnumber: EC 2.3.3.9 |
FUNCTION: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA. {ECO:0000255|HAMAP-Rule:MF_00641, ECO:0000269|PubMed:14336062, ECO:0000269|PubMed:4892366, ECO:0000269|PubMed:7925370}. | |||
| b3974 | b3974 | Pantothenate kinase (EC 2.7.1.33) (Pantothenic acid kinase) (Rts protein) | Cytoplasm | R_PNTK_enzyme | R_PNTK | 316 | Translation: 316.0, Folding: 31.6 | 36,360 | UniprotID: P0A6I3 ECnumber: EC 2.7.1.33 |
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| b2574 | b2574 | L-aspartate oxidase (LASPO) (EC 1.4.3.16) (Quinolinate synthase B) | Cytoplasm | R_ASPO3_enzyme R_ASPO4_enzyme R_ASPO5_enzyme R_ASPO6_enzyme |
R_ASPO3 R_ASPO4 R_ASPO5 R_ASPO6 |
540 | Translation: 540.0, Folding: 54.0 | 60,337 | UniprotID: P10902 ECnumber: EC 1.4.3.16 |
FUNCTION: Catalyzes the oxidation of L-aspartate to iminoaspartate. | |
| b2579 | b2579 | Autonomous glycyl radical cofactor | Cytoplasm | R_OBTFL_duplicate_2_enzyme R_PFL_duplicate_4_enzyme |
R_OBTFL_duplicate_2 R_PFL_duplicate_4 |
127 | Translation: 127.0, Folding: 12.7 | 14,284 | UniprotID: P68066 | FUNCTION: Acts as a radical domain for damaged PFL and possibly other radical proteins. {ECO:0000269|PubMed:11444864}. | |
| b2578 | b2578 | Cysteine/O-acetylserine efflux protein | Cell_inner_membrane | R_ACSERtpp_enzyme R_CYStpp_enzyme |
R_ACSERtpp R_CYStpp |
195 | Secretion: 195.0, Translation: 195.0, Folding: 19.5 | 21,248 | UniprotID: P38101 | FUNCTION: Exporter of O-acetylserine (OAS) and cysteine. {ECO:0000269|PubMed:12562784}. | |
| b3431 | b3431 | Glycogen debranching enzyme (EC 3.2.1.196) (Glycogen operon protein GlgX) (Limit dextrin alpha-1,6-maltotetraose-hydrolase) | Cytoplasm | R_GLDBRAN2_enzyme | R_GLDBRAN2 | 657 | Translation: 657.0, Folding: 65.7 | 73,577 | UniprotID: P15067 ECnumber: EC 3.2.1.196 |
FUNCTION: Removes maltotriose and maltotetraose chains that are attached by 1,6-alpha-linkage to the limit dextrin main chain, generating a debranched limit dextrin. Shows only very little activity with native glycogen. {ECO:0000269|PubMed:15687211, ECO:0000269|PubMed:779849, ECO:0000269|PubMed:8576033}. | |
| b1981 | b1981 | Shikimate transporter | Cell_inner_membrane | R_SKMt2pp_enzyme | R_SKMt2pp | 438 | Secretion: 438.0, Translation: 438.0, Folding: 43.8 | 47,817 | UniprotID: P76350 | ||
| b2947 | b2947 | Glutathione synthetase (EC 6.3.2.3) (GSH synthetase) (GSH-S) (GSHase) (Glutathione synthase) | Cytoplasm | R_GTHS_enzyme | R_GTHS | 316 | Translation: 316.0, Folding: 31.6 | 35,561 | UniprotID: P04425 ECnumber: EC 6.3.2.3 |
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| b2539 | b2539 | 3-phenylpropionate/cinnamic acid dioxygenase subunit beta (EC 1.14.12.19) | Cytoplasm | R_CINNDO_enzyme R_PPPNDO_enzyme |
R_CINNDO R_PPPNDO |
172 | Translation: 172.0, Folding: 17.2 | 20,579 | UniprotID: Q47140 ECnumber: EC 1.14.12.19 |
FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively. {ECO:0000269|PubMed:9603882}. | |
| b2538 | b2538 | 3-phenylpropionate/cinnamic acid dioxygenase subunit alpha (EC 1.14.12.19) | Cytoplasm | R_CINNDO_enzyme R_PPPNDO_enzyme |
R_CINNDO R_PPPNDO |
453 | Translation: 453.0, Folding: 45.3 | 51,109 | UniprotID: P0ABR5 ECnumber: EC 1.14.12.19 |
FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase. Converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively. {ECO:0000269|PubMed:9603882}. | |
| b2889 | b2889 | Isopentenyl-diphosphate Delta-isomerase (IPP isomerase) (EC 5.3.3.2) (IPP:DMAPP isomerase) (Isopentenyl pyrophosphate isomerase) | Cytoplasm | R_IPDDI_enzyme | R_IPDDI | 182 | Translation: 182.0, Folding: 18.2 | 20,508 | UniprotID: Q46822 ECnumber: EC 5.3.3.2 |
FUNCTION: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). {ECO:0000269|PubMed:10099534, ECO:0000269|PubMed:9603997}. | |
| b2883 | b2883 | Guanine deaminase (Guanase) (Guanine aminase) (EC 3.5.4.3) (Guanine aminohydrolase) (GAH) | Cytoplasm | R_GUAD_enzyme | R_GUAD | 439 | Translation: 439.0, Folding: 43.9 | 50,244 | UniprotID: P76641 ECnumber: EC 3.5.4.3 |
FUNCTION: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia. | |
| b2882 | b2882 | Xanthine permease XanQ | Cell_inner_membrane | R_XANt2pp_duplicate_2_enzyme | R_XANt2pp_duplicate_2 | 466 | Secretion: 466.0, Translation: 466.0, Folding: 46.6 | 49,108 | UniprotID: P67444 | FUNCTION: Specific, proton motive force-dependent high-affinity transporter for xanthine. {ECO:0000269|PubMed:16096267}. | |
| b2799 | b2799 | Lactaldehyde reductase (EC 1.1.1.77) (Propanediol oxidoreductase) | Cytoplasm | R_LCARS_enzyme | R_LCARS | 382 | Translation: 382.0, Folding: 38.2 | 40,513 | UniprotID: P0A9S1 ECnumber: EC 1.1.1.77 |
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| b2794 | b2794 | NADPH-dependent 7-cyano-7-deazaguanine reductase (EC 1.7.1.13) (7-cyano-7-carbaguanine reductase) (NADPH-dependent nitrile oxidoreductase) (PreQ(0) reductase) | Cytoplasm | R_CDGR_enzyme | R_CDGR | 282 | Translation: 282.0, Folding: 28.2 | 32,588 | UniprotID: Q46920 ECnumber: EC 1.7.1.13 |
FUNCTION: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1), a late step in the queuosine pathway. Is highly specific for its natural substrate preQ0, since it cannot use various aliphatic, aromatic, benzylic and heterocyclic nitriles, such as acetonitrile, benzonitrile, benzylcyanide and 2-cyanopyrrole, although it can reduce the substrate analog 5-cyanopyrrolo[2,3-d]pyrimidin-4-one with lesser efficiency. {ECO:0000269|PubMed:15767583, ECO:0000269|PubMed:23410922, ECO:0000269|PubMed:23595998}. |
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| b2797 | b2797 | L-serine dehydratase 2 (SDH 2) (EC 4.3.1.17) (L-serine deaminase 2) (L-SD2) | Cytoplasm | R_SERD_L_enzyme | R_SERD_L | 455 | Translation: 455.0, Folding: 45.5 | 48,753 | UniprotID: P30744 ECnumber: EC 4.3.1.17 |
FUNCTION: Deaminates also threonine, particularly when it is present in high concentration. | |
| b2796 | b2796 | Serine transporter | Cell_inner_membrane | R_SERt2rpp_enzyme | R_SERt2rpp | 429 | Secretion: 429.0, Translation: 429.0, Folding: 42.9 | 46,906 | UniprotID: P0AAD6 | FUNCTION: Involved in the import of serine into the cell. May be required for phage C1 adsorption by interacting with DrcB. May also be involved in ampicillin sensitivity. | |
| b2536 | b2536 | Probable 3-phenylpropionic acid transporter | Cell_inner_membrane | R_PPPNt2rpp_enzyme | R_PPPNt2rpp | 379 | Secretion: 379.0, Translation: 379.0, Folding: 37.9 | 41,593 | UniprotID: Q47142 | FUNCTION: Probable permease involved in the uptake of 3-phenylpropionic acid. | |
| b1210 | b1210 | Glutamyl-tRNA reductase (GluTR) (EC 1.2.1.70) | Cytoplasm | R_GLUTRR_enzyme | R_GLUTRR | 418 | Translation: 418.0, Folding: 41.8 | 46,307 | UniprotID: P0A6X1 ECnumber: EC 1.2.1.70 |
FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA. {ECO:0000269|PubMed:12370189, ECO:0000269|PubMed:1569081}. | |
| b1215 | b1215 | 2-dehydro-3-deoxyphosphooctonate aldolase (EC 2.5.1.55) (3-deoxy-D-manno-octulosonic acid 8-phosphate synthase) (KDO-8-phosphate synthase) (KDO 8-P synthase) (KDOPS) (Phospho-2-dehydro-3-deoxyoctonate aldolase) | Cytoplasm | R_KDOPS_enzyme | R_KDOPS | 284 | Translation: 284.0, Folding: 28.4 | 30,833 | UniprotID: P0A715 ECnumber: EC 2.5.1.55 |
FUNCTION: Synthesis of KDO 8-P which is required for lipid A maturation and cellular growth. | |
| b1216 | b1216 | Sodium-potassium/proton antiporter ChaA (Na(+)/H(+) exchanger) | Cell_inner_membrane | R_CA2t3pp_enzyme R_Kt3pp_duplicate_2_enzyme R_NAt3pp_duplicate_2_enzyme |
R_CA2t3pp R_Kt3pp_duplicate_2 R_NAt3pp_duplicate_2 |
366 | Secretion: 366.0, Translation: 366.0, Folding: 36.6 | 39,168 | UniprotID: P31801 | FUNCTION: Sodium exporter that functions mainly at alkaline pH. Can also function as a potassium/proton and calcium/proton antiporter at alkaline pH. Does not play a major role in calcium export. {ECO:0000269|PubMed:16687400, ECO:0000269|PubMed:18342619, ECO:0000269|PubMed:8021217, ECO:0000269|PubMed:8496184, ECO:0000269|PubMed:9518629}. | |
| b1189 | b1189 | D-amino acid dehydrogenase (EC 1.4.99.-) (D-alanine dehydrogenase) | Cell_inner_membrane | R_DAAD_enzyme | R_DAAD | 432 | Secretion: 432.0, Translation: 432.0, Folding: 43.2 | 47,607 | UniprotID: P0A6J5 ECnumber: EC 1.4.99.- |
FUNCTION: Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D-serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. {ECO:0000269|PubMed:13292, ECO:0000269|PubMed:15358424}. |
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| b1185 | b1185 | Disulfide bond formation protein B (Disulfide oxidoreductase) | Cell_inner_membrane | R_DSBAO1_enzyme R_DSBAO2_enzyme |
R_DSBAO1 R_DSBAO2 |
176 | Secretion: 176.0, Translation: 176.0, Folding: 17.6 | 20,142 | UniprotID: P0A6M2 | FUNCTION: Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by oxidizing the DsbA protein. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. {ECO:0000269|PubMed:22267510, ECO:0000269|PubMed:7688471, ECO:0000269|PubMed:8430071}. |
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| b1186 | b1186 | Na(+)/H(+) antiporter NhaB (Sodium/proton antiporter NhaB) | Cell_inner_membrane | R_NAt3_1p5pp_enzyme | R_NAt3_1p5pp | 513 | Secretion: 513.0, Translation: 513.0, Folding: 51.3 | 56,728 | UniprotID: P0AFA7 | FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Catalyzes the exchange of 3 H(+) per 2 Na(+). Has a high affinity for sodium, but can also transport lithium. Activity is weakly pH-dependent. Essential for regulation of intracellular pH under alkaline conditions. {ECO:0000269|PubMed:7822245, ECO:0000269|PubMed:7929345, ECO:0000269|PubMed:8019504, ECO:0000269|PubMed:8093613}. |
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| b0854 | b0854 | Putrescine-binding periplasmic protein | Periplasm | R_PTRCabcpp_duplicate_2_enzyme | R_PTRCabcpp_duplicate_2 | 370 | Secretion: 370.0, Translation: 370.0, Folding: 37.0 | 40,840 | UniprotID: P31133 | FUNCTION: Required for the activity of the bacterial periplasmic transport system of putrescine. Polyamine binding protein. {ECO:0000269|PubMed:8416922}. | |
| b0855 | b0855 | Putrescine transport ATP-binding protein PotG | Cell_inner_membrane | R_PTRCabcpp_duplicate_2_enzyme | R_PTRCabcpp_duplicate_2 | 377 | Secretion: 377.0, Translation: 377.0, Folding: 37.7 | 41,931 | UniprotID: P31134 | FUNCTION: Part of the binding-protein-dependent transport system for putrescine. Probably responsible for energy coupling to the transport system. | |
| b0856 | b0856 | Putrescine transport system permease protein PotH | Cell_inner_membrane | R_PTRCabcpp_duplicate_2_enzyme | R_PTRCabcpp_duplicate_2 | 317 | Secretion: 317.0, Translation: 317.0, Folding: 31.7 | 35,490 | UniprotID: P31135 | FUNCTION: Required for the activity of the bacterial periplasmic transport system of putrescine. | |
| b0857 | b0857 | Putrescine transport system permease protein PotI | Cell_inner_membrane | R_PTRCabcpp_duplicate_2_enzyme | R_PTRCabcpp_duplicate_2 | 281 | Secretion: 281.0, Translation: 281.0, Folding: 28.1 | 30,541 | UniprotID: P0AFL1 | FUNCTION: Required for the activity of the bacterial periplasmic transport system of putrescine. | |
| b1852 | b1852 | Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) [Cleaved into: Extracellular death factor (EDF) | Cytoplasm | 491 | Translation: 491.0, Folding: 49.1 | 55,704 | UniprotID: P0AC53 ECnumber: EC 1.1.1.49 |
FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:15113569, ECO:0000269|PubMed:17962566}.; FUNCTION: Probable source of extracellular death factor (EDF, sequence Asn-Asn-Trp-Asn-Asn, NNWNN) following processing and amidation. This pentapeptide stimulates cell death mediated by MazF (PubMed:17962566). Artificial peptides with altered sequence show that NNGNN, GNWNG and NWN no longer stimulate MazFs endoribonuclease activity; other peptides (NNGN, GNWMM, NNWNG, NNNWNNN) retain MazF-stimulating activity. NNWNN, NNGN, GNWMM and NNWNG prevent cognate antitoxin MazE from inhibiting MazF; although NNNWNNN stimulates MazF it does not do so in the presence of MazE. EDF also stimulates ChpBs endoribonuclease activity in vitro; in this case NWN partially stimulates ChpB, whereas NNGNN, GNWNN, NNWNG, GNWNG and NNNWNNN do not. Only the wild-type EDF peptide prevents cognate antitoxin ChpS from inhibiting ChpB (PubMed:21419338). {ECO:0000269|PubMed:17962566, ECO:0000269|PubMed:21419338}. |
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| b1851 | b1851 | Phosphogluconate dehydratase (EC 4.2.1.12) (6-phosphogluconate dehydratase) (Entner-Doudoroff dehydrase) | Cytoplasm | R_EDD_enzyme | R_EDD | 603 | Translation: 603.0, Folding: 60.3 | 64,639 | UniprotID: P0ADF6 ECnumber: EC 4.2.1.12 |
FUNCTION: Catalyzes the dehydration of 6-phospho-D-gluconate to 2-dehydro-3-deoxy-6-phospho-D-gluconate. {ECO:0000255|HAMAP-Rule:MF_02094, ECO:0000269|PubMed:17102132, ECO:0000269|PubMed:1846355}. | |
| b1850 | b1850 | KHG/KDPG aldolase [Includes: 4-hydroxy-2-oxoglutarate aldolase (EC 4.1.3.16) (2-keto-4-hydroxyglutarate aldolase) (KHG-aldolase); 2-dehydro-3-deoxy-phosphogluconate aldolase (EC 4.1.2.14) (2-keto-3-deoxy-6-phosphogluconate aldolase) (KDPG-aldolase) (Phospho-2-dehydro-3-deoxygluconate aldolase) (Phospho-2-keto-3-deoxygluconate aldolase) | Cytoplasm | R_EDA_enzyme R_OAADC_enzyme |
R_EDA R_OAADC |
213 | Translation: 213.0, Folding: 21.3 | 22,284 | UniprotID: P0A955 ECnumber: EC 4.1.3.16; 4.1.2.14 |
FUNCTION: Involved in the degradation of glucose via the Entner-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-Keto-3-deoxy-6-phosphogluconate (KDPG) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with si-facial selectivity. It accepts some nucleophiles other than pyruvate, including 2-oxobutanoate, phenylpyruvate, and fluorobutanoate. It has a preference for the S-configuration at C2 of the electrophile. {ECO:0000269|PubMed:1339418, ECO:0000269|PubMed:17981470}. |
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| b1857 | b1857 | High-affinity zinc uptake system protein ZnuA | Periplasm | R_ZNabcpp_enzyme | R_ZNabcpp | 310 | Secretion: 310.0, Translation: 310.0, Folding: 31.0 | 33,777 | UniprotID: P39172 | FUNCTION: Involved in the high-affinity zinc uptake transport system. | |
| b1679 | b1679 | Cysteine desulfuration protein SufE | Cytoplasm | R_S2FE2SR_enzyme R_S2FE2SS_enzyme R_S2FE2SS2_enzyme R_SCYSDS_enzyme |
R_S2FE2SR R_S2FE2SS R_S2FE2SS2 R_SCYSDS |
138 | Translation: 138.0, Folding: 13.8 | 15,800 | UniprotID: P76194 | FUNCTION: Participates in cysteine desulfuration mediated by SufS. Cysteine desulfuration mobilizes sulfur from L-cysteine to yield L-alanine and constitutes an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Functions as a sulfur acceptor for SufS, by mediating the direct transfer of the sulfur atom from the S-sulfanylcysteine of SufS, an intermediate product of cysteine desulfuration process. Together with the SufBCD complex, it thereby enhances up to 50-fold, the cysteine desulfurase activity of SufS. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Does not affect the selenocysteine lyase activity of SufS. {ECO:0000269|PubMed:12876288, ECO:0000269|PubMed:12941942, ECO:0000269|PubMed:14644425}. |
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| b1854 | b1854 | Pyruvate kinase II (EC 2.7.1.40) (PK-2) | Cytoplasm | R_PYK_enzyme | R_PYK | 480 | Translation: 480.0, Folding: 48.0 | 51,357 | UniprotID: P21599 ECnumber: EC 2.7.1.40 |
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| b1677 | b1677 | Major outer membrane prolipoprotein Lpp [Cleaved into: Major outer membrane lipoprotein Lpp (Braun lipoprotein) (Murein-lipoprotein) | Cell_outer_membrane | R_ALPATE160pp_enzyme R_ALPATG160pp_enzyme |
R_ALPATE160pp R_ALPATG160pp |
78 | Secretion: 78.0, Translation: 78.0, Folding: 7.8 | 8,323 | UniprotID: P69776 | FUNCTION: Interacts with the peptidoglycan both covalently and noncovalently. This interaction contributes to the maintenance of the structural and functional integrity of the cell envelope. | |
| b1676 | b1676 | Pyruvate kinase I (EC 2.7.1.40) (PK-1) | Cytoplasm | R_PYK_duplicate_2_enzyme | R_PYK_duplicate_2 | 470 | Translation: 470.0, Folding: 47.0 | 50,729 | UniprotID: P0AD61 ECnumber: EC 2.7.1.40 |
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| b1859 | b1859 | High-affinity zinc uptake system membrane protein ZnuB | Cell_inner_membrane | R_ZNabcpp_enzyme | R_ZNabcpp | 261 | Secretion: 261.0, Translation: 261.0, Folding: 26.1 | 27,729 | UniprotID: P39832 | FUNCTION: Involved in the high-affinity zinc uptake transport system. | |
| b1858 | b1858 | Zinc import ATP-binding protein ZnuC (EC 3.6.3.-) | Cell_inner_membrane | R_ZNabcpp_enzyme | R_ZNabcpp | 251 | Secretion: 251.0, Translation: 251.0, Folding: 25.1 | 27,867 | UniprotID: P0A9X1 ECnumber: EC 3.6.3.- |
FUNCTION: Part of the ABC transporter complex ZnuABC involved in zinc import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01725, ECO:0000269|PubMed:9680209}. | |
| b1325 | b1325 | L-Ala-D/L-Glu epimerase (AE epimerase) (AEE) (EC 5.1.1.20) | Cytoplasm | R_ALAGLUE_enzyme | R_ALAGLUE | 321 | Translation: 321.0, Folding: 32.1 | 34,674 | UniprotID: P51981 ECnumber: EC 5.1.1.20 |
FUNCTION: Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has a role in the recycling of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of all the L-Ala-X dipeptides, except L-Ala-L-Arg, L-Ala-L-Lys and L-Ala-L-Pro. Is also active with L-Gly-L-Glu, L-Phe-L-Glu, and L-Ser-L-Glu, but not with L-Glu-L-Glu, L-Lys-L-Glu, L-Pro-L-Glu, L-Lys-L-Ala, or D-Ala-D-Ala. {ECO:0000269|PubMed:11747447, ECO:0000269|PubMed:18535144}. |
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| b1326 | b1326 | Protein MpaA | Cytoplasm | R_LADGMDH_enzyme | R_LADGMDH | 242 | Translation: 242.0, Folding: 24.2 | 26,558 | UniprotID: P0ACV6 | ||
| b1453 | b1453 | L-asparagine permease (L-asparagine transport protein) | Cell_inner_membrane | R_ASNt2rpp_enzyme | R_ASNt2rpp | 499 | Secretion: 499.0, Translation: 499.0, Folding: 49.9 | 54,233 | UniprotID: P77610 | ||
| b0109 | b0109 | Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) (Quinolinate phosphoribosyltransferase [decarboxylating]) (QAPRTase) | Cytoplasm | R_NNDPR_enzyme | R_NNDPR | 297 | Translation: 297.0, Folding: 29.7 | 32,762 | UniprotID: P30011 ECnumber: EC 2.4.2.19 |
FUNCTION: Involved in the catabolism of quinolinic acid (QA). {ECO:0000250}. | |
| b0104 | b0104 | GMP reductase (EC 1.7.1.7) (Guanosine 5-monophosphate oxidoreductase) (Guanosine monophosphate reductase) | Cytoplasm | R_GMPR_enzyme | R_GMPR | 347 | Translation: 347.0, Folding: 34.7 | 37,384 | UniprotID: P60560 ECnumber: EC 1.7.1.7 |
FUNCTION: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. | |
| b1329 | b1329 | Periplasmic murein peptide-binding protein | Periplasm | R_3PEPTabcpp_enzyme | R_3PEPTabcpp | 537 | Secretion: 537.0, Translation: 537.0, Folding: 53.7 | 59,900 | UniprotID: P77348 | FUNCTION: Essential for the uptake of the murein peptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate. Also transports some alpha-linked peptides such as Pro-Phe-Lys with low affinity. The transport is effected by the oligopeptide permease system. | |
| b0103 | b0103 | Dephospho-CoA kinase (EC 2.7.1.24) (Dephosphocoenzyme A kinase) | Cytoplasm | R_DPCOAK_enzyme | R_DPCOAK | 206 | Translation: 206.0, Folding: 20.6 | 22,622 | UniprotID: P0A6I9 ECnumber: EC 2.7.1.24 |
FUNCTION: Catalyzes the phosphorylation of the 3-hydroxyl group of dephosphocoenzyme A to form coenzyme A. | |
| b4481 | b4481 | TDP-N-acetylfucosamine:lipid II N-acetylfucosaminyltransferase (EC 2.4.1.325) (4-alpha-L-fucosyltransferase) (TDP-Fuc4NAc:lipid II Fuc4NAc transferase) (Fuc4NAc transferase) | Cell_inner_membrane | R_AADDGT_enzyme | R_AADDGT | 359 | Secretion: 359.0, Translation: 359.0, Folding: 35.9 | 40,640 | UniprotID: P56258 ECnumber: EC 2.4.1.325 |
FUNCTION: Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (Lipid III), the third lipid-linked intermediate involved in ECA synthesis. {ECO:0000269|PubMed:11673418}. | |
| b1693 | b1693 | 3-dehydroquinate dehydratase (3-dehydroquinase) (EC 4.2.1.10) (Type I DHQase) (Type I dehydroquinase) (DHQ1) | Cytoplasm | R_DHQTi_enzyme | R_DHQTi | 252 | Translation: 252.0, Folding: 25.2 | 27,467 | UniprotID: P05194 ECnumber: EC 4.2.1.10 |
FUNCTION: Involved in the third step of the chorismate pathway, which leads to the biosynthesis of aromatic amino acids (AroAA). Catalyzes the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the first double bond of the aromatic ring to yield 3-dehydroshikimate. The reaction involves the formation of an imine intermediate between the keto group of 3-dehydroquinate and the epsylon-amino group of a lys-170 at the active site. {ECO:0000255|HAMAP-Rule:MF_00214, ECO:0000269|PubMed:13198937, ECO:0000269|PubMed:2950851, ECO:0000269|PubMed:3541912, ECO:0000269|PubMed:7592767}. |
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| b4245 | b4245 | Aspartate carbamoyltransferase catalytic subunit (EC 2.1.3.2) (Aspartate transcarbamylase) (ATCase) | Cytoplasm | R_ASPCT_enzyme R_ASPCT_duplicate_2_enzyme |
R_ASPCT R_ASPCT_duplicate_2 |
311 | Translation: 311.0, Folding: 31.1 | 34,427 | UniprotID: P0A786 ECnumber: EC 2.1.3.2 |
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| b4244 | b4244 | Aspartate carbamoyltransferase regulatory chain | Cytoplasm | R_ASPCT_enzyme | R_ASPCT | 153 | Translation: 153.0, Folding: 15.3 | 17,121 | UniprotID: P0A7F3 | FUNCTION: Involved in allosteric regulation of aspartate carbamoyltransferase. | |
| b4240 | b4240 | PTS system trehalose-specific EIIBC component (EIIBC-Tre) (EII-Tre) [Includes: Trehalose-specific phosphotransferase enzyme IIB component (EC 2.7.1.201) (PTS system trehalose-specific EIIB component); Trehalose permease IIC component (PTS system trehalose-specific EIIC component) | Cell_inner_membrane | R_TREptspp_enzyme | R_TREptspp | 473 | Secretion: 473.0, Translation: 473.0, Folding: 47.3 | 51,081 | UniprotID: P36672 ECnumber: EC 2.7.1.201 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in trehalose transport at low osmolarity. {ECO:0000269|PubMed:2160944, ECO:0000305|PubMed:7608078}. | |
| b4242 | b4242 | Magnesium-transporting ATPase, P-type 1 (EC 3.6.3.2) (Mg(2+) transport ATPase, P-type 1) | Cell_inner_membrane | R_MG2uabcpp_enzyme R_NI2uabcpp_duplicate_2_enzyme |
R_MG2uabcpp R_NI2uabcpp_duplicate_2 |
898 | Secretion: 898.0, Translation: 898.0, Folding: 89.8 | 99,466 | UniprotID: P0ABB8 ECnumber: EC 3.6.3.2 |
FUNCTION: Mediates magnesium influx to the cytosol. | |
| b0583 | b0583 | Enterobactin synthase component D (4-phosphopantetheinyl transferase EntD) (EC 2.7.8.-) (Enterochelin synthase D) | Cell_inner_membrane | R_ENTCS_enzyme | R_ENTCS | 206 | Secretion: 206.0, Translation: 206.0, Folding: 20.6 | 23,259 | UniprotID: P19925 ECnumber: EC 2.7.8.- |
FUNCTION: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively. {ECO:0000269|PubMed:8939709, ECO:0000269|PubMed:9214294, ECO:0000269|PubMed:9485415}. |
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| b0586 | b0586 | Enterobactin synthase component F (EC 2.7.7.-) (Enterochelin synthase F) (Serine-activating enzyme) (Seryl-AMP ligase) | Cytoplasm | R_SERASr_enzyme | R_SERASr | 1293 | Translation: 1293.0, Folding: 129.3 | 141,991 | UniprotID: P11454 ECnumber: EC 2.7.7.- |
FUNCTION: Activates the carboxylate group of L-serine via ATP-dependent PPi exchange reactions to the aminoacyladenylate, preparing that molecule for the final stages of enterobactin synthesis. Holo-EntF acts as the catalyst for the formation of the three amide and three ester bonds present in the cyclic (2,3-dihydroxybenzoyl)serine trimer enterobactin, using seryladenylate and acyl-holo-EntB (acylated with 2,3-dihydroxybenzoate by EntE). |
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| b0584 | b0584 | Ferrienterobactin receptor (Enterobactin outer-membrane receptor) | Cell_outer_membrane | R_FEENTERtonex_enzyme | R_FEENTERtonex | 746 | Secretion: 746.0, Translation: 746.0, Folding: 74.6 | 82,107 | UniprotID: P05825 | FUNCTION: This protein is involved in the initial step of iron uptake by binding ferrienterobactin (Fe-ENT), an iron chelatin siderophore that allows E.coli to extract iron from the environment. FepA also acts as a receptor for colicins B and D. | |
| b0585 | b0585 | Enterochelin esterase (Ferric enterobactin esterase) | Cytoplasm | R_ENTERES_enzyme R_ENTERES2_enzyme |
R_ENTERES R_ENTERES2 |
400 | Translation: 400.0, Folding: 40.0 | 45,652 | UniprotID: P13039 | FUNCTION: Upon internalization, ferric enterobactin is processed via an exquisitely specific pathway that is dependent on FES activity, making iron available for metabolic use. | |
| b0588 | b0588 | Ferric enterobactin transport ATP-binding protein FepC | Cell_inner_membrane | R_FE3DHBZSabcpp_enzyme R_FEENTERabcpp_enzyme |
R_FE3DHBZSabcpp R_FEENTERabcpp |
271 | Secretion: 271.0, Translation: 271.0, Folding: 27.1 | 29,784 | UniprotID: P23878 | FUNCTION: Part of the binding-protein-dependent transport system for ferric enterobactin. Probably responsible for energy coupling to the transport system. | |
| b0589 | b0589 | Ferric enterobactin transport system permease protein FepG | Cell_inner_membrane | R_FE3DHBZSabcpp_enzyme R_FEENTERabcpp_enzyme |
R_FE3DHBZSabcpp R_FEENTERabcpp |
330 | Secretion: 330.0, Translation: 330.0, Folding: 33.0 | 34,910 | UniprotID: P23877 | FUNCTION: Part of the binding-protein-dependent transport system for ferric enterobactin. Probably responsible for the translocation of the substrate across the membrane. | |
| b0612 | b0612 | Citrate/succinate antiporter (Citrate carrier) (Citrate transporter) | Cell_inner_membrane | R_CITt7pp_enzyme | R_CITt7pp | 487 | Secretion: 487.0, Translation: 487.0, Folding: 48.7 | 53,093 | UniprotID: P0AE74 | FUNCTION: Responsible for the uptake of citrate in exchange with the efflux of succinate, fumarate or tartrate. Has a relatively broad specificity for C(4)-dicarboxylates and tricarboxylates (PubMed:9696764). {ECO:0000269|PubMed:9696764}. | |
| b0613 | b0613 | 2-(5-triphosphoribosyl)-3-dephosphocoenzyme-A synthase (2-(5-triphosphoribosyl)-3-dephospho-CoA synthase) (EC 2.4.2.52) | Cytoplasm | R_TPRDCOAS_enzyme | R_TPRDCOAS | 292 | Translation: 292.0, Folding: 29.2 | 31,644 | UniprotID: P77231 ECnumber: EC 2.4.2.52 |
FUNCTION: Catalyzes the formation of 2-(5-triphosphoribosyl)-3-dephosphocoenzyme-A, the precursor of the prosthetic group of the holo-acyl carrier protein (gamma chain) of citrate lyase, from ATP and dephospho-CoA. {ECO:0000269|PubMed:10924139, ECO:0000269|PubMed:11042274}. | |
| b0616 | b0616 | Citrate lyase subunit beta (Citrase beta chain) (EC 4.1.3.6) (Citrate (pro-3S)-lyase subunit beta) (Citryl-CoA lyase subunit) (EC 4.1.3.34) | Cytoplasm | R_CITL_enzyme | R_CITL | 302 | Translation: 302.0, Folding: 30.2 | 33,110 | UniprotID: P0A9I1 ECnumber: EC 4.1.3.6; 4.1.3.34 |
FUNCTION: Represents a citryl-ACP lyase. {ECO:0000250}. | |
| b0617 | b0617 | Citrate lyase acyl carrier protein (Citrate lyase gamma chain) | Cytoplasm | R_CITL_enzyme | R_CITL | 98 | Translation: 98.0, Folding: 9.8 | 10,689 | UniprotID: P69330 | FUNCTION: Covalent carrier of the coenzyme of citrate lyase. | |
| b0614 | b0614 | Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase (EC 2.7.7.61) (Apo-ACP nucleodityltransferase) (Holo-ACP synthase) (Holo-citrate lyase synthase) | Cytoplasm | R_CITL_enzyme | R_CITL | 183 | Translation: 183.0, Folding: 18.3 | 20,270 | UniprotID: P0A6G5 ECnumber: EC 2.7.7.61 |
FUNCTION: Transfers 2-(5-triphosphoribosyl)-3-dephosphocoenzyme-A on a serine residue to the apo-acyl carrier protein (gamma chain) of the citrate lyase to yield holo-acyl carrier protein. {ECO:0000269|PubMed:10924139, ECO:0000269|PubMed:11042274}. | |
| b0615 | b0615 | Citrate lyase alpha chain (Citrase alpha chain) (EC 4.1.3.6) (Citrate (pro-3S)-lyase alpha chain) (Citrate CoA-transferase subunit) (EC 2.8.3.10) | Cytoplasm | R_CITL_enzyme | R_CITL | 510 | Translation: 510.0, Folding: 51.0 | 55,173 | UniprotID: P75726 ECnumber: EC 4.1.3.6; 2.8.3.10 |
FUNCTION: Represents a citrate:acetyl-ACP transferase. {ECO:0000250}. | |
| b0446 | b0446 | HMP-PP phosphatase (EC 3.6.1.-) | Cytoplasm | R_2MAHMP_enzyme R_PYDXPP_duplicate_2_enzyme |
R_2MAHMP R_PYDXPP_duplicate_2 |
272 | Translation: 272.0, Folding: 27.2 | 30,371 | UniprotID: P46891 ECnumber: EC 3.6.1.- |
FUNCTION: Catalyzes the hydrolysis of 4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate (HMP-P). Can also hydrolyze other substrates such as MeO-HMP-PP and 4-amino-2-trifluoromethyl 5-hydroxymethylpyrimidine pyrophosphate (CF3-HMP-PP) to give MeO-HMP-P and 4-amino-2-trifluoromethyl-5-hydroxymethylpyrimidine phosphate. This hydrolysis generates resistance to the antibiotics (bacimethrin, CF3-HMP) by reducing the formation of their toxic forms, 2-methoxythiamin pyrophosphate (MeO-TPP) and CF3-HMP-PP. Also hydrolyzes pyridoxal-phosphate (PLP) and flavin mononucleotide (FMN), and purines (GMP and IMP) as secondary substrates. {ECO:0000255|HAMAP-Rule:MF_01847, ECO:0000269|PubMed:15292217, ECO:0000269|PubMed:16990279}. |
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| b1656 | b1656 | Superoxide dismutase [Fe] (EC 1.15.1.1) | Cytoplasm | R_SPODM_duplicate_2_enzyme | R_SPODM_duplicate_2 | 193 | Translation: 193.0, Folding: 19.3 | 21,266 | UniprotID: P0AGD3 ECnumber: EC 1.15.1.1 |
FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | |
| b4069 | b4069 | Acetyl-coenzyme A synthetase (AcCoA synthetase) (Acs) (EC 6.2.1.1) (Acetate--CoA ligase) (Acyl-activating enzyme) | Cytoplasm | R_ACCOAL_enzyme R_ACS_enzyme |
R_ACCOAL R_ACS |
652 | Translation: 652.0, Folding: 65.2 | 72,094 | UniprotID: P27550 ECnumber: EC 6.2.1.1 |
FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. Acs undergoes a two-step reaction. In the first half reaction, Acs combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA.; FUNCTION: Enables the cell to use acetate during aerobic growth to generate energy via the TCA cycle, and biosynthetic compounds via the glyoxylate shunt. Acetylates CheY, the response regulator involved in flagellar movement and chemotaxis. |
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| b1521 | b1521 | Altronate oxidoreductase (EC 1.1.1.58) (Tagaturonate dehydrogenase) (Tagaturonate reductase) | Cytoplasm | R_TAGURr_enzyme | R_TAGURr | 483 | Translation: 483.0, Folding: 48.3 | 54,808 | UniprotID: P0A6L7 ECnumber: EC 1.1.1.58 |
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| b1525 | b1525 | Succinate semialdehyde dehydrogenase [NAD(P)+] Sad (SSADH) (SSDH) (EC 1.2.1.16) | Cytoplasm | R_SSALx_enzyme R_SSALy_duplicate_2_enzyme |
R_SSALx R_SSALy_duplicate_2 |
462 | Translation: 462.0, Folding: 46.2 | 49,718 | UniprotID: P76149 ECnumber: EC 1.2.1.16 |
FUNCTION: Catalyzes the NAD(+)-dependent oxidation of succinate semialdehyde to succinate. It acts preferentially with NAD as cosubstrate but can also use NADP. Prevents the toxic accumulation of succinate semialdehyde (SSA) and plays an important role when arginine and putrescine are used as the sole nitrogen or carbon sources. {ECO:0000269|PubMed:17873044, ECO:0000269|PubMed:20639325, ECO:0000269|PubMed:7009588, ECO:0000269|PubMed:7011797}. |
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| b1524 | b1524 | Glutaminase 2 (EC 3.5.1.2) | Cytoplasm | R_GLUN_duplicate_3_enzyme | R_GLUN_duplicate_3 | 308 | Translation: 308.0, Folding: 30.8 | 33,516 | UniprotID: P0A6W0 ECnumber: EC 3.5.1.2 |
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| b0032 | b0032 | Carbamoyl-phosphate synthase small chain (EC 6.3.5.5) (Carbamoyl-phosphate synthetase glutamine chain) | Cytoplasm | R_CBPS_enzyme | R_CBPS | 382 | Translation: 382.0, Folding: 38.2 | 41,431 | UniprotID: P0A6F1 ECnumber: EC 6.3.5.5 |
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| b0033 | b0033 | Carbamoyl-phosphate synthase large chain (EC 6.3.5.5) (Carbamoyl-phosphate synthetase ammonia chain) | Cytoplasm | R_CBPS_enzyme | R_CBPS | 1073 | Translation: 1073.0, Folding: 107.3 | 117,842 | UniprotID: P00968 ECnumber: EC 6.3.5.5 |
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| b0030 | b0030 | Non-specific ribonucleoside hydrolase RihC (EC 3.2.-.-) (Purine/pyrimidine ribonucleoside hydrolase) | Cytoplasm | R_ADNUC_enzyme R_CYTDH_duplicate_3_enzyme R_INSH_enzyme R_URIH_duplicate_3_enzyme R_XTSNH_enzyme |
R_ADNUC R_CYTDH_duplicate_3 R_INSH R_URIH_duplicate_3 R_XTSNH |
304 | Translation: 304.0, Folding: 30.4 | 32,561 | UniprotID: P22564 ECnumber: EC 3.2.-.- |
FUNCTION: Hydrolyzes both purine and pyrimidine ribonucleosides with a broad-substrate specificity with decreasing activity in the order uridine, xanthosine, inosine, adenosine, cytidine, guanosine. | |
| b0031 | b0031 | 4-hydroxy-tetrahydrodipicolinate reductase (HTPA reductase) (EC 1.17.1.8) | Cytoplasm | R_DHDPRy_enzyme | R_DHDPRy | 273 | Translation: 273.0, Folding: 27.3 | 28,757 | UniprotID: P04036 ECnumber: EC 1.17.1.8 |
FUNCTION: Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. Can use both NADH and NADPH as a reductant, with NADH being twice as effective as NADPH. {ECO:0000255|HAMAP-Rule:MF_00102, ECO:0000269|PubMed:20503968, ECO:0000269|PubMed:7893644}. | |
| b0036 | b0036 | Carnitinyl-CoA dehydratase (EC 4.2.1.149) (Crotonobetainyl-CoA hydratase) | Cytoplasm | R_CRNCAR_enzyme R_CRNCDH_enzyme |
R_CRNCAR R_CRNCDH |
261 | Translation: 261.0, Folding: 26.1 | 28,190 | UniprotID: P31551 ECnumber: EC 4.2.1.149 |
FUNCTION: Catalyzes the reversible dehydration of L-carnitinyl-CoA to crotonobetainyl-CoA. {ECO:0000269|PubMed:11551212}. | |
| b0037 | b0037 | Probable crotonobetaine/carnitine-CoA ligase (EC 6.2.1.-) | Cytoplasm | R_CRNCAL2_enzyme R_CRNDCAL2_enzyme R_CTBTCAL2_enzyme |
R_CRNCAL2 R_CRNDCAL2 R_CTBTCAL2 |
517 | Translation: 517.0, Folding: 51.7 | 58,559 | UniprotID: P31552 ECnumber: EC 6.2.1.- |
FUNCTION: Could catalyze the transfer of CoA to carnitine, generating the initial carnitinyl-CoA needed for the CaiB reaction cycle. | |
| b4067 | b4067 | Cation/acetate symporter ActP (Acetate permease) (Acetate transporter ActP) | Cell_inner_membrane | R_ACt4pp_enzyme R_GLYCLTt4pp_enzyme |
R_ACt4pp R_GLYCLTt4pp |
549 | Secretion: 549.0, Translation: 549.0, Folding: 54.9 | 59,197 | UniprotID: P32705 | FUNCTION: Transports acetate. Also able to transport glycolate. {ECO:0000269|PubMed:14563880}. | |
| b0928 | b0928 | Aspartate aminotransferase (AspAT) (EC 2.6.1.1) (Transaminase A) | Cytoplasm | R_ASPTA_enzyme R_PHETA1_enzyme R_TYRTA_duplicate_2_enzyme |
R_ASPTA R_PHETA1 R_TYRTA_duplicate_2 |
396 | Translation: 396.0, Folding: 39.6 | 43,573 | UniprotID: P00509 ECnumber: EC 2.6.1.1 |
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| b0929 | b0929 | Outer membrane protein F (Outer membrane protein 1A) (Outer membrane protein B) (Outer membrane protein IA) (Porin OmpF) | Cell_outer_membrane | R_pqqtex_duplicate_2_enzyme R_12PPDRtex_duplicate_3_enzyme R_12PPDStex_duplicate_3_enzyme R_23CAMPtex_duplicate_3_enzyme R_23CCMPtex_duplicate_3_enzyme R_23CGMPtex_duplicate_3_enzyme R_23CUMPtex_duplicate_3_enzyme R_23DAPPAtex_duplicate_3_enzyme R_26DAHtex_duplicate_3_enzyme R_34dhpactex_duplicate_3_enzyme R_3AMPtex_duplicate_3_enzyme R_3CMPtex_duplicate_3_enzyme R_3GMPtex_duplicate_2_enzyme R_3HPPtex_duplicate_3_enzyme R_3PEPTtex_duplicate_3_enzyme R_3UMPtex_duplicate_3_enzyme R_4HOXPACDtex_duplicate_3_enzyme R_4PEPTtex_duplicate_3_enzyme R_5DGLCNtex_duplicate_3_enzyme R_5MTRtex_duplicate_3_enzyme R_ABUTtex_duplicate_3_enzyme R_ACACtex_duplicate_3_enzyme R_ACALDtex_duplicate_3_enzyme R_ACGAL1Ptex_duplicate_3_enzyme R_ACGALtex_duplicate_3_enzyme R_ACGAM1Ptex_duplicate_3_enzyme R_ACGAtex_duplicate_3_enzyme R_ACMANAtex_duplicate_3_enzyme R_ACMUMtex_duplicate_3_enzyme R_ACNAMtex_enzyme R_ACSERtex_duplicate_4_enzyme R_ACtex_duplicate_3_enzyme R_ADEtex_duplicate_3_enzyme R_AGMtex_duplicate_3_enzyme R_AKGtex_duplicate_3_enzyme R_ALAALAtex_duplicate_3_enzyme R_ALAtex_duplicate_3_enzyme R_ALLTNtex_duplicate_3_enzyme R_ALLtex_duplicate_3_enzyme R_AMPtex_duplicate_3_enzyme R_ANHGMtex_duplicate_3_enzyme R_ARBTtex_duplicate_4_enzyme R_ARBtex_duplicate_3_enzyme R_ARGtex_duplicate_3_enzyme R_ASCBtex_duplicate_3_enzyme R_ASNtex_duplicate_3_enzyme R_ASO3tex_duplicate_3_enzyme R_ASPtex_duplicate_3_enzyme R_BALAtex_duplicate_3_enzyme R_BTNtex_duplicate_4_enzyme R_BUTSO3tex_duplicate_3_enzyme R_BUTtex_duplicate_3_enzyme R_CA2tex_duplicate_3_enzyme R_CD2tex_duplicate_3_enzyme R_CGLYtex_duplicate_3_enzyme R_CHLtex_duplicate_3_enzyme R_CHTBStex_duplicate_3_enzyme R_CITtex_duplicate_3_enzyme R_CLtex_duplicate_3_enzyme R_CMPtex_duplicate_3_enzyme R_CMtex_enzyme R_CO2tex_duplicate_3_enzyme R_COBALT2tex_duplicate_3_enzyme R_CRNDtex_enzyme R_CRNtex_duplicate_3_enzyme R_CSNtex_duplicate_3_enzyme R_CU2tex_enzyme R_CUtex_duplicate_3_enzyme R_CYANtex_duplicate_3_enzyme R_CYNTtex_duplicate_3_enzyme R_CYSDtex_duplicate_3_enzyme R_CYStex_duplicate_3_enzyme R_CYTDtex_duplicate_3_enzyme R_D_LACtex_duplicate_3_enzyme R_DALAtex_duplicate_3_enzyme R_DAMPtex_duplicate_3_enzyme R_DAPtex_duplicate_3_enzyme R_DCAtex_duplicate_3_enzyme R_DCMPtex_duplicate_3_enzyme R_DDGLCNtex_duplicate_2_enzyme R_DGMPtex_duplicate_3_enzyme R_DGSNtex_duplicate_3_enzyme R_DHAtex_duplicate_3_enzyme R_DIMPtex_duplicate_3_enzyme R_DINStex_duplicate_3_enzyme R_DMSOtex_duplicate_3_enzyme R_DMStex_duplicate_3_enzyme R_DOPAtex_duplicate_3_enzyme R_DOXRBCNtex_enzyme R_DSERtex_duplicate_3_enzyme R_DTMPtex_duplicate_3_enzyme R_DUMPtex_duplicate_3_enzyme R_ETHAtex_duplicate_3_enzyme R_ETHSO3tex_duplicate_3_enzyme R_ETOHtex_duplicate_3_enzyme R_F6Ptex_duplicate_3_enzyme R_FALDtex_duplicate_3_enzyme R_FE2tex_duplicate_3_enzyme R_FE3tex_duplicate_3_enzyme R_FORtex_duplicate_3_enzyme R_FRULYStex_duplicate_3_enzyme R_FRUURtex_duplicate_3_enzyme R_FRUtex_duplicate_3_enzyme R_FUCtex_duplicate_3_enzyme R_FUMtex_duplicate_3_enzyme R_FUSAtex_enzyme R_G1Ptex_duplicate_3_enzyme R_G3PCtex_duplicate_3_enzyme R_G3PEtex_duplicate_2_enzyme R_G3PGtex_duplicate_3_enzyme R_G3PItex_duplicate_3_enzyme R_G3PStex_duplicate_3_enzyme R_G6Ptex_duplicate_3_enzyme R_GAL1Ptex_duplicate_3_enzyme R_GALBDtex_duplicate_3_enzyme R_GALCTNLtex_enzyme R_GALCTNtex_duplicate_3_enzyme R_GALCTtex_duplicate_3_enzyme R_GALTtex_duplicate_3_enzyme R_GALURtex_duplicate_3_enzyme R_GALtex_duplicate_3_enzyme R_GAMAN6Ptex_duplicate_3_enzyme R_GAMtex_duplicate_3_enzyme R_GBBTNtex_duplicate_3_enzyme R_GDPtex_enzyme R_GLCNtex_duplicate_3_enzyme R_GLCRtex_duplicate_3_enzyme R_GLCUR1Ptex_duplicate_3_enzyme R_GLCURtex_duplicate_3_enzyme R_GLCtex_copy1_duplicate_2_enzyme R_GLNtex_duplicate_3_enzyme R_GLUtex_duplicate_3_enzyme R_GLYALDtex_duplicate_3_enzyme R_GLYBtex_duplicate_3_enzyme R_GLYC2Ptex_enzyme R_GLYC3Ptex_duplicate_3_enzyme R_GLYCAtex_duplicate_3_enzyme R_GLYCLTtex_duplicate_3_enzyme R_GLYCtex_duplicate_3_enzyme R_GLYtex_duplicate_3_enzyme R_GMPtex_duplicate_4_enzyme R_GSNtex_duplicate_3_enzyme R_GTHOXtex_duplicate_3_enzyme R_GTHRDtex_duplicate_3_enzyme R_GTPtex_duplicate_3_enzyme R_H2O2tex_duplicate_3_enzyme R_H2Otex_duplicate_8_enzyme R_H2Stex_duplicate_3_enzyme R_H2tex_duplicate_3_enzyme R_HCINNMtex_duplicate_3_enzyme R_HG2tex_duplicate_3_enzyme R_HIStex_duplicate_3_enzyme R_HOMtex_duplicate_3_enzyme R_HPPPNtex_duplicate_2_enzyme R_HXAtex_enzyme R_HYXNtex_duplicate_3_enzyme R_Htex_duplicate_2_enzyme R_IDONtex_duplicate_3_enzyme R_ILEtex_duplicate_3_enzyme R_IMPtex_duplicate_3_enzyme R_INDOLEtex_duplicate_3_enzyme R_INSTtex_duplicate_3_enzyme R_ISETACtex_duplicate_3_enzyme R_Ktex_duplicate_3_enzyme R_L_LACtex_duplicate_2_enzyme R_LALADGLUtex_duplicate_4_enzyme R_LALALGLUtex_duplicate_4_enzyme R_LCTStex_duplicate_3_enzyme R_LEUtex_duplicate_3_enzyme R_LIPOtex_enzyme R_LYStex_duplicate_3_enzyme R_LYXtex_duplicate_3_enzyme R_MALDtex_duplicate_4_enzyme R_MALtex_duplicate_3_enzyme R_MAN6Ptex_duplicate_3_enzyme R_MANGLYCtex_duplicate_3_enzyme R_MANtex_duplicate_3_enzyme R_MELIBtex_duplicate_3_enzyme R_MEOHtex_duplicate_3_enzyme R_METDtex_duplicate_3_enzyme R_METSOX1tex_duplicate_3_enzyme R_METSOX2tex_duplicate_3_enzyme R_METtex_duplicate_3_enzyme R_MG2tex_duplicate_3_enzyme R_MINCYCtex_enzyme R_MMETtex_duplicate_3_enzyme R_MNLtex_duplicate_3_enzyme R_MNtex_duplicate_3_enzyme R_MOBDtex_duplicate_3_enzyme R_MSO3tex_duplicate_3_enzyme R_N2Otex_duplicate_3_enzyme R_NACtex_duplicate_3_enzyme R_NAtex_duplicate_3_enzyme R_NH4tex_duplicate_3_enzyme R_NI2tex_duplicate_3_enzyme R_NMNtex_duplicate_3_enzyme R_NO2tex_duplicate_3_enzyme R_NO3tex_enzyme R_NOtex_duplicate_3_enzyme R_O2Stex_duplicate_4_enzyme R_O2tex_duplicate_3_enzyme R_OCTAtex_duplicate_3_enzyme R_ORNtex_duplicate_3_enzyme R_OROTtex_enzyme R_PACALDtex_duplicate_3_enzyme R_PEAMNtex_duplicate_3_enzyme R_PHEtex_duplicate_3_enzyme R_PItex_duplicate_3_enzyme R_PNTOtex_duplicate_3_enzyme R_PPALtex_duplicate_3_enzyme R_PPAtex_duplicate_3_enzyme R_PPPNtex_duplicate_3_enzyme R_PPTtex_duplicate_3_enzyme R_PROGLYtex_duplicate_3_enzyme R_PROtex_duplicate_4_enzyme R_PSCLYStex_duplicate_4_enzyme R_PSERtex_duplicate_3_enzyme R_PTRCtex_duplicate_3_enzyme R_PYDAMtex_duplicate_3_enzyme R_PYDXNtex_duplicate_3_enzyme R_PYDXtex_duplicate_3_enzyme R_PYRtex_duplicate_3_enzyme R_QUIN2tex_duplicate_4_enzyme R_R5Ptex_duplicate_3_enzyme R_RIBtex_duplicate_3_enzyme R_RMNtex_enzyme R_SBTtex_duplicate_3_enzyme R_SELtex_duplicate_3_enzyme R_SERtex_duplicate_3_enzyme R_SKMtex_duplicate_3_enzyme R_SLNTtex_duplicate_3_enzyme R_SO2tex_duplicate_3_enzyme R_SO3tex_duplicate_3_enzyme R_SO4tex_duplicate_3_enzyme R_SPMDtex_duplicate_3_enzyme R_SUCCtex_duplicate_3_enzyme R_SUCRtex_duplicate_3_enzyme R_SULFACtex_duplicate_4_enzyme R_TARTRDtex_duplicate_4_enzyme R_TARTRtex_duplicate_3_enzyme R_TAURtex_duplicate_3_enzyme R_TCYNTtex_duplicate_3_enzyme R_THMDtex_duplicate_3_enzyme R_THMtex_duplicate_3_enzyme R_THRPtex_duplicate_3_enzyme R_THRtex_duplicate_3_enzyme R_THYMtex_duplicate_2_enzyme R_TMAOtex_duplicate_3_enzyme R_TMAtex_duplicate_3_enzyme R_TREtex_duplicate_3_enzyme R_TRPtex_duplicate_3_enzyme R_TSULtex_duplicate_3_enzyme R_TTRCYCtex_enzyme R_TUNGStex_duplicate_4_enzyme R_TYMtex_duplicate_3_enzyme R_TYRPtex_enzyme R_TYRtex_duplicate_3_enzyme R_UACGAMtex_duplicate_3_enzyme R_UDPACGALtex_duplicate_3_enzyme R_UDPGALtex_duplicate_3_enzyme R_UDPGLCURtex_duplicate_3_enzyme R_UDPGtex_duplicate_3_enzyme R_UMPtex_duplicate_2_enzyme R_URAtex_duplicate_3_enzyme R_UREAtex_duplicate_3_enzyme R_VALtex_duplicate_3_enzyme R_XANtex_duplicate_3_enzyme R_XMPtex_duplicate_3_enzyme R_XTSNtex_duplicate_3_enzyme R_XYLUtex_duplicate_3_enzyme R_XYLtex_duplicate_3_enzyme R_Zn2tex_duplicate_3_enzyme |
R_pqqtex_duplicate_2 R_12PPDRtex_duplicate_3 R_12PPDStex_duplicate_3 R_23CAMPtex_duplicate_3 R_23CCMPtex_duplicate_3 R_23CGMPtex_duplicate_3 R_23CUMPtex_duplicate_3 R_23DAPPAtex_duplicate_3 R_26DAHtex_duplicate_3 R_34dhpactex_duplicate_3 R_3AMPtex_duplicate_3 R_3CMPtex_duplicate_3 R_3GMPtex_duplicate_2 R_3HPPtex_duplicate_3 R_3PEPTtex_duplicate_3 R_3UMPtex_duplicate_3 R_4HOXPACDtex_duplicate_3 R_4PEPTtex_duplicate_3 R_5DGLCNtex_duplicate_3 R_5MTRtex_duplicate_3 R_ABUTtex_duplicate_3 R_ACACtex_duplicate_3 R_ACALDtex_duplicate_3 R_ACGAL1Ptex_duplicate_3 R_ACGALtex_duplicate_3 R_ACGAM1Ptex_duplicate_3 R_ACGAtex_duplicate_3 R_ACMANAtex_duplicate_3 R_ACMUMtex_duplicate_3 R_ACNAMtex R_ACSERtex_duplicate_4 R_ACtex_duplicate_3 R_ADEtex_duplicate_3 R_AGMtex_duplicate_3 R_AKGtex_duplicate_3 R_ALAALAtex_duplicate_3 R_ALAtex_duplicate_3 R_ALLTNtex_duplicate_3 R_ALLtex_duplicate_3 R_AMPtex_duplicate_3 R_ANHGMtex_duplicate_3 R_ARBTtex_duplicate_4 R_ARBtex_duplicate_3 R_ARGtex_duplicate_3 R_ASCBtex_duplicate_3 R_ASNtex_duplicate_3 R_ASO3tex_duplicate_3 R_ASPtex_duplicate_3 R_BALAtex_duplicate_3 R_BTNtex_duplicate_4 R_BUTSO3tex_duplicate_3 R_BUTtex_duplicate_3 R_CA2tex_duplicate_3 R_CD2tex_duplicate_3 R_CGLYtex_duplicate_3 R_CHLtex_duplicate_3 R_CHTBStex_duplicate_3 R_CITtex_duplicate_3 R_CLtex_duplicate_3 R_CMPtex_duplicate_3 R_CMtex R_CO2tex_duplicate_3 R_COBALT2tex_duplicate_3 R_CRNDtex R_CRNtex_duplicate_3 R_CSNtex_duplicate_3 R_CU2tex R_CUtex_duplicate_3 R_CYANtex_duplicate_3 R_CYNTtex_duplicate_3 R_CYSDtex_duplicate_3 R_CYStex_duplicate_3 R_CYTDtex_duplicate_3 R_D_LACtex_duplicate_3 R_DALAtex_duplicate_3 R_DAMPtex_duplicate_3 R_DAPtex_duplicate_3 R_DCAtex_duplicate_3 R_DCMPtex_duplicate_3 R_DDGLCNtex_duplicate_2 R_DGMPtex_duplicate_3 R_DGSNtex_duplicate_3 R_DHAtex_duplicate_3 R_DIMPtex_duplicate_3 R_DINStex_duplicate_3 R_DMSOtex_duplicate_3 R_DMStex_duplicate_3 R_DOPAtex_duplicate_3 R_DOXRBCNtex R_DSERtex_duplicate_3 R_DTMPtex_duplicate_3 R_DUMPtex_duplicate_3 R_ETHAtex_duplicate_3 R_ETHSO3tex_duplicate_3 R_ETOHtex_duplicate_3 R_F6Ptex_duplicate_3 R_FALDtex_duplicate_3 R_FE2tex_duplicate_3 R_FE3tex_duplicate_3 R_FORtex_duplicate_3 R_FRULYStex_duplicate_3 R_FRUURtex_duplicate_3 R_FRUtex_duplicate_3 R_FUCtex_duplicate_3 R_FUMtex_duplicate_3 R_FUSAtex R_G1Ptex_duplicate_3 R_G3PCtex_duplicate_3 R_G3PEtex_duplicate_2 R_G3PGtex_duplicate_3 R_G3PItex_duplicate_3 R_G3PStex_duplicate_3 R_G6Ptex_duplicate_3 R_GAL1Ptex_duplicate_3 R_GALBDtex_duplicate_3 R_GALCTNLtex R_GALCTNtex_duplicate_3 R_GALCTtex_duplicate_3 R_GALTtex_duplicate_3 R_GALURtex_duplicate_3 R_GALtex_duplicate_3 R_GAMAN6Ptex_duplicate_3 R_GAMtex_duplicate_3 R_GBBTNtex_duplicate_3 R_GDPtex R_GLCNtex_duplicate_3 R_GLCRtex_duplicate_3 R_GLCUR1Ptex_duplicate_3 R_GLCURtex_duplicate_3 R_GLCtex_copy1_duplicate_2 R_GLNtex_duplicate_3 R_GLUtex_duplicate_3 R_GLYALDtex_duplicate_3 R_GLYBtex_duplicate_3 R_GLYC2Ptex R_GLYC3Ptex_duplicate_3 R_GLYCAtex_duplicate_3 R_GLYCLTtex_duplicate_3 R_GLYCtex_duplicate_3 R_GLYtex_duplicate_3 R_GMPtex_duplicate_4 R_GSNtex_duplicate_3 R_GTHOXtex_duplicate_3 R_GTHRDtex_duplicate_3 R_GTPtex_duplicate_3 R_H2O2tex_duplicate_3 R_H2Otex_duplicate_8 R_H2Stex_duplicate_3 R_H2tex_duplicate_3 R_HCINNMtex_duplicate_3 R_HG2tex_duplicate_3 R_HIStex_duplicate_3 R_HOMtex_duplicate_3 R_HPPPNtex_duplicate_2 R_HXAtex R_HYXNtex_duplicate_3 R_Htex_duplicate_2 R_IDONtex_duplicate_3 R_ILEtex_duplicate_3 R_IMPtex_duplicate_3 R_INDOLEtex_duplicate_3 R_INSTtex_duplicate_3 R_ISETACtex_duplicate_3 R_Ktex_duplicate_3 R_L_LACtex_duplicate_2 R_LALADGLUtex_duplicate_4 R_LALALGLUtex_duplicate_4 R_LCTStex_duplicate_3 R_LEUtex_duplicate_3 R_LIPOtex R_LYStex_duplicate_3 R_LYXtex_duplicate_3 R_MALDtex_duplicate_4 R_MALtex_duplicate_3 R_MAN6Ptex_duplicate_3 R_MANGLYCtex_duplicate_3 R_MANtex_duplicate_3 R_MELIBtex_duplicate_3 R_MEOHtex_duplicate_3 R_METDtex_duplicate_3 R_METSOX1tex_duplicate_3 R_METSOX2tex_duplicate_3 R_METtex_duplicate_3 R_MG2tex_duplicate_3 R_MINCYCtex R_MMETtex_duplicate_3 R_MNLtex_duplicate_3 R_MNtex_duplicate_3 R_MOBDtex_duplicate_3 R_MSO3tex_duplicate_3 R_N2Otex_duplicate_3 R_NACtex_duplicate_3 R_NAtex_duplicate_3 R_NH4tex_duplicate_3 R_NI2tex_duplicate_3 R_NMNtex_duplicate_3 R_NO2tex_duplicate_3 R_NO3tex R_NOtex_duplicate_3 R_O2Stex_duplicate_4 R_O2tex_duplicate_3 R_OCTAtex_duplicate_3 R_ORNtex_duplicate_3 R_OROTtex R_PACALDtex_duplicate_3 R_PEAMNtex_duplicate_3 R_PHEtex_duplicate_3 R_PItex_duplicate_3 R_PNTOtex_duplicate_3 R_PPALtex_duplicate_3 R_PPAtex_duplicate_3 R_PPPNtex_duplicate_3 R_PPTtex_duplicate_3 R_PROGLYtex_duplicate_3 R_PROtex_duplicate_4 R_PSCLYStex_duplicate_4 R_PSERtex_duplicate_3 R_PTRCtex_duplicate_3 R_PYDAMtex_duplicate_3 R_PYDXNtex_duplicate_3 R_PYDXtex_duplicate_3 R_PYRtex_duplicate_3 R_QUIN2tex_duplicate_4 R_R5Ptex_duplicate_3 R_RIBtex_duplicate_3 R_RMNtex R_SBTtex_duplicate_3 R_SELtex_duplicate_3 R_SERtex_duplicate_3 R_SKMtex_duplicate_3 R_SLNTtex_duplicate_3 R_SO2tex_duplicate_3 R_SO3tex_duplicate_3 R_SO4tex_duplicate_3 R_SPMDtex_duplicate_3 R_SUCCtex_duplicate_3 R_SUCRtex_duplicate_3 R_SULFACtex_duplicate_4 R_TARTRDtex_duplicate_4 R_TARTRtex_duplicate_3 R_TAURtex_duplicate_3 R_TCYNTtex_duplicate_3 R_THMDtex_duplicate_3 R_THMtex_duplicate_3 R_THRPtex_duplicate_3 R_THRtex_duplicate_3 R_THYMtex_duplicate_2 R_TMAOtex_duplicate_3 R_TMAtex_duplicate_3 R_TREtex_duplicate_3 R_TRPtex_duplicate_3 R_TSULtex_duplicate_3 R_TTRCYCtex R_TUNGStex_duplicate_4 R_TYMtex_duplicate_3 R_TYRPtex R_TYRtex_duplicate_3 R_UACGAMtex_duplicate_3 R_UDPACGALtex_duplicate_3 R_UDPGALtex_duplicate_3 R_UDPGLCURtex_duplicate_3 R_UDPGtex_duplicate_3 R_UMPtex_duplicate_2 R_URAtex_duplicate_3 R_UREAtex_duplicate_3 R_VALtex_duplicate_3 R_XANtex_duplicate_3 R_XMPtex_duplicate_3 R_XTSNtex_duplicate_3 R_XYLUtex_duplicate_3 R_XYLtex_duplicate_3 R_Zn2tex_duplicate_3 |
362 | Secretion: 362.0, Translation: 362.0, Folding: 36.2 | 39,333 | UniprotID: P02931 | FUNCTION: Forms pores that allow passive diffusion of small molecules across the outer membrane. It is also a receptor for the bacteriophage T2. {ECO:0000269|PubMed:19721064}. | |
| b0323 | b0323 | Carbamate kinase-like protein YahI | Cytoplasm | R_CBMKr_enzyme | R_CBMKr | 316 | Translation: 316.0, Folding: 31.6 | 33,931 | UniprotID: P77624 | ||
| b4467 | b4467 | Glycolate oxidase iron-sulfur subunit | Cytoplasm | R_GLYCTO2_enzyme R_GLYCTO3_enzyme R_GLYCTO4_enzyme |
R_GLYCTO2 R_GLYCTO3 R_GLYCTO4 |
407 | Translation: 407.0, Folding: 40.7 | 45,110 | UniprotID: P52074 | ||
| b4460 | b4460 | L-arabinose transport system permease protein AraH | Cell_inner_membrane | R_ARBabcpp_enzyme | R_ARBabcpp | 328 | Secretion: 328.0, Translation: 328.0, Folding: 32.8 | 34,211 | UniprotID: P0AE26 | FUNCTION: Part of the binding-protein-dependent transport system for L-arabinose. Probably responsible for the translocation of the substrate across the membrane. | |
| b4468 | b4468 | Glycolate oxidase subunit GlcE | Cytoplasm | R_GLYCTO2_enzyme R_GLYCTO3_enzyme R_GLYCTO4_enzyme |
R_GLYCTO2 R_GLYCTO3 R_GLYCTO4 |
350 | Translation: 350.0, Folding: 35.0 | 38,361 | UniprotID: P52073 | ||
| b2234 | b2234 | Ribonucleoside-diphosphate reductase 1 subunit alpha (EC 1.17.4.1) (Protein B1) (Ribonucleoside-diphosphate reductase 1 R1 subunit) (Ribonucleotide reductase 1) | Cytoplasm | 761 | Translation: 761.0, Folding: 76.1 | 85,775 | UniprotID: P00452 ECnumber: EC 1.17.4.1 |
FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1 contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. It also provides redox-active cysteines. | |||
| b3568 | b3568 | Xylose transport system permease protein XylH | Cell_inner_membrane | R_XYLabcpp_enzyme | R_XYLabcpp | 393 | Secretion: 393.0, Translation: 393.0, Folding: 39.3 | 41,031 | UniprotID: P0AGI4 | FUNCTION: Part of the binding-protein-dependent transport system for D-xylose. Probably responsible for the translocation of the substrate across the membrane. | |
| b3565 | b3565 | Xylose isomerase (EC 5.3.1.5) (D-xylulose keto-isomerase) | Cytoplasm | R_XYLI1_enzyme R_XYLI2_enzyme |
R_XYLI1 R_XYLI2 |
440 | Translation: 440.0, Folding: 44.0 | 49,742 | UniprotID: P00944 ECnumber: EC 5.3.1.5 |
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| b3564 | b3564 | Xylulose kinase (Xylulokinase) (EC 2.7.1.17) | Cytoplasm | R_DXYLK_enzyme R_XYLK_duplicate_2_enzyme |
R_DXYLK R_XYLK_duplicate_2 |
484 | Translation: 484.0, Folding: 48.4 | 52,618 | UniprotID: P09099 ECnumber: EC 2.7.1.17 |
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| b3567 | b3567 | Xylose import ATP-binding protein XylG (EC 3.6.3.17) | Cell_inner_membrane | R_XYLabcpp_enzyme | R_XYLabcpp | 513 | Secretion: 513.0, Translation: 513.0, Folding: 51.3 | 56,470 | UniprotID: P37388 ECnumber: EC 3.6.3.17 |
FUNCTION: Part of the ABC transporter complex XylFGH involved in xylose import. Responsible for energy coupling to the transport system (Probable). The XylFGH system can also transport ribose in absence of xylose. {ECO:0000255|HAMAP-Rule:MF_01722, ECO:0000269|PubMed:9673030, ECO:0000305}. | |
| b3566 | b3566 | D-xylose-binding periplasmic protein | Periplasm | R_XYLabcpp_enzyme | R_XYLabcpp | 330 | Secretion: 330.0, Translation: 330.0, Folding: 33.0 | 35,734 | UniprotID: P37387 | FUNCTION: Involved in the high-affinity D-xylose membrane transport system. Binds with high affinity to xylose. | |
| b3560 | b3560 | Glycine--tRNA ligase alpha subunit (EC 6.1.1.14) (Glycyl-tRNA synthetase alpha subunit) (GlyRS) | Cytoplasm | R_GLYTRS_enzyme | R_GLYTRS | 303 | Translation: 303.0, Folding: 30.3 | 34,774 | UniprotID: P00960 ECnumber: EC 6.1.1.14 |
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| b3161 | b3161 | Tryptophan-specific transport protein (Tryptophan permease) | Cell_inner_membrane | R_INDOLEt2rpp_enzyme R_TRPt2rpp_duplicate_2_enzyme |
R_INDOLEt2rpp R_TRPt2rpp_duplicate_2 |
414 | Secretion: 414.0, Translation: 414.0, Folding: 41.4 | 44,333 | UniprotID: P0AAD2 | FUNCTION: Involved in transporting tryptophan across the cytoplasmic membrane. | |
| b2366 | b2366 | D-serine dehydratase (EC 4.3.1.18) (D-serine deaminase) (DSD) | Cytoplasm | R_SERD_D_enzyme | R_SERD_D | 442 | Translation: 442.0, Folding: 44.2 | 47,901 | UniprotID: P00926 ECnumber: EC 4.3.1.18 |
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| b3415 | b3415 | High-affinity gluconate transporter (Gluconate permease) (Gnt-I system) | Cell_inner_membrane | R_GLCNt2rpp_enzyme | R_GLCNt2rpp | 438 | Secretion: 438.0, Translation: 438.0, Folding: 43.8 | 45,967 | UniprotID: P39835 | FUNCTION: Part of the gluconate utilization system Gnt-I; high-affinity intake of gluconate. | |
| b3946 | b3946 | Fructose-6-phosphate aldolase 2 (EC 4.1.2.-) (Fructose-6-phosphate aldolase B) (FSAB) | Cytoplasm | R_F6PA_duplicate_2_enzyme | R_F6PA_duplicate_2 | 220 | Translation: 220.0, Folding: 22.0 | 23,555 | UniprotID: P32669 ECnumber: EC 4.1.2.- |
FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize hydroxyacetone as an alternative donor substrate. Is also able to catalyze the direct self-aldol addition of glycolaldehyde. Is less catalytically efficient than the isozyme FsaA. Does not display transaldolase activity. {ECO:0000269|PubMed:11120740, ECO:0000269|Ref.6}. |
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| b3417 | b3417 | Maltodextrin phosphorylase (EC 2.4.1.1) | Cytoplasm | R_GLCP_duplicate_2_enzyme R_GLCP2_enzyme R_MLTP1_enzyme R_MLTP2_enzyme R_MLTP3_enzyme |
R_GLCP_duplicate_2 R_GLCP2 R_MLTP1 R_MLTP2 R_MLTP3 |
797 | Translation: 797.0, Folding: 79.7 | 90,522 | UniprotID: P00490 ECnumber: EC 2.4.1.1 |
FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | |
| b3416 | b3416 | 4-alpha-glucanotransferase (EC 2.4.1.25) (Amylomaltase) (Disproportionating enzyme) (D-enzyme) | Cytoplasm | R_AMALT1_enzyme R_AMALT2_enzyme R_AMALT3_enzyme R_AMALT4_enzyme |
R_AMALT1 R_AMALT2 R_AMALT3 R_AMALT4 |
694 | Translation: 694.0, Folding: 69.4 | 78,503 | UniprotID: P15977 ECnumber: EC 2.4.1.25 |
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| b2148 | b2148 | Galactoside transport system permease protein MglC | Cell_inner_membrane | R_GALabcpp_enzyme R_GLCabcpp_enzyme |
R_GALabcpp R_GLCabcpp |
336 | Secretion: 336.0, Translation: 336.0, Folding: 33.6 | 35,550 | UniprotID: P23200 | FUNCTION: Part of the binding-protein-dependent transport system for galactoside. Probably responsible for the translocation of the substrate across the membrane. | |
| b2149 | b2149 | Galactose/methyl galactoside import ATP-binding protein MglA (EC 3.6.3.17) | Cell_inner_membrane | R_GALabcpp_enzyme R_GLCabcpp_enzyme |
R_GALabcpp R_GLCabcpp |
506 | Secretion: 506.0, Translation: 506.0, Folding: 50.6 | 56,415 | UniprotID: P0AAG8 ECnumber: EC 3.6.3.17 |
FUNCTION: Part of the ABC transporter complex MglABC involved in galactose/methyl galactoside import. Responsible for energy coupling to the transport system (Probable). {ECO:0000305|PubMed:4910389, ECO:0000305|PubMed:6294056, ECO:0000305|PubMed:6807987}. | |
| b3941 | b3941 | 5,10-methylenetetrahydrofolate reductase (EC 1.5.1.20) | Cytoplasm | R_MTHFR2_enzyme | R_MTHFR2 | 296 | Translation: 296.0, Folding: 29.6 | 33,103 | UniprotID: P0AEZ1 ECnumber: EC 1.5.1.20 |
FUNCTION: Methylenetetrahydrofolate reductase required to generate the methyl groups necessary for methionine synthetase to convert homocysteine to methionine. {ECO:0000269|PubMed:14275142}. | |
| b3412 | b3412 | Pimeloyl-[acyl-carrier protein] methyl ester esterase (EC 3.1.1.85) (Biotin synthesis protein BioH) (Carboxylesterase BioH) | Cytoplasm | R_PMEACPE_enzyme | R_PMEACPE | 256 | Translation: 256.0, Folding: 25.6 | 28,505 | UniprotID: P13001 ECnumber: EC 3.1.1.85 |
FUNCTION: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain p-nitrophenyl esters. Also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis.; FUNCTION: Catalyzes the hydrolysis of the methyl ester bond of dimethylbutyryl-S-methyl mercaptopropionate (DMB-S-MMP) to yield dimethylbutyryl mercaptopropionic acid (DMBS-MPA) during the biocatalytic conversion of simvastin acid from monacolin J acid. Can also use acyl carriers such as dimethylbutyryl-S-ethyl mercaptopropionate (DMB-S-EMP) and dimethylbutyryl-S-methyl thioglycolate (DMB-S-MTG) as the thioester substrates. |
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| b2416 | b2416 | Phosphoenolpyruvate-protein phosphotransferase (EC 2.7.3.9) (Phosphotransferase system, enzyme I) | Cytoplasm | R_ACGAptspp_enzyme R_ACGAptspp_duplicate_2_enzyme R_ACMANAptspp_enzyme R_ACMUMptspp_enzyme R_ARBTptspp_enzyme R_ARBTptspp_duplicate_2_enzyme R_ASCBptspp_enzyme R_CHTBSptspp_enzyme R_DHAPT_enzyme R_FRUpts2pp_enzyme R_FRUptspp_enzyme R_GALTptspp_enzyme R_GAMptspp_enzyme R_GLCptspp_enzyme R_GLCptspp_duplicate_2_enzyme R_GLCptspp_duplicate_3_enzyme R_MALTptspp_enzyme R_MANGLYCptspp_enzyme R_MANptspp_enzyme R_MNLptspp_enzyme R_SBTptspp_enzyme R_SUCptspp_enzyme R_TREptspp_enzyme |
575 | Translation: 575.0, Folding: 57.5 | 63,562 | UniprotID: P08839 ECnumber: EC 2.7.3.9 |
FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) (PubMed:7876255, PubMed:12705838, PubMed:17053069). Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl-PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP) as alternative phosphoryl donors (PubMed:12705838). {ECO:0000269|PubMed:12705838, ECO:0000269|PubMed:17053069, ECO:0000269|PubMed:7876255}. |
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| b2417 | b2417 | PTS system glucose-specific EIIA component (EIIA-Glc) (EIII-Glc) (Glucose-specific phosphotransferase enzyme IIA component) (EC 2.7.1.199) | Cytoplasm | 169 | Translation: 169.0, Folding: 16.9 | 18,251 | UniprotID: P69783 ECnumber: EC 2.7.1.199 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:3129430, PubMed:17158705). The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:2657735). The non-phosphorylated EIII-Glc is an inhibitor for uptake of certain sugars such as maltose, melibiose, lactose, and glycerol. Phosphorylated EIII-Glc, however, may be an activator for adenylate cyclase. It is an important regulatory protein for cell metabolism (PubMed:789369). {ECO:0000269|PubMed:2657735, ECO:0000269|PubMed:3129430, ECO:0000269|PubMed:789369, ECO:0000305|PubMed:17158705}. |
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| b2146 | b2146 | NAD-dependent dihydropyrimidine dehydrogenase subunit PreT (DPD) (EC 1.3.1.1) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) | Cytoplasm | R_DURADx_enzyme | R_DURADx | 412 | Translation: 412.0, Folding: 41.2 | 44,329 | UniprotID: P76440 ECnumber: EC 1.3.1.1 |
FUNCTION: Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). {ECO:0000269|PubMed:18482579, ECO:0000269|PubMed:21169495}. | |
| b2147 | b2147 | NAD-dependent dihydropyrimidine dehydrogenase subunit PreA (DPD) (EC 1.3.1.1) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) | Cytoplasm | R_DURADx_enzyme | R_DURADx | 411 | Translation: 411.0, Folding: 41.1 | 45,069 | UniprotID: P25889 ECnumber: EC 1.3.1.1 |
FUNCTION: Involved in pyrimidine base degradation. Catalyzes physiologically the reduction of uracil to 5,6-dihydrouracil (DHU) by using NADH as a specific cosubstrate. It also catalyzes the reverse reaction and the reduction of thymine to 5,6-dihydrothymine (DHT). {ECO:0000269|PubMed:18482579, ECO:0000269|PubMed:21169495}. | |
| b2411 | b2411 | DNA ligase (EC 6.5.1.2) (Polydeoxyribonucleotide synthase [NAD(+)]) | Cytoplasm | R_NADDP_duplicate_2_enzyme | R_NADDP_duplicate_2 | 671 | Translation: 671.0, Folding: 67.1 | 73,606 | UniprotID: P15042 ECnumber: EC 6.5.1.2 |
FUNCTION: DNA ligase that catalyzes the formation of phosphodiester linkages between 5-phosphoryl and 3-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. | |
| b3785 | b3785 | ECA polysaccharide chain length modulation protein | Cell_inner_membrane | R_ECAP1pp_enzyme R_ECAP2pp_enzyme R_ECAP3pp_enzyme |
R_ECAP1pp R_ECAP2pp R_ECAP3pp |
348 | Secretion: 348.0, Translation: 348.0, Folding: 34.8 | 39,489 | UniprotID: P0AG00 | FUNCTION: Modulates the polysaccharide chain length of enterobacterial common antigen (ECA). Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)). {ECO:0000269|PubMed:10515954, ECO:0000269|PubMed:16199561}. | |
| b3784 | b3784 | Undecaprenyl-phosphate alpha-N-acetylglucosaminyl 1-phosphate transferase (EC 2.7.8.33) (UDP-GlcNAc:undecaprenyl-phosphate GlcNAc-1-phosphate transferase) (Undecaprenyl-phosphate GlcNAc-1-phosphate transferase) | Cell_inner_membrane | R_ACGAMT_enzyme | R_ACGAMT | 367 | Secretion: 367.0, Translation: 367.0, Folding: 36.7 | 40,957 | UniprotID: P0AC78 ECnumber: EC 2.7.8.33 |
FUNCTION: Catalyzes the transfer of the GlcNAc-1-phosphate moiety from UDP-GlcNAc onto the carrier lipid undecaprenyl phosphate (C55-P), yielding GlcNAc-pyrophosphoryl-undecaprenyl (GlcNAc-PP-C55). It is the first lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis, and an acceptor for the addition of subsequent sugars to complete the biosynthesis of O-antigen lipopolysaccharide (LPS) in many E.coli O types. The apparent affinity of WecA for the polyisoprenyl phosphate substrates increases with the polyisoprenyl chain length. WecA is unable to utilize dolichyl phosphate (Dol-P). {ECO:0000269|PubMed:11700352, ECO:0000269|PubMed:17237164, ECO:0000269|PubMed:1730666, ECO:0000269|PubMed:9134438}. |
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| b3787 | b3787 | UDP-N-acetyl-D-mannosamine dehydrogenase (EC 1.1.1.336) (UDP-ManNAc 6-dehydrogenase) | Cytoplasm | R_UACMAMO_enzyme | R_UACMAMO | 420 | Translation: 420.0, Folding: 42.0 | 45,839 | UniprotID: P27829 ECnumber: EC 1.1.1.336 |
FUNCTION: Catalyzes the four-electron oxidation of UDP-N-acetyl-D-mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N-acetylmannosaminuronic acid (UDP-ManNAcA). {ECO:0000255|HAMAP-Rule:MF_02029, ECO:0000269|PubMed:381306}. | |
| b3786 | b3786 | UDP-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) (Bacteriophage N4 adsorption protein C) (UDP-GlcNAc-2-epimerase) | Cytoplasm | R_UAG2E_enzyme | R_UAG2E | 376 | Translation: 376.0, Folding: 37.6 | 42,245 | UniprotID: P27828 ECnumber: EC 5.1.3.14 |
FUNCTION: Catalyzes the reversible epimerization at C-2 of UDP-N-acetylglucosamine (UDP-GlcNAc) and thereby provides bacteria with UDP-N-acetylmannosamine (UDP-ManNAc), the activated donor of ManNAc residues. Also involved in bacteriophage N4 adsorption. {ECO:0000269|PubMed:15210128, ECO:0000269|PubMed:7559340, ECO:0000269|PubMed:8170390, ECO:0000269|PubMed:8226648, ECO:0000269|Ref.9}. | |
| b3781 | b3781 | Thioredoxin 1 (Trx-1) | Cytoplasm | 109 | Translation: 109.0, Folding: 10.9 | 11,807 | UniprotID: P0AA25 | FUNCTION: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. | |||
| b2964 | b2964 | Nucleoside permease NupG (Nucleoside-transport system protein NupG) | Cell_inner_membrane | 418 | Secretion: 418.0, Translation: 418.0, Folding: 41.8 | 46,389 | UniprotID: P0AFF4 | FUNCTION: Broad-specificity transporter of purine and pyrimidine nucleosides. Driven by a proton motive force. Can transport uridine, adenosine, inosine, guanosine, thymidine and cytidine. Can also transport xanthosine, but with a very low affinity. {ECO:0000269|PubMed:11466294, ECO:0000269|PubMed:15513740, ECO:0000269|PubMed:15678184, ECO:0000269|PubMed:3311747, ECO:0000269|PubMed:374403}. | |||
| b2965 | b2965 | Constitutive ornithine decarboxylase (EC 4.1.1.17) | Cytoplasm | R_ORNDC_enzyme | R_ORNDC | 711 | Translation: 711.0, Folding: 71.1 | 79,416 | UniprotID: P21169 ECnumber: EC 4.1.1.17 |
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| b3789 | b3789 | Glucose-1-phosphate thymidylyltransferase 2 (G1P-TT 2) (EC 2.7.7.24) (dTDP-glucose pyrophosphorylase 2) (dTDP-glucose synthase 2) | Cytoplasm | R_G1PTT_duplicate_2_enzyme | R_G1PTT_duplicate_2 | 293 | Translation: 293.0, Folding: 29.3 | 32,734 | UniprotID: P61887 ECnumber: EC 2.7.7.24 |
FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000269|PubMed:7559340}. | |
| b3788 | b3788 | dTDP-glucose 4,6-dehydratase 2 (EC 4.2.1.46) | Cytoplasm | R_TDPGDH_enzyme | R_TDPGDH | 355 | Translation: 355.0, Folding: 35.5 | 39,754 | UniprotID: P27830 ECnumber: EC 4.2.1.46 |
FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction. {ECO:0000269|PubMed:11380254, ECO:0000269|PubMed:11601973, ECO:0000269|PubMed:7559340}. | |
| b2092 | b2092 | PTS system galactitol-specific EIIC component (EIIC-Gat) (Galactitol permease IIC component) | Cell_inner_membrane | R_GALTptspp_enzyme | R_GALTptspp | 451 | Secretion: 451.0, Translation: 451.0, Folding: 45.1 | 48,365 | UniprotID: P69831 | FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of GatA, GatB and GatC is involved in galactitol transport. {ECO:0000269|PubMed:8955298}. | |
| b2093 | b2093 | PTS system galactitol-specific EIIB component (EIIB-Gat) (Galactitol-specific phosphotransferase enzyme IIB component) (EC 2.7.1.200) | Cytoplasm | R_GALTptspp_enzyme | R_GALTptspp | 94 | Translation: 94.0, Folding: 9.4 | 10,222 | UniprotID: P37188 ECnumber: EC 2.7.1.200 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of GatA, GatB and GatC is involved in galactitol transport. It can also use D-glucitol. {ECO:0000269|PubMed:1100608, ECO:0000269|PubMed:8955298}. |
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| b2091 | b2091 | Galactitol 1-phosphate 5-dehydrogenase (EC 1.1.1.251) | Cytoplasm | R_GLTPD_enzyme | R_GLTPD | 346 | Translation: 346.0, Folding: 34.6 | 37,390 | UniprotID: P0A9S3 ECnumber: EC 1.1.1.251 |
FUNCTION: Converts galactitol 1-phosphate to D-tagatose 6-phosphate. {ECO:0000269|PubMed:13331868}. | |
| b2096 | b2096 | D-tagatose-1,6-bisphosphate aldolase subunit GatY (TBPA) (TagBP aldolase) (EC 4.1.2.40) (D-tagatose-bisphosphate aldolase class II) (Tagatose-bisphosphate aldolase) | Cytoplasm | R_TGBPA_duplicate_2_enzyme | R_TGBPA_duplicate_2 | 284 | Translation: 284.0, Folding: 28.4 | 30,812 | UniprotID: P0C8J6 ECnumber: EC 4.1.2.40 |
FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase GatYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires GatZ subunit for full activity and stability. Is involved in the catabolism of galactitol. {ECO:0000269|PubMed:11976750, ECO:0000269|PubMed:8955298}. |
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| b2097 | b2097 | Fructose-bisphosphate aldolase class 1 (EC 4.1.2.13) (Fructose-bisphosphate aldolase class I) (FBP aldolase) | Cytoplasm | R_FBA_duplicate_2_enzyme | R_FBA_duplicate_2 | 350 | Translation: 350.0, Folding: 35.0 | 38,109 | UniprotID: P0A991 ECnumber: EC 4.1.2.13 |
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| b2094 | b2094 | PTS system galactitol-specific EIIA component (EIIB-Gat) (Galactitol-specific phosphotransferase enzyme IIA component) (EC 2.7.1.200) | Cytoplasm | R_GALTptspp_enzyme | R_GALTptspp | 150 | Translation: 150.0, Folding: 15.0 | 16,907 | UniprotID: P69828 ECnumber: EC 2.7.1.200 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of GatA, GatB and GatC is involved in galactitol transport. It can also use D-glucitol. {ECO:0000269|PubMed:1100608, ECO:0000269|PubMed:8955298}. |
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| b2095 | b2095 | D-tagatose-1,6-bisphosphate aldolase subunit GatZ | Cytoplasm | R_TGBPA_duplicate_2_enzyme | R_TGBPA_duplicate_2 | 420 | Translation: 420.0, Folding: 42.0 | 47,109 | UniprotID: P0C8J8 | FUNCTION: Component of the tagatose-1,6-bisphosphate aldolase GatYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of GatY. When expressed alone, GatZ does not show any aldolase activity. Is involved in the catabolism of galactitol. {ECO:0000269|PubMed:11976750, ECO:0000269|PubMed:8955298}. | |
| b2563 | b2563 | Holo-[acyl-carrier-protein] synthase (Holo-ACP synthase) (EC 2.7.8.7) (4-phosphopantetheinyl transferase AcpS) | Cytoplasm | R_ACPS1_duplicate_2_enzyme | R_ACPS1_duplicate_2 | 126 | Translation: 126.0, Folding: 12.6 | 14,052 | UniprotID: P24224 ECnumber: EC 2.7.8.7 |
FUNCTION: Transfers the 4-phosphopantetheine moiety from coenzyme A to the Ser-36 of acyl-carrier-protein. {ECO:0000269|PubMed:7559576}. | |
| b2564 | b2564 | Pyridoxine 5-phosphate synthase (PNP synthase) (EC 2.6.99.2) | Cytoplasm | R_PDX5PS_enzyme | R_PDX5PS | 243 | Translation: 243.0, Folding: 24.3 | 26,384 | UniprotID: P0A794 ECnumber: EC 2.6.99.2 |
FUNCTION: Catalyzes the complicated ring closure reaction between the two acyclic compounds 1-deoxy-D-xylulose-5-phosphate (DXP) and 3-amino-2-oxopropyl phosphate (1-amino-acetone-3-phosphate or AAP) to form pyridoxine 5-phosphate (PNP) and inorganic phosphate. {ECO:0000269|PubMed:10225425}. | |
| b1069 | b1069 | Lipid II flippase MurJ (Peptidoglycan biosynthesis protein MurJ) | Cell_inner_membrane | R_MPTG R_MPTG_duplicate_2 R_MPTG_duplicate_3 R_MPTG2 R_MPTG2_duplicate_2 R_MPTG2_duplicate_3 |
511 | Secretion: 511.0, Translation: 511.0, Folding: 51.1 | 55,267 | UniprotID: P0AF16 | FUNCTION: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:18708495, ECO:0000269|PubMed:18832143, ECO:0000269|PubMed:25013077}. | ||
| b1064 | b1064 | Glutaredoxin 2 (Grx2) | Cytoplasm | 215 | Translation: 215.0, Folding: 21.5 | 24,350 | UniprotID: P0AC59 | FUNCTION: Involved in reducing some disulfide bonds in a coupled system with glutathione reductase. Does not act as hydrogen donor for ribonucleotide reductase. | |||
| b1062 | b1062 | Dihydroorotase (DHOase) (EC 3.5.2.3) | Cytoplasm | R_DHORTS_enzyme | R_DHORTS | 348 | Translation: 348.0, Folding: 34.8 | 38,827 | UniprotID: P05020 ECnumber: EC 3.5.2.3 |
FUNCTION: Catalyzes the reversible cyclization of carbamoyl aspartate to dihydroorotate. {ECO:0000255|HAMAP-Rule:MF_00219, ECO:0000269|PubMed:15610022, ECO:0000269|PubMed:6142052}. | |
| b1992 | b1992 | Adenosylcobinamide-GDP ribazoletransferase (EC 2.7.8.26) (Cobalamin synthase) (Cobalamin-5-phosphate synthase) | Cell_inner_membrane | R_ADOCBLS_enzyme | R_ADOCBLS | 247 | Secretion: 247.0, Translation: 247.0, Folding: 24.7 | 26,386 | UniprotID: P36561 ECnumber: EC 2.7.8.26 |
FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to generate adenosylcobalamin (Ado-cobalamin). Also synthesizes adenosylcobalamin 5-phosphate from adenosylcobinamide-GDP and alpha-ribazole 5-phosphate (By similarity). {ECO:0000250}. | |
| b1993 | b1993 | Bifunctional adenosylcobalamin biosynthesis protein CobU (Adenosylcobinamide kinase) (EC 2.7.1.156) (Adenosylcobinamide-phosphate guanylyltransferase) (EC 2.7.7.62) | Cytoplasm | R_ACBIPGT_enzyme R_ADOCBIK_enzyme |
R_ACBIPGT R_ADOCBIK |
181 | Translation: 181.0, Folding: 18.1 | 20,164 | UniprotID: P0AE76 ECnumber: EC 2.7.1.156; 2.7.7.62 |
FUNCTION: Catalyzes ATP-dependent phosphorylation of adenosylcobinamide and addition of GMP to adenosylcobinamide phosphate. {ECO:0000250|UniProtKB:Q05599}. | |
| b1991 | b1991 | Nicotinate-nucleotide--dimethylbenzimidazole phosphoribosyltransferase (NN:DBI PRT) (EC 2.4.2.21) (N(1)-alpha-phosphoribosyltransferase) | Cytoplasm | R_NNDMBRT_enzyme | R_NNDMBRT | 359 | Translation: 359.0, Folding: 35.9 | 36,987 | UniprotID: P36562 ECnumber: EC 2.4.2.21 |
FUNCTION: Catalyzes the synthesis of alpha-ribazole-5-phosphate from nicotinate mononucleotide (NAMN) and 5,6-dimethylbenzimidazole (DMB). | |
| b1488 | b1488 | D-alanyl-D-alanine dipeptidase (D-Ala-D-Ala dipeptidase) (EC 3.4.13.22) | Cytoplasm | R_ALAALAD_enzyme | R_ALAALAD | 193 | Translation: 193.0, Folding: 19.3 | 21,213 | UniprotID: P77790 ECnumber: EC 3.4.13.22 |
FUNCTION: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. May have a role in cell-wall turnover. {ECO:0000255|HAMAP-Rule:MF_01924, ECO:0000269|PubMed:9751644}. | |
| b2890 | b2890 | Lysine--tRNA ligase (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS) | Cytoplasm | R_LYSTRS_duplicate_2_enzyme | R_LYSTRS_duplicate_2 | 505 | Translation: 505.0, Folding: 50.5 | 57,603 | UniprotID: P0A8N3 ECnumber: EC 6.1.1.6 |
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| b2895 | b2895 | Flavodoxin 2 | Cytoplasm | 173 | Translation: 173.0, Folding: 17.3 | 19,700 | UniprotID: P0ABY4 | FUNCTION: Low-potential electron donor to a number of redox enzymes. {ECO:0000305}. | |||
| b2788 | b2788 | Glucarate dehydratase-related protein (GDH-RP) (GlucDRP) (EC 4.2.1.-) | Cytoplasm | R_GLCRD_enzyme | R_GLCRD | 446 | Translation: 446.0, Folding: 44.6 | 48,850 | UniprotID: Q46915 ECnumber: EC 4.2.1.- |
FUNCTION: Does not seem to have an in-vivo activity on glucarate or idarate. Its real substrate is unknown. | |
| b2789 | b2789 | Probable glucarate transporter (D-glucarate permease) | Cell_inner_membrane | R_GALCTt2rpp_enzyme R_GLCRt2rpp_duplicate_2_enzyme R_GLYCAt2rpp_enzyme |
R_GALCTt2rpp R_GLCRt2rpp_duplicate_2 R_GLYCAt2rpp |
450 | Secretion: 450.0, Translation: 450.0, Folding: 45.0 | 49,142 | UniprotID: Q46916 | FUNCTION: Uptake of D-glucarate. | |
| b2787 | b2787 | Glucarate dehydratase (GDH) (GlucD) (EC 4.2.1.40) | Cytoplasm | R_GLCRD_duplicate_2_enzyme | R_GLCRD_duplicate_2 | 446 | Translation: 446.0, Folding: 44.6 | 49,141 | UniprotID: P0AES2 ECnumber: EC 4.2.1.40 |
FUNCTION: Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc). Also acts on L-idarate. | |
| b2784 | b2784 | GTP pyrophosphokinase (EC 2.7.6.5) ((p)ppGpp synthase) (ATP:GTP 3-pyrophosphotransferase) (ppGpp synthase I) | Cytoplasm | R_GDPDPK_enzyme R_GTPDPK_enzyme |
R_GDPDPK R_GTPDPK |
744 | Translation: 744.0, Folding: 74.4 | 83,876 | UniprotID: P0AG20 ECnumber: EC 2.7.6.5 |
FUNCTION: In eubacteria ppGpp (guanosine 3-diphosphate 5- diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the formation of pppGpp which is then hydrolyzed to form ppGpp. {ECO:0000269|PubMed:14622409, ECO:0000269|PubMed:19460094, ECO:0000269|PubMed:26051177}. | |
| b2780 | b2780 | CTP synthase (EC 6.3.4.2) (Cytidine 5-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase) | Cytoplasm | R_CTPS2_enzyme | R_CTPS2 | 545 | Translation: 545.0, Folding: 54.5 | 60,374 | UniprotID: P0A7E5 ECnumber: EC 6.3.4.2 |
FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. {ECO:0000269|PubMed:11336655, ECO:0000269|PubMed:8385490, ECO:0000305|PubMed:15157079}. | |
| b2781 | b2781 | Nucleoside triphosphate pyrophosphohydrolase (NTP-PPase) (EC 3.6.1.8) | Cytoplasm | 263 | Translation: 263.0, Folding: 26.3 | 30,412 | UniprotID: P0AEY3 ECnumber: EC 3.6.1.8 |
FUNCTION: Involved in the regulation of bacterial cell survival under conditions of nutritional stress. Regulates the type II MazE-MazF toxin-antitoxin (TA) module which mediates programmed cell death (PCD). This is achieved by lowering the cellular concentration of (p)ppGpp produced by RelA under amino acid starvation, thus protecting the cell from the toxicity of MazF. Reduction of (p)ppGpp can be achieved by direct degradation of (p)ppGpp or by degradation of NTPs, which are substrates for (p)ppGpp synthesis by RelA. {ECO:0000269|PubMed:16390452, ECO:0000269|PubMed:18353782, ECO:0000269|PubMed:20529853}. |
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| b4322 | b4322 | Mannonate dehydratase (EC 4.2.1.8) (D-mannonate hydro-lyase) | Cytoplasm | R_MNNH_enzyme | R_MNNH | 394 | Translation: 394.0, Folding: 39.4 | 44,838 | UniprotID: P24215 ECnumber: EC 4.2.1.8 |
FUNCTION: Catalyzes the dehydration of D-mannonate. {ECO:0000269|PubMed:3038546}. | |
| b4323 | b4323 | D-mannonate oxidoreductase (EC 1.1.1.57) (Fructuronate reductase) | Cytoplasm | R_MANAO_enzyme | R_MANAO | 486 | Translation: 486.0, Folding: 48.6 | 53,580 | UniprotID: P39160 ECnumber: EC 1.1.1.57 |
||
| b1208 | b1208 | 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (CMK) (EC 2.7.1.148) (4-(cytidine-5-diphospho)-2-C-methyl-D-erythritol kinase) | Cytoplasm | R_CDPMEK_enzyme | R_CDPMEK | 283 | Translation: 283.0, Folding: 28.3 | 30,925 | UniprotID: P62615 ECnumber: EC 2.7.1.148 |
FUNCTION: Catalyzes the phosphorylation of the position 2 hydroxy group of 4-diphosphocytidyl-2C-methyl-D-erythritol. Phosphorylates isopentenyl phosphate at low rates. Also acts on isopentenol, and, much less efficiently, dimethylallyl alcohol. Dimethylallyl monophosphate does not serve as a substrate. | |
| b4321 | b4321 | High-affinity gluconate transporter (Gluconate permease 3) (Gnt-III system) | Cell_inner_membrane | R_FRUURt2rpp_enzyme R_GLCNt2rpp_duplicate_2_enzyme |
R_FRUURt2rpp R_GLCNt2rpp_duplicate_2 |
447 | Secretion: 447.0, Translation: 447.0, Folding: 44.7 | 47,138 | UniprotID: P0AC94 | FUNCTION: High-affinity gluconate transporter with fairly broad specificity, including low affinity for glucuronate, several disaccharides, and some hexoses, but not glucose. | |
| b1492 | b1492 | Probable glutamate/gamma-aminobutyrate antiporter (Extreme acid sensitivity protein) | Cell_inner_membrane | R_GLUABUTt7pp_enzyme | R_GLUABUTt7pp | 511 | Secretion: 511.0, Translation: 511.0, Folding: 51.1 | 55,077 | UniprotID: P63235 | FUNCTION: Involved in glutamate-dependent acid resistance. Imports glutamate inside the cell while simultaneously exporting to the periplasm the GABA produced by GadA and GadB. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. |
|
| b1200 | b1200 | PEP-dependent dihydroxyacetone kinase, dihydroxyacetone-binding subunit DhaK (EC 2.7.1.121) | Cytoplasm | R_DHAPT_enzyme | R_DHAPT | 356 | Translation: 356.0, Folding: 35.6 | 38,215 | UniprotID: P76015 ECnumber: EC 2.7.1.121 |
FUNCTION: Dihydroxyacetone binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone via a phosphoryl group transfer from DhaL-ATP (PubMed:15476397). Binds covalently dihydroxyacetone in hemiaminal linkage (PubMed:15476397). DhaK acts also as corepressor of the transcription activator DhaR by binding to the sensor domain of DhaR (PubMed:24440518). In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity (PubMed:24440518). In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR (PubMed:24440518). {ECO:0000269|PubMed:15476397, ECO:0000269|PubMed:24440518}. |
|
| b1206 | b1206 | C4-dicarboxylic acid transporter DauA (Dicarboxylic acid uptake system A) | Cell_inner_membrane | R_SO4t2pp_enzyme | R_SO4t2pp | 559 | Secretion: 559.0, Translation: 559.0, Folding: 55.9 | 59,429 | UniprotID: P0AFR2 | FUNCTION: Responsible for the aerobic transport of succinate from the periplasm to the cytoplasm at acidic pH. Can transport other C4-dicarboxylic acids such as aspartate and fumarate. May also play a role in the regulation of C4-dicarboxylic acid metabolism at pH 7, via regulation of expression and/or activity of DctA. May act as a co-sensor of DcuS. {ECO:0000269|PubMed:23278959}. | |
| b1207 | b1207 | Ribose-phosphate pyrophosphokinase (RPPK) (EC 2.7.6.1) (5-phospho-D-ribosyl alpha-1-diphosphate) (Phosphoribosyl diphosphate synthase) (Phosphoribosyl pyrophosphate synthase) (P-Rib-PP synthase) (PRPP synthase) (PRPPase) | Cytoplasm | R_PRPPS_enzyme | R_PRPPS | 315 | Translation: 315.0, Folding: 31.5 | 34,218 | UniprotID: P0A717 ECnumber: EC 2.7.6.1 |
FUNCTION: Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P). {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10954724, ECO:0000269|PubMed:2542328, ECO:0000269|PubMed:3009477, ECO:0000269|PubMed:6290219, ECO:0000269|PubMed:7657655, ECO:0000269|PubMed:8679571, ECO:0000269|PubMed:9125530}. |
|
| b1198 | b1198 | Protein-lysine deacetylase (EC 3.5.1.-) (Dihydroxyacetone kinase subunit M) (Lysine deacetylase) (KDAC) (PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM) | Cytoplasm | R_DHAPT_enzyme | R_DHAPT | 472 | Translation: 472.0, Folding: 47.2 | 51,449 | UniprotID: P37349 ECnumber: EC 3.5.1.- |
FUNCTION: Protein deacetylase that removes acetyl groups on specific lysine residues in target proteins. Regulates transcription by catalyzing deacetylation of Lys-52 and Lys-62 of the transcriptional repressor RutR. Is also able to deacetylate NhoA and RluC in vitro. Targets a distinct set of substrates compared to CobB. {ECO:0000269|PubMed:26716769}.; FUNCTION: Component of the dihydroxyacetone kinase complex, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone. DhaM serves as the phosphoryl donor. Is phosphorylated by phosphoenolpyruvate in an EI- and HPr-dependent reaction, and a phosphorelay system on histidine residues finally leads to phosphoryl transfer to DhaL and dihydroxyacetone. {ECO:0000269|PubMed:11350937}. |
|
| b1199 | b1199 | PEP-dependent dihydroxyacetone kinase, ADP-binding subunit DhaL (EC 2.7.1.121) | Cytoplasm | R_DHAPT_enzyme | R_DHAPT | 210 | Translation: 210.0, Folding: 21.0 | 22,632 | UniprotID: P76014 ECnumber: EC 2.7.1.121 |
FUNCTION: ADP-binding subunit of the dihydroxyacetone kinase, which is responsible for the phosphoenolpyruvate (PEP)-dependent phosphorylation of dihydroxyacetone (PubMed:11350937). DhaL-ADP is converted to DhaL-ATP via a phosphoryl group transfer from DhaM and transmits it to dihydroxyacetone binds to DhaK (PubMed:11350937). DhaL acts also as coactivator of the transcription activator DhaR by binding to the sensor domain of DhaR (PubMed:15616579). In the presence of dihydroxyacetone, DhaL-ADP displaces DhaK and stimulates DhaR activity (PubMed:15616579). In the absence of dihydroxyacetone, DhaL-ADP is converted by the PTS to DhaL-ATP, which does not bind to DhaR (PubMed:15616579). {ECO:0000269|PubMed:11350937, ECO:0000269|PubMed:15616579}. |
|
| b1192 | b1192 | Murein tetrapeptide carboxypeptidase (EC 3.4.17.13) (LD-carboxypeptidase A) (Muramoyltetrapeptide carboxypeptidase) | Cytoplasm | R_4PCP_enzyme R_AGM4PCP_enzyme R_AM4PCP_enzyme R_UM4PCP_enzyme |
R_4PCP R_AGM4PCP R_AM4PCP R_UM4PCP |
304 | Translation: 304.0, Folding: 30.4 | 33,567 | UniprotID: P76008 ECnumber: EC 3.4.17.13 |
FUNCTION: Releases the terminal D-alanine residue from the cytoplasmic tetrapeptide recycling product L-Ala-gamma-D-Glu-meso-Dap-D-Ala. To a lesser extent, can also cleave D-Ala from murein derivatives containing the tetrapeptide, i.e. MurNAc-tetrapeptide, UDP-MurNAc-tetrapeptide, GlcNAc-MurNAc-tetrapeptide, and GlcNAc-anhMurNAc-tetrapeptide. Does not act on murein sacculi or cross-linked muropeptides. The tripeptides produced by the LcdA reaction can then be reused as peptidoglycan building blocks; LcdA is thereby involved in murein recycling. Is also essential for viability during stationary phase. {ECO:0000269|PubMed:10428950, ECO:0000269|PubMed:18535144}. |
|
| b1193 | b1193 | Endo-type membrane-bound lytic murein transglycosylase A (EC 4.2.2.n2) (Peptidoglycan lytic endotransglycosylase) | Cell_outer_membrane | R_MLTGY1pp_duplicate_6_enzyme R_MLTGY2pp_duplicate_3_enzyme R_MLTGY3pp_duplicate_3_enzyme R_MLTGY4pp_duplicate_4_enzyme |
R_MLTGY1pp_duplicate_6 R_MLTGY2pp_duplicate_3 R_MLTGY3pp_duplicate_3 R_MLTGY4pp_duplicate_4 |
203 | Secretion: 203.0, Translation: 203.0, Folding: 20.3 | 22,227 | UniprotID: P0C960 ECnumber: EC 4.2.2.n2 |
FUNCTION: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Preferentially cleaves at a distance of more than two disaccharide units from the ends of the glycan chain. Prefers cross-linked murein in vivo. | |
| b1190 | b1190 | Alanine racemase, catabolic (EC 5.1.1.1) | Cytoplasm | R_ALAR_enzyme | R_ALAR | 356 | Translation: 356.0, Folding: 35.6 | 38,845 | UniprotID: P29012 ECnumber: EC 5.1.1.1 |
FUNCTION: Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. {ECO:0000250}. | |
| b1197 | b1197 | Periplasmic trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) (Tre37A) | Periplasm | R_TREHpp_enzyme | R_TREHpp | 565 | Secretion: 565.0, Translation: 565.0, Folding: 56.5 | 63,637 | UniprotID: P13482 ECnumber: EC 3.2.1.28 |
FUNCTION: Provides the cells with the ability to utilize trehalose at high osmolarity by splitting it into glucose molecules that can subsequently be taken up by the phosphotransferase-mediated uptake system. | |
| b0420 | b0420 | 1-deoxy-D-xylulose-5-phosphate synthase (EC 2.2.1.7) (1-deoxyxylulose-5-phosphate synthase) (DXP synthase) (DXPS) | Cytoplasm | R_DXPS_enzyme | R_DXPS | 620 | Translation: 620.0, Folding: 62.0 | 67,617 | UniprotID: P77488 ECnumber: EC 2.2.1.7 |
FUNCTION: Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D-xylulose-5-phosphate (DXP). {ECO:0000269|PubMed:17135236}. | |
| b0822 | b0822 | Sugar phosphatase YbiV (EC 3.1.3.23) | Cytoplasm | R_F6PP_enzyme R_G3PT_enzyme R_G6PP_enzyme R_MN6PP_enzyme R_R5PP_enzyme |
R_F6PP R_G3PT R_G6PP R_MN6PP R_R5PP |
271 | Translation: 271.0, Folding: 27.1 | 30,413 | UniprotID: P75792 ECnumber: EC 3.1.3.23 |
FUNCTION: Catalyzes the hydrolysis of sugar phosphate to sugar and inorganic phosphate. Has a wide substrate specificity catalyzing the hydrolysis of ribose-5-phosphate, glucose-6-phosphate, fructose-1-phosphate, acetyl-phosphate, glycerol-1-phosphate, glycerol-2-phosphate, 2-deoxy-glucose-6-phosphate, mannose-6-phosphate and fructose-6-phosphate. Appears to have a low level of phosphotransferase activity using monophosphates as the phosphate donor. {ECO:0000269|PubMed:15657928, ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16990279}. |
|
| b0825 | b0825 | Fructose-6-phosphate aldolase 1 (EC 4.1.2.-) (Fructose-6-phosphate aldolase A) (FSAA) | Cytoplasm | R_F6PA_enzyme | R_F6PA | 220 | Translation: 220.0, Folding: 22.0 | 22,997 | UniprotID: P78055 ECnumber: EC 4.1.2.- |
FUNCTION: Catalyzes the reversible formation of fructose 6-phosphate from dihydroxyacetone (DHA) and D-glyceraldehyde 3-phosphate via an aldolization reaction. Can utilize several aldehydes as acceptor compounds in vitro, and hydroxyacetone (HA) or 1-hydroxy-butan-2-one as alternative donor substrate. Is also able to catalyze the direct stereoselective self-aldol addition of glycolaldehyde to furnish D-(-)-threose, and cross-aldol reactions of glycolaldehyde to other aldehyde acceptors. Is not able to cleave fructose, fructose 1-phosphate, glucose 6-phosphate, sedoheptulose 1,7-bisphosphate, xylulose 5-phosphate, ribulose 5-phosphate, and fructose 1,6-bisphosphate; cannot use dihydroxyacetone phosphate as donor compound nor D-glyceraldehyde as acceptor. Does not display transaldolase activity. {ECO:0000269|PubMed:11120740, ECO:0000269|PubMed:17985886, ECO:0000269|PubMed:19554584, ECO:0000269|Ref.6}. |
|
| b0423 | b0423 | tRNA sulfurtransferase (EC 2.8.1.4) (Sulfur carrier protein ThiS sulfurtransferase) (Thiamine biosynthesis protein ThiI) (tRNA 4-thiouridine synthase) | Cytoplasm | R_THZPSN3_enzyme | R_THZPSN3 | 482 | Translation: 482.0, Folding: 48.2 | 54,973 | UniprotID: P77718 ECnumber: EC 2.8.1.4 |
FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. {ECO:0000269|PubMed:10722656, ECO:0000269|PubMed:10753862, ECO:0000269|PubMed:18604845}. |
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| b0827 | b0827 | Molybdopterin molybdenumtransferase (MPT Mo-transferase) (EC 2.10.1.1) | Cytoplasm | R_BMOCOS_enzyme R_BWCOS_enzyme R_MOCOS_enzyme R_WCOS_enzyme |
R_BMOCOS R_BWCOS R_MOCOS R_WCOS |
411 | Translation: 411.0, Folding: 41.1 | 44,067 | UniprotID: P12281 ECnumber: EC 2.10.1.1 |
FUNCTION: Catalyzes the insertion of molybdate into adenylated molybdopterin with the concomitant release of AMP. {ECO:0000269|PubMed:15632135}. | |
| b0826 | b0826 | Molybdopterin-synthase adenylyltransferase (EC 2.7.7.80) (MoaD protein adenylase) (Molybdopterin-converting factor subunit 1 adenylase) (Sulfur carrier protein MoaD adenylyltransferase) | Cytoplasm | R_MPTSS_enzyme | R_MPTSS | 249 | Translation: 249.0, Folding: 24.9 | 26,719 | UniprotID: P12282 ECnumber: EC 2.7.7.80 |
FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD. {ECO:0000269|PubMed:11290749, ECO:0000269|PubMed:11463785}. | |
| b0829 | b0829 | Glutathione import ATP-binding protein GsiA (EC 3.6.3.-) | Cell_inner_membrane | R_GTHRDabcpp_enzyme | R_GTHRDabcpp | 623 | Secretion: 623.0, Translation: 623.0, Folding: 62.3 | 69,114 | UniprotID: P75796 ECnumber: EC 3.6.3.- |
FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. Responsible for energy coupling to the transport system. {ECO:0000269|PubMed:16109926}. | |
| b0828 | b0828 | Isoaspartyl peptidase (EC 3.4.19.5) (Beta-aspartyl-peptidase) (EcAIII) (Isoaspartyl dipeptidase) [Cleaved into: Isoaspartyl peptidase subunit alpha; Isoaspartyl peptidase subunit beta | Cytoplasm | R_ASNN_duplicate_2_enzyme | R_ASNN_duplicate_2 | 321 | Translation: 321.0, Folding: 32.1 | 33,394 | UniprotID: P37595 ECnumber: EC 3.4.19.5 |
FUNCTION: Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function. {ECO:0000269|PubMed:11988085}.; FUNCTION: May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption. {ECO:0000269|PubMed:11988085}. |
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| b1849 | b1849 | Formate-dependent phosphoribosylglycinamide formyltransferase (5-phosphoribosylglycinamide transformylase 2) (Formate-dependent GAR transformylase) (EC 2.1.2.-) (GAR transformylase 2) (GART 2) (Non-folate glycinamide ribonucleotide transformylase) (Phosphoribosylglycinamide formyltransferase 2) | Cytoplasm | R_ACKr_duplicate_3_enzyme R_GART_enzyme |
R_ACKr_duplicate_3 R_GART |
392 | Translation: 392.0, Folding: 39.2 | 42,434 | UniprotID: P33221 ECnumber: EC 2.1.2.- |
FUNCTION: Involved in the de novo purine biosynthesis. Catalyzes the transfer of formate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR). Formate is provided by PurU via hydrolysis of 10-formyl-tetrahydrofolate. PurT is also able to cleave acetyl phosphate and carbamoyl phosphate to produce ATP with acetate and carbamate, respectively. {ECO:0000269|PubMed:8117714, ECO:0000269|PubMed:9184151}. |
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| b1661 | b1661 | Cyclopropane-fatty-acyl-phospholipid synthase (CFA synthase) (Cyclopropane fatty acid synthase) (EC 2.1.1.79) | Cytoplasm | R_CFAS160E_enzyme R_CFAS160G_enzyme R_CFAS180E_enzyme R_CFAS180G_enzyme |
R_CFAS160E R_CFAS160G R_CFAS180E R_CFAS180G |
382 | Translation: 382.0, Folding: 38.2 | 43,909 | UniprotID: P0A9H7 ECnumber: EC 2.1.1.79 |
FUNCTION: Transfers a methylene group from S-adenosyl-L-methionine to the cis double bond of an unsaturated fatty acid chain resulting in the replacement of the double bond with a methylene bridge. {ECO:0000250}. | |
| b1662 | b1662 | Riboflavin synthase (RS) (EC 2.5.1.9) | Cytoplasm | R_RBFSa_enzyme | R_RBFSa | 213 | Translation: 213.0, Folding: 21.3 | 23,445 | UniprotID: P0AFU8 ECnumber: EC 2.5.1.9 |
FUNCTION: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil. {ECO:0000269|PubMed:9022701}. | |
| b1440 | b1440 | Putative ABC transporter periplasmic-binding protein YdcS | Periplasm | R_PTRCabcpp_duplicate_3_enzyme R_SPMDabcpp_duplicate_2_enzyme |
R_PTRCabcpp_duplicate_3 R_SPMDabcpp_duplicate_2 |
381 | Secretion: 381.0, Translation: 381.0, Folding: 38.1 | 42,295 | UniprotID: P76108 | FUNCTION: Probably part of the binding-protein-dependent transport system YdcSTUV. | |
| b1441 | b1441 | Uncharacterized ABC transporter ATP-binding protein YdcT | Cytoplasm | R_PTRCabcpp_duplicate_3_enzyme R_SPMDabcpp_duplicate_2_enzyme |
R_PTRCabcpp_duplicate_3 R_SPMDabcpp_duplicate_2 |
337 | Translation: 337.0, Folding: 33.7 | 37,041 | UniprotID: P77795 | FUNCTION: Probably part of a binding-protein-dependent transport system YdcSTUV. Probably responsible for energy coupling to the transport system. | |
| b1442 | b1442 | Inner membrane ABC transporter permease protein YdcU | Cell_inner_membrane | R_PTRCabcpp_duplicate_3_enzyme R_SPMDabcpp_duplicate_2_enzyme |
R_PTRCabcpp_duplicate_3 R_SPMDabcpp_duplicate_2 |
313 | Secretion: 313.0, Translation: 313.0, Folding: 31.3 | 34,360 | UniprotID: P77156 | FUNCTION: Probably part of the binding-protein-dependent transport system YdcSTUV; probably responsible for the translocation of the substrate across the membrane. | |
| b1443 | b1443 | Inner membrane ABC transporter permease protein YdcV | Cell_inner_membrane | R_PTRCabcpp_duplicate_3_enzyme R_SPMDabcpp_duplicate_2_enzyme |
R_PTRCabcpp_duplicate_3 R_SPMDabcpp_duplicate_2 |
264 | Secretion: 264.0, Translation: 264.0, Folding: 26.4 | 28,722 | UniprotID: P0AFR9 | FUNCTION: Probably part of the binding-protein-dependent transport system YdcSTUV; probably responsible for the translocation of the substrate across the membrane. | |
| b1444 | b1444 | Gamma-aminobutyraldehyde dehydrogenase (EC 1.2.1.19) (1-pyrroline dehydrogenase) (4-aminobutanal dehydrogenase) (ABALDH) | Cytoplasm | R_ABUTD_enzyme | R_ABUTD | 474 | Translation: 474.0, Folding: 47.4 | 50,830 | UniprotID: P77674 ECnumber: EC 1.2.1.19 |
FUNCTION: Catalyzes the oxidation of 1-pyrroline, which is spontaneously formed from 4-aminobutanal, leading to 4-aminobutanoate (GABA). Can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency. {ECO:0000269|PubMed:15381418, ECO:0000269|PubMed:16023116}. | |
| b0133 | b0133 | Pantothenate synthetase (PS) (EC 6.3.2.1) (Pantoate--beta-alanine ligase) (Pantoate-activating enzyme) | Cytoplasm | R_PANTS_enzyme | R_PANTS | 283 | Translation: 283.0, Folding: 28.3 | 31,598 | UniprotID: P31663 ECnumber: EC 6.3.2.1 |
FUNCTION: Catalyzes the condensation of pantoate with beta-alanine in an ATP-dependent reaction via a pantoyl-adenylate intermediate. {ECO:0000269|PubMed:357689}. | |
| b0131 | b0131 | Aspartate 1-decarboxylase (EC 4.1.1.11) (Aspartate alpha-decarboxylase) [Cleaved into: Aspartate 1-decarboxylase beta chain; Aspartate 1-decarboxylase alpha chain | Cytoplasm | R_ASP1DC_enzyme | R_ASP1DC | 126 | Translation: 126.0, Folding: 12.6 | 13,834 | UniprotID: P0A790 ECnumber: EC 4.1.1.11 |
FUNCTION: Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine. {ECO:0000269|PubMed:6767707}. | |
| b0134 | b0134 | 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) (Ketopantoate hydroxymethyltransferase) (KPHMT) | Cytoplasm | R_MOHMT_enzyme | R_MOHMT | 264 | Translation: 264.0, Folding: 26.4 | 28,237 | UniprotID: P31057 ECnumber: EC 2.1.2.11 |
FUNCTION: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate. {ECO:0000269|PubMed:776976}. | |
| b1684 | b1684 | Protein SufA | Cytoplasm | R_S2FE2ST_enzyme R_S4FE4ST_enzyme |
R_S2FE2ST R_S4FE4ST |
122 | Translation: 122.0, Folding: 12.2 | 13,300 | UniprotID: P77667 | ||
| b1682 | b1682 | Probable ATP-dependent transporter SufC | Cytoplasm | R_S2FE2SR_enzyme R_S2FE2SS_enzyme R_S2FE2SS2_enzyme R_S2FE2ST_enzyme R_S4FE4SR_enzyme R_S4FE4ST_enzyme |
R_S2FE2SR R_S2FE2SS R_S2FE2SS2 R_S2FE2ST R_S4FE4SR R_S4FE4ST |
248 | Translation: 248.0, Folding: 24.8 | 27,582 | UniprotID: P77499 | FUNCTION: Has low ATPase activity. The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. {ECO:0000269|PubMed:12554644, ECO:0000269|PubMed:12941942}. |
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| b1683 | b1683 | FeS cluster assembly protein SufB | Cytoplasm | R_S2FE2SR_enzyme R_S2FE2SS_enzyme R_S2FE2SS2_enzyme R_S2FE2ST_enzyme R_S4FE4SR_enzyme R_S4FE4ST_enzyme |
R_S2FE2SR R_S2FE2SS R_S2FE2SS2 R_S2FE2ST R_S4FE4SR R_S4FE4ST |
495 | Translation: 495.0, Folding: 49.5 | 54,745 | UniprotID: P77522 | FUNCTION: The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. {ECO:0000269|PubMed:12941942}. | |
| b1680 | b1680 | Cysteine desulfurase (EC 2.8.1.7) (Selenocysteine beta-lyase) (SCL) (Selenocysteine lyase) (EC 4.4.1.16) (Selenocysteine reductase) | Cytoplasm | R_S2FE2SR_enzyme R_S2FE2SS_enzyme R_S2FE2SS2_enzyme R_SCYSDS_enzyme |
R_S2FE2SR R_S2FE2SS R_S2FE2SS2 R_SCYSDS |
406 | Translation: 406.0, Folding: 40.6 | 44,434 | UniprotID: P77444 ECnumber: EC 2.8.1.7; 4.4.1.16 |
FUNCTION: Cysteine desulfurases mobilize the sulfur from L-cysteine to yield L-alanine, an essential step in sulfur metabolism for biosynthesis of a variety of sulfur-containing biomolecules. Component of the suf operon, which is activated and required under specific conditions such as oxidative stress and iron limitation. Acts as a potent selenocysteine lyase in vitro, that mobilizes selenium from L-selenocysteine. Selenocysteine lyase activity is however unsure in vivo. {ECO:0000269|PubMed:10829016, ECO:0000269|PubMed:11997471, ECO:0000269|PubMed:12089140, ECO:0000269|PubMed:12876288, ECO:0000269|PubMed:12941942}. |
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| b1681 | b1681 | FeS cluster assembly protein SufD | Cytoplasm | R_S2FE2SR_enzyme R_S2FE2SS_enzyme R_S2FE2SS2_enzyme R_S2FE2ST_enzyme R_S4FE4SR_enzyme R_S4FE4ST_enzyme |
R_S2FE2SR R_S2FE2SS R_S2FE2SS2 R_S2FE2ST R_S4FE4SR R_S4FE4ST |
423 | Translation: 423.0, Folding: 42.3 | 46,823 | UniprotID: P77689 | FUNCTION: The SufBCD complex acts synergistically with SufE to stimulate the cysteine desulfurase activity of SufS. The SufBCD complex contributes to the assembly or repair of oxygen-labile iron-sulfur clusters under oxidative stress. May facilitate iron uptake from extracellular iron chelators under iron limitation. Required for the stability of the FhuF protein. {ECO:0000269|PubMed:10322040, ECO:0000269|PubMed:12941942}. |
|
| b4254 | b4254 | Ornithine carbamoyltransferase subunit I (OTCase-1) (EC 2.1.3.3) | Cytoplasm | R_OCBT_enzyme | R_OCBT | 334 | Translation: 334.0, Folding: 33.4 | 36,907 | UniprotID: P04391 ECnumber: EC 2.1.3.3 |
FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. {ECO:0000269|PubMed:3072022, ECO:0000269|PubMed:789338}. | |
| b0628 | b0628 | Lipoyl synthase (EC 2.8.1.8) (Lip-syn) (LS) (Lipoate synthase) (Lipoic acid synthase) (Sulfur insertion protein LipA) | Cytoplasm | R_LIPOS_enzyme | R_LIPOS | 321 | Translation: 321.0, Folding: 32.1 | 36,072 | UniprotID: P60716 ECnumber: EC 2.8.1.8 |
FUNCTION: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives. Free octanoate is not a substrate for LipA. {ECO:0000269|PubMed:11106496, ECO:0000269|PubMed:14700636, ECO:0000269|PubMed:15157071}. | |
| b0622 | b0622 | Lipid A palmitoyltransferase PagP (EC 2.3.1.251) (Lipid A acylation protein) | Cell_outer_membrane | R_LIPAHT2ex_enzyme R_LIPAHTex_enzyme |
R_LIPAHT2ex R_LIPAHTex |
186 | Secretion: 186.0, Translation: 186.0, Folding: 18.6 | 21,770 | UniprotID: P37001 ECnumber: EC 2.3.1.251 |
FUNCTION: Transfers a palmitate residue from the sn-1 position of a phospholipid to the N-linked hydroxymyristate on the proximal unit of lipid A or its precursors. Phosphatidylglycerol (PtdGro), phosphatidylethanolamine (PtdEtn), phosphatidylserine (PtdSer) and phosphatidic acid (Ptd-OH) are all effective acyl donors. {ECO:0000269|PubMed:11013210, ECO:0000269|PubMed:20826347, ECO:0000269|PubMed:20853818}. |
|
| b0621 | b0621 | Anaerobic C4-dicarboxylate transporter DcuC | Cell_inner_membrane | R_FUMt2_3pp_duplicate_3_enzyme R_SUCASPtpp_duplicate_3_enzyme R_SUCFUMtpp_enzyme R_SUCMALtpp_duplicate_3_enzyme |
R_FUMt2_3pp_duplicate_3 R_SUCASPtpp_duplicate_3 R_SUCFUMtpp R_SUCMALtpp_duplicate_3 |
461 | Secretion: 461.0, Translation: 461.0, Folding: 46.1 | 48,412 | UniprotID: P0ABP3 | FUNCTION: Responsible for the transport of C4-dicarboxylates during anaerobic growth. {ECO:0000269|PubMed:10368146}. | |
| b0007 | b0007 | Uncharacterized transporter YaaJ | Cell_inner_membrane | R_ALAt4pp_enzyme R_GLYt4pp_enzyme |
R_ALAt4pp R_GLYt4pp |
476 | Secretion: 476.0, Translation: 476.0, Folding: 47.6 | 51,663 | UniprotID: P30143 | ||
| b0004 | b0004 | Threonine synthase (TS) (EC 4.2.3.1) | Cytoplasm | R_4HTHRS_enzyme R_THRS_enzyme |
R_4HTHRS R_THRS |
428 | Translation: 428.0, Folding: 42.8 | 47,114 | UniprotID: P00934 ECnumber: EC 4.2.3.1 |
FUNCTION: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine. To a lesser extent, is able to slowly catalyze the deamination of L-threonine into alpha-ketobutyrate and that of L-serine and 3-chloroalanine into pyruvate. Is also able to rapidly convert vinylglycine to threonine, which proves that the pyridoxal p-quinonoid of vinylglycine is an intermediate in the TS reaction. {ECO:0000269|PubMed:7907888}. |
|
| b0003 | b0003 | Homoserine kinase (HK) (HSK) (EC 2.7.1.39) | Cytoplasm | R_HSK_enzyme | R_HSK | 310 | Translation: 310.0, Folding: 31.0 | 33,624 | UniprotID: P00547 ECnumber: EC 2.7.1.39 |
FUNCTION: Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate. Is also able to phosphorylate the hydroxy group on gamma-carbon of L-homoserine analogs when the functional group at the alpha-position is a carboxyl, an ester, or even a hydroxymethyl group. Neither L-threonine nor L-serine are substrates of the enzyme. {ECO:0000269|PubMed:8973190}. | |
| b0002 | b0002 | Bifunctional aspartokinase/homoserine dehydrogenase 1 (Aspartokinase I/homoserine dehydrogenase I) (AKI-HDI) [Includes: Aspartokinase (EC 2.7.2.4); Homoserine dehydrogenase (EC 1.1.1.3) | Cytoplasm | R_ASPK_duplicate_2_enzyme R_HSDy_duplicate_2_enzyme |
R_ASPK_duplicate_2 R_HSDy_duplicate_2 |
820 | Translation: 820.0, Folding: 82.0 | 89,120 | UniprotID: P00561 ECnumber: EC 2.7.2.4; 1.1.1.3 |
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| b0009 | b0009 | Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) | Cytoplasm | R_MPTAT_enzyme | R_MPTAT | 195 | Translation: 195.0, Folding: 19.5 | 21,222 | UniprotID: P0AF03 ECnumber: EC 2.7.7.75 |
FUNCTION: Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor. {ECO:0000269|PubMed:15632135}. | |
| b0008 | b0008 | Transaldolase B (EC 2.2.1.2) | Cytoplasm | R_TALA_duplicate_2_enzyme | R_TALA_duplicate_2 | 317 | Translation: 317.0, Folding: 31.7 | 35,219 | UniprotID: P0A870 ECnumber: EC 2.2.1.2 |
FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. {ECO:0000269|PubMed:7592346}. | |
| b4079 | b4079 | Formate dehydrogenase H (EC 1.17.1.9) (EC 1.17.99.7) (Formate dehydrogenase-H subunit alpha) (FDH-H) (Formate-hydrogen-lyase-linked, selenocysteine-containing polypeptide) | Cytoplasm | R_FHL_enzyme R_FHL_duplicate_2_enzyme |
R_FHL R_FHL_duplicate_2 |
715 | Translation: 714.0, Folding: 71.4 | 79,374 | UniprotID: P07658 ECnumber: EC 1.17.1.9; 1.17.99.7 |
FUNCTION: Decomposes formic acid to hydrogen and carbon dioxide under anaerobic conditions in the absence of exogenous electron acceptors. | |
| b1539 | b1539 | NADP-dependent 3-hydroxy acid dehydrogenase YdfG (L-allo-threonine dehydrogenase) (EC 1.1.1.381) (Malonic semialdehyde reductase) (EC 1.1.1.298) | Cytoplasm | R_ATHRDHr_enzyme R_DSERDHr_enzyme R_LSERDHr_enzyme R_MSAR_duplicate_2_enzyme |
R_ATHRDHr R_DSERDHr R_LSERDHr R_MSAR_duplicate_2 |
248 | Translation: 248.0, Folding: 24.8 | 27,249 | UniprotID: P39831 ECnumber: EC 1.1.1.381; 1.1.1.298 |
FUNCTION: NADP-dependent dehydrogenase with broad substrate specificity acting on 3-hydroxy acids. Catalyzes the NADP-dependent oxidation of L-allo-threonine to L-2-amino-3-keto-butyrate, which is spontaneously decarboxylated into aminoacetone. Also acts on D-threonine, L-serine, D-serine, D-3-hydroxyisobutyrate, L-3-hydroxyisobutyrate, D-glycerate and L-glycerate (PubMed:12535615). Able to catalyze the reduction of the malonic semialdehyde to 3-hydroxypropionic acid. YdfG is apparently supplementing RutE, the presumed malonic semialdehyde reductase involved in pyrimidine degradation since both are able to detoxify malonic semialdehyde (PubMed:20400551). {ECO:0000269|PubMed:12535615, ECO:0000269|PubMed:20400551}. |
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| b4072 | b4072 | Protein NrfC | Cytoplasm | R_NTRIR3pp_enzyme R_NTRIR4pp_enzyme |
R_NTRIR3pp R_NTRIR4pp |
223 | Translation: 223.0, Folding: 22.3 | 24,567 | UniprotID: P0AAK7 | FUNCTION: Probably involved in the transfer of electrons from the quinone pool to the type-c cytochromes. | |
| b4073 | b4073 | Protein NrfD | Cell_inner_membrane | R_NTRIR3pp_enzyme R_NTRIR4pp_enzyme |
R_NTRIR3pp R_NTRIR4pp |
318 | Secretion: 318.0, Translation: 318.0, Folding: 31.8 | 35,042 | UniprotID: P32709 | FUNCTION: Probably involved in the transfer of electrons from the quinone pool to the type-c cytochromes. | |
| b4070 | b4070 | Cytochrome c-552 (EC 1.7.2.2) (Ammonia-forming cytochrome c nitrite reductase) (Cytochrome c nitrite reductase) | Periplasm | R_NTRIR3pp_enzyme R_NTRIR4pp_enzyme |
R_NTRIR3pp R_NTRIR4pp |
478 | Secretion: 478.0, Translation: 478.0, Folding: 47.8 | 53,703 | UniprotID: P0ABK9 ECnumber: EC 1.7.2.2 |
FUNCTION: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process (PubMed:9593308, PubMed:11863430, PubMed:18311941, PubMed:20629638). Has very low activity toward hydroxylamine (PubMed:11863430). Has even lower activity toward sulfite (PubMed:20629638). Sulfite reductase activity is maximal at neutral pH (By similarity). {ECO:0000250|UniProtKB:L0DSL2, ECO:0000269|PubMed:11863430, ECO:0000269|PubMed:18311941, ECO:0000269|PubMed:20629638, ECO:0000269|PubMed:9593308, ECO:0000305|PubMed:7934939}. |
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| b4071 | b4071 | Cytochrome c-type protein NrfB | Periplasm | R_NTRIR3pp_enzyme R_NTRIR4pp_enzyme |
R_NTRIR3pp R_NTRIR4pp |
188 | Secretion: 188.0, Translation: 188.0, Folding: 18.8 | 20,714 | UniprotID: P0ABL1 | FUNCTION: Plays a role in nitrite reduction. | |
| b4077 | b4077 | Proton/glutamate-aspartate symporter (Glutamate-aspartate carrier protein) (Proton-glutamate-aspartate transport protein) | Cell_inner_membrane | R_ASPt2pp_copy1_enzyme R_GLUt2rpp_enzyme |
R_ASPt2pp_copy1 R_GLUt2rpp |
437 | Secretion: 437.0, Translation: 437.0, Folding: 43.7 | 47,159 | UniprotID: P21345 | FUNCTION: Catalyzes the proton-dependent, binding-protein-independent transport of glutamate and aspartate. {ECO:0000269|PubMed:1971622, ECO:0000269|PubMed:2537813, ECO:0000269|PubMed:336628, ECO:0000269|PubMed:8596452}. | |
| b1533 | b1533 | Probable amino-acid metabolite efflux pump | Cell_inner_membrane | R_ACSERtpp_duplicate_2_enzyme R_CYStpp_duplicate_2_enzyme |
R_ACSERtpp_duplicate_2 R_CYStpp_duplicate_2 |
299 | Secretion: 299.0, Translation: 299.0, Folding: 29.9 | 32,324 | UniprotID: P31125 | FUNCTION: May be an export pump for cysteine and other metabolites of the cysteine pathway (such as N-acetyl-L-serine (NAS) and O-acetyl-L-serine (OAS)), and for other amino acids and their metabolites. {ECO:0000269|PubMed:10844694, ECO:0000269|Ref.6}. | |
| b0480 | b0480 | Protein UshA [Includes: UDP-sugar hydrolase (EC 3.6.1.45) (UDP-sugar diphosphatase) (UDP-sugar pyrophosphatase); 5-nucleotidase (5-NT) (EC 3.1.3.5) | Periplasm | 550 | Secretion: 550.0, Translation: 550.0, Folding: 55.0 | 60,824 | UniprotID: P07024 ECnumber: EC 3.6.1.45; 3.1.3.5 |
FUNCTION: Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell. | |||
| b0954 | b0954 | 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59) (3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA) (Beta-hydroxydecanoyl thioester dehydrase) (Trans-2-decenoyl-[acyl-carrier-protein] isomerase) (EC 5.3.3.14) | Cytoplasm | 172 | Translation: 172.0, Folding: 17.2 | 18,969 | UniprotID: P0A6Q3 ECnumber: EC 4.2.1.59; 5.3.3.14 |
FUNCTION: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP. {ECO:0000269|PubMed:8910376}. |
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| b0485 | b0485 | Glutaminase 1 (EC 3.5.1.2) | Cytoplasm | R_GLUN_enzyme | R_GLUN | 310 | Translation: 310.0, Folding: 31.0 | 32,903 | UniprotID: P77454 ECnumber: EC 3.5.1.2 |
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| b0484 | b0484 | Copper-exporting P-type ATPase (EC 3.6.3.54) (Copper-exporting P-type ATPase A) (Cu(+)-exporting ATPase) (Soluble copper chaperone CopA(Z)) | Cell_inner_membrane | R_CU1abcpp_enzyme | R_CU1abcpp | 834 | Secretion: 834.0, Translation: 834.0, Folding: 83.4 | 87,873 | UniprotID: Q59385 ECnumber: EC 3.6.3.54 |
FUNCTION: Copper-exporting P-type ATPase: Exports Cu(+) from the cytoplasm to the periplasm (PubMed:10639134, PubMed:11167016, PubMed:11500054, PubMed:12351646). Binds 2 Cu(+) ions per monomer, which are transferred to periplasmic copper chaperone CusF upon ATP hydrolysis (PubMed:24917681). In vitro an excess of CusF over CopA is required for efficient transfer (PubMed:24917681). May also be involved in silver export (PubMed:12351646, PubMed:12832075). {ECO:0000269|PubMed:10639134, ECO:0000269|PubMed:11167016, ECO:0000269|PubMed:11500054, ECO:0000269|PubMed:12351646, ECO:0000269|PubMed:12832075, ECO:0000269|PubMed:24917681}.; FUNCTION: Soluble copper chaperone CopA(Z): mRNA is subject to programmed ribosomal frameshifting which produces a cytoplasmic copper chaperone CopA(Z) that corresponds to the first HMA domain (PubMed:28107647). The soluble form is essential for cell survivial in the presence of CuSO(4); in growth competition experiments between wild-type and a version that prevents expression of CopA(Z) after 50 generations the non-CopA(Z) version is nearly extinct (PubMed:28107647). The first HMA domain (residues 1-70) can be replaced by B.subtilis Cu chaperone CopZ (PubMed:25899340). {ECO:0000269|PubMed:25899340, ECO:0000269|PubMed:28107647}. |
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| b0312 | b0312 | NAD/NADP-dependent betaine aldehyde dehydrogenase (BADH) (EC 1.2.1.8) | Cytoplasm | R_BETALDHx_enzyme R_BETALDHy_enzyme |
R_BETALDHx R_BETALDHy |
490 | Translation: 490.0, Folding: 49.0 | 52,911 | UniprotID: P17445 ECnumber: EC 1.2.1.8 |
FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the reversible oxidation of betaine aldehyde to the corresponding acid. It is highly specific for betaine and has a significantly higher affinity for NAD than for NADP. {ECO:0000255|HAMAP-Rule:MF_00804, ECO:0000269|PubMed:2194570, ECO:0000269|PubMed:3512525}. | |
| b0311 | b0311 | Oxygen-dependent choline dehydrogenase (CDH) (CHD) (EC 1.1.99.1) (Betaine aldehyde dehydrogenase) (BADH) (EC 1.2.1.8) | Cell_inner_membrane | R_CHOLD_enzyme | R_CHOLD | 556 | Secretion: 556.0, Translation: 556.0, Folding: 55.6 | 61,878 | UniprotID: P17444 ECnumber: EC 1.1.99.1; 1.2.1.8 |
FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine betaine. Catalyzes the oxidation of choline to betaine aldehyde and betaine aldehyde to glycine betaine at the same rate. {ECO:0000255|HAMAP-Rule:MF_00750, ECO:0000269|PubMed:3512525, ECO:0000269|PubMed:3512526}. | |
| b0314 | b0314 | High-affinity choline transport protein | Cell_inner_membrane | R_CHLt2pp_enzyme | R_CHLt2pp | 677 | Secretion: 677.0, Translation: 677.0, Folding: 67.7 | 75,842 | UniprotID: P0ABC9 | FUNCTION: High-affinity uptake of choline driven by a proton-motive force. {ECO:0000269|PubMed:1956285}. | |
| b4476 | b4476 | Low-affinity gluconate transporter (Gluconate permease) (Gnt-I system) | Cell_inner_membrane | R_GLCNt2rpp_duplicate_3_enzyme | R_GLCNt2rpp_duplicate_3 | 446 | Secretion: 446.0, Translation: 446.0, Folding: 44.6 | 46,416 | UniprotID: P0AC96 | FUNCTION: Part of the gluconate utilization system Gnt-I; low-affinity intake of gluconate. | |
| b4477 | b4477 | 2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC 4.1.2.21) (2-oxo-3-deoxygalactonate 6-phosphate aldolase) (6-phospho-2-dehydro-3-deoxygalactonate aldolase) (6-phospho-2-keto-3-deoxygalactonate aldolase) (KDPGal) | Cytoplasm | R_DDPGALA_enzyme | R_DDPGALA | 205 | Translation: 205.0, Folding: 20.5 | 21,391 | UniprotID: Q6BF16 ECnumber: EC 4.1.2.21 |
FUNCTION: Involved in the degradation of galactose via the DeLey-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with re-facial selectivity. It can use a limited number of aldehyde substrates, including D-glyceraldehyde-3-phosphate (natural substrate), D-glyceraldehyde, glycolaldehyde, 2-pyridinecarboxaldehyde, D-ribose, D-erythrose and D-threose. It efficiently catalyzes aldol addition only using pyruvate as the nucleophilic component and accepts both stereochemical configurations at C2 of the electrophile. {ECO:0000269|PubMed:17981470, ECO:0000269|PubMed:324806}. |
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| b4474 | b4474 | Fructoselysine 3-epimerase (EC 5.1.3.-) | Cytoplasm | R_FRULYSE_enzyme | R_FRULYSE | 276 | Translation: 276.0, Folding: 27.6 | 31,169 | UniprotID: P45541 ECnumber: EC 5.1.3.- |
FUNCTION: Catalyzes the reversible interconversion of fructoselysine with its C-3 epimer, psicoselysine. Allows E.coli to utilize psicoselysine for growth. Does not act on psicose or fructoselysine 6-phosphate. {ECO:0000269|PubMed:14641112}. | |
| b4471 | b4471 | L-serine dehydratase TdcG (SDH) (EC 4.3.1.17) (L-serine deaminase) | Cytoplasm | R_SERD_L_duplicate_2_enzyme | R_SERD_L_duplicate_2 | 454 | Translation: 454.0, Folding: 45.4 | 48,522 | UniprotID: P42630 ECnumber: EC 4.3.1.17 |
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| b4478 | b4478 | D-galactonate dehydratase (GalD) (EC 4.2.1.6) | Cytoplasm | R_GALCTND_enzyme | R_GALCTND | 382 | Translation: 382.0, Folding: 38.2 | 42,523 | UniprotID: Q6BF17 ECnumber: EC 4.2.1.6 |
FUNCTION: Catalyzes the dehydration of D-galactonate to 2-keto-3-deoxy-D-galactonate. {ECO:0000269|PubMed:324806, ECO:0000269|Ref.7}. | |
| b3517 | b3517 | Glutamate decarboxylase alpha (GAD-alpha) (EC 4.1.1.15) | Cytoplasm | R_GLUDC_enzyme | R_GLUDC | 466 | Translation: 466.0, Folding: 46.6 | 52,685 | UniprotID: P69908 ECnumber: EC 4.1.1.15 |
FUNCTION: Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. |
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| b0451 | b0451 | Ammonia channel (Ammonia transporter) | Cell_inner_membrane | R_NH4tpp_enzyme | R_NH4tpp | 428 | Secretion: 428.0, Translation: 428.0, Folding: 42.8 | 44,515 | UniprotID: P69681 | FUNCTION: Involved in the uptake of ammonia. | |
| b0452 | b0452 | Acyl-CoA thioesterase 2 (EC 3.1.2.-) (Acyl-CoA thioesterase II) (TEII) | Cytoplasm | 286 | Translation: 286.0, Folding: 28.6 | 31,966 | UniprotID: P0AGG2 ECnumber: EC 3.1.2.- |
FUNCTION: Can hydrolyze a broad range of acyl-CoA thioesters. Its physiological function is not known. | |||
| b3578 | b3578 | 2,3-diketo-L-gulonate TRAP transporter large permease protein YiaN | Cell_inner_membrane | R_XYLUt2pp_enzyme | R_XYLUt2pp | 425 | Secretion: 425.0, Translation: 425.0, Folding: 42.5 | 45,368 | UniprotID: P37675 | FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP) transport system YiaMNO involved in the uptake of 2,3-diketo-L-gulonate. {ECO:0000269|PubMed:16385129}. | |
| b3579 | b3579 | 2,3-diketo-L-gulonate-binding periplasmic protein YiaO (2,3-DKG-binding protein) (Extracytoplasmic solute receptor protein YiaO) | Periplasm | R_XYLUt2pp_enzyme | R_XYLUt2pp | 328 | Secretion: 328.0, Translation: 328.0, Folding: 32.8 | 35,970 | UniprotID: P37676 | FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP) transport system YiaMNO involved in the uptake of 2,3-diketo-L-gulonate. This protein specifically binds 2,3-diketo-L-gulonate. Is not able to bind either L-ascorbate or dehydroascorbate. {ECO:0000269|PubMed:16385129}. | |
| b3577 | b3577 | 2,3-diketo-L-gulonate TRAP transporter small permease protein YiaM | Cell_inner_membrane | R_XYLUt2pp_enzyme | R_XYLUt2pp | 157 | Secretion: 157.0, Translation: 157.0, Folding: 15.7 | 17,516 | UniprotID: P37674 | FUNCTION: Part of the tripartite ATP-independent periplasmic (TRAP) transport system YiaMNO involved in the uptake of 2,3-diketo-L-gulonate. {ECO:0000269|PubMed:16385129}. | |
| b3575 | b3575 | 2,3-diketo-L-gulonate reductase (2,3-DKG reductase) (EC 1.1.1.130) (3-dehydro-L-gulonate 2-dehydrogenase) | Cytoplasm | R_DOGULNR_enzyme | R_DOGULNR | 332 | Translation: 332.0, Folding: 33.2 | 36,573 | UniprotID: P37672 ECnumber: EC 1.1.1.130 |
FUNCTION: Catalyzes the reduction of 2,3-diketo-L-gulonate in the presence of NADH, to form 3-keto-L-gulonate. {ECO:0000269|PubMed:11741871}. | |
| b3572 | b3572 | Valine--pyruvate aminotransferase (EC 2.6.1.66) (Alanine--valine transaminase) (Transaminase C) | Cytoplasm | R_VPAMTr_enzyme | R_VPAMTr | 417 | Translation: 417.0, Folding: 41.7 | 46,711 | UniprotID: P09053 ECnumber: EC 2.6.1.66 |
FUNCTION: Involved in the biosynthesis of alanine. {ECO:0000269|PubMed:13034817, ECO:0000269|PubMed:20729367}. | |
| b3571 | b3571 | Periplasmic alpha-amylase (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) | Periplasm | R_AAMYLpp_enzyme | R_AAMYLpp | 676 | Secretion: 676.0, Translation: 676.0, Folding: 67.6 | 75,713 | UniprotID: P25718 ECnumber: EC 3.2.1.1 |
FUNCTION: Since only maltooligosaccharides up to a chain length of 6 glucose units are actively transported through the cytoplasmic membrane via the membrane-bound complex of three proteins, MalF, MalG, and MalK, longer maltooligosaccharides must first be degraded by the periplasmic alpha-amylase, the MalS protein. | |
| b3172 | b3172 | Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate ligase) | Cytoplasm | R_ARGSS_enzyme | R_ARGSS | 447 | Translation: 447.0, Folding: 44.7 | 49,898 | UniprotID: P0A6E4 ECnumber: EC 6.3.4.5 |
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| b3176 | b3176 | Phosphoglucosamine mutase (EC 5.4.2.10) | Cytoplasm | R_PGAMT_enzyme | R_PGAMT | 445 | Translation: 445.0, Folding: 44.5 | 47,544 | UniprotID: P31120 ECnumber: EC 5.4.2.10 |
FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. Can also catalyze the formation of glucose-6-P from glucose-1-P, although at a 1400-fold lower rate. {ECO:0000269|PubMed:10231382}. | |
| b3177 | b3177 | Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase) | Cytoplasm | R_DHPS2_enzyme | R_DHPS2 | 282 | Translation: 282.0, Folding: 28.2 | 30,615 | UniprotID: P0AC13 ECnumber: EC 2.5.1.15 |
FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-dihydropteroate (H2Pte), the immediate precursor of folate derivatives. {ECO:0000269|PubMed:368012}. | |
| b2311 | b2311 | Flavin prenyltransferase UbiX (EC 2.5.1.129) | Cytoplasm | R_OPHBDC_enzyme | R_OPHBDC | 189 | Translation: 189.0, Folding: 18.9 | 20,695 | UniprotID: P0AG03 ECnumber: EC 2.5.1.129 |
FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN (By similarity). Acts in concert with UbiD to perform the decarboxylation of 4-hydroxy-3-octaprenyl-benzoate, a step in the biosynthesis of coenzyme Q (PubMed:16923914, PubMed:17889824). {ECO:0000255|HAMAP-Rule:MF_01984, ECO:0000269|PubMed:16923914, ECO:0000269|PubMed:17889824}. |
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| b2310 | b2310 | Lysine/arginine/ornithine-binding periplasmic protein (LAO-binding protein) | Periplasm | R_ARGabcpp_enzyme R_LYSabcpp_enzyme R_ORNabcpp_enzyme |
R_ARGabcpp R_LYSabcpp R_ORNabcpp |
260 | Secretion: 260.0, Translation: 260.0, Folding: 26.0 | 27,992 | UniprotID: P09551 | FUNCTION: Part of an ABC transporter involved in lysine, arginine and ornithine transport. Stimulates ATPase activity of HisP (By similarity). {ECO:0000250}. | |
| b2312 | b2312 | Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPATase) | Cytoplasm | R_GLUPRT_enzyme | R_GLUPRT | 505 | Translation: 505.0, Folding: 50.5 | 56,488 | UniprotID: P0AG16 ECnumber: EC 2.4.2.14 |
FUNCTION: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine. Can also use NH(3) in place of glutamine. {ECO:0000269|PubMed:372191}. | |
| b2315 | b2315 | Dihydrofolate synthase/folylpolyglutamate synthase (DHFS / FPGS) (EC 6.3.2.12) (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase) (Folylpolyglutamate synthetase) (Tetrahydrofolylpolyglutamate synthase) | Cytoplasm | R_DHFS_enzyme | R_DHFS | 422 | Translation: 422.0, Folding: 42.2 | 45,406 | UniprotID: P08192 ECnumber: EC 6.3.2.12; 6.3.2.17 |
FUNCTION: Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives. {ECO:0000269|PubMed:18232714, ECO:0000269|PubMed:1989505, ECO:0000269|PubMed:2985605}. |
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| b2316 | b2316 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta (ACCase subunit beta) (Acetyl-CoA carboxylase carboxyltransferase subunit beta) (EC 6.4.1.2) | Cytoplasm | R_ACCOAC_enzyme | R_ACCOAC | 304 | Translation: 304.0, Folding: 30.4 | 33,322 | UniprotID: P0A9Q5 ECnumber: EC 6.4.1.2 |
FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA.; FUNCTION: Controls translation of mRNA for both itself and the alpha-subunit (accA) by binding to a probable hairpin in the 5 of the mRNA. Binding to mRNA inhibits translation; this is partially relieved by acetyl-CoA. Increasing amounts of mRNA also inhibit enzyme activity. |
|
| b3779 | b3779 | Guanosine-5-triphosphate,3-diphosphate pyrophosphatase (EC 3.6.1.40) (Guanosine pentaphosphate phosphohydrolase) (pppGpp-5-phosphohydrolase) | Cytoplasm | R_GTPDPDP_enzyme | R_GTPDPDP | 494 | Translation: 494.0, Folding: 49.4 | 54,871 | UniprotID: P25552 ECnumber: EC 3.6.1.40 |
FUNCTION: Catalyzes the conversion of pppGpp to ppGpp. Guanosine pentaphosphate (pppGpp) is a cytoplasmic signaling molecule which together with ppGpp controls the 'stringent response | |
| b3770 | b3770 | Branched-chain-amino-acid aminotransferase (BCAT) (EC 2.6.1.42) (Transaminase B) | Cytoplasm | R_ILETA_enzyme R_LEUTAi_enzyme R_PHETA1_duplicate_3_enzyme R_VALTA_enzyme |
R_ILETA R_LEUTAi R_PHETA1_duplicate_3 R_VALTA |
309 | Translation: 309.0, Folding: 30.9 | 34,094 | UniprotID: P0AB80 ECnumber: EC 2.6.1.42 |
FUNCTION: Acts on leucine, isoleucine and valine. | |
| b3771 | b3771 | Dihydroxy-acid dehydratase (DAD) (EC 4.2.1.9) | Cytoplasm | R_DHAD1_enzyme R_DHAD2_enzyme |
R_DHAD1 R_DHAD2 |
616 | Translation: 616.0, Folding: 61.6 | 65,532 | UniprotID: P05791 ECnumber: EC 4.2.1.9 |
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| b3772 | b3772 | L-threonine dehydratase biosynthetic IlvA (EC 4.3.1.19) (Threonine deaminase) | Cytoplasm | R_THRD_L_duplicate_2_enzyme | R_THRD_L_duplicate_2 | 514 | Translation: 514.0, Folding: 51.4 | 56,195 | UniprotID: P04968 ECnumber: EC 4.3.1.19 |
FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and ammonia from threonine in a two-step reaction. The first step involved a dehydration of threonine and a production of enamine intermediates (aminocrotonate), which tautomerizes to its imine form (iminobutyrate). Both intermediates are unstable and short-lived. The second step is the nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-ketobutyrate and free ammonia. In the low water environment of the cell, the second step is accelerated by RidA. {ECO:0000269|PubMed:13405870}. |
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| b3774 | b3774 | Ketol-acid reductoisomerase (NADP(+)) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 2) (Ketol-acid reductoisomerase type II) | Cytoplasm | R_DPR_duplicate_2_enzyme R_KARA1_enzyme R_KARA2_enzyme |
R_DPR_duplicate_2 R_KARA1 R_KARA2 |
491 | Translation: 491.0, Folding: 49.1 | 54,069 | UniprotID: P05793 ECnumber: EC 1.1.1.86 |
FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate, 3-hydroxypyruvate, 3-hydroxy-2-ketobutyrate and pyruvate (PubMed:15654896). {ECO:0000269|PubMed:15654896, ECO:0000269|PubMed:21515217, ECO:0000269|PubMed:2653423, ECO:0000269|PubMed:9015391}. |
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| b3951 | b3951 | Formate acetyltransferase 2 (EC 2.3.1.54) (Pyruvate formate-lyase 2) | Cytoplasm | R_PFL_enzyme | R_PFL | 765 | Translation: 765.0, Folding: 76.5 | 85,960 | UniprotID: P32674 ECnumber: EC 2.3.1.54 |
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| b2429 | b2429 | PTS system N-acetylmuramic acid-specific EIIBC component (EIIBC-MurNAc) [Includes: N-acetylmuramic acid-specific phosphotransferase enzyme IIB component (EC 2.7.1.192) (PTS system N-acetylmuramic acid-specific EIIB component); N-acetylmuramic acid permease IIC component (PTS system N-acetylmuramic acid-specific EIIC component) | Cell_inner_membrane | R_ACMUMptspp_enzyme R_SUCptspp_enzyme |
R_ACMUMptspp R_SUCptspp |
474 | Secretion: 474.0, Translation: 474.0, Folding: 47.4 | 49,802 | UniprotID: P77272 ECnumber: EC 2.7.1.192 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in N-acetylmuramic acid (MurNAc) transport, yielding cytoplasmic MurNAc-6-P. Is responsible for growth on MurNAc as the sole source of carbon and energy. Is also able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably because of the 1,6-anhydro ring. {ECO:0000269|PubMed:15060041, ECO:0000269|PubMed:16452451}. |
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| b2428 | b2428 | N-acetylmuramic acid 6-phosphate etherase (MurNAc-6-P etherase) (EC 4.2.1.126) (N-acetylmuramic acid 6-phosphate hydrolase) (N-acetylmuramic acid 6-phosphate lyase) | Cytoplasm | R_ACM6PH_enzyme | R_ACM6PH | 298 | Translation: 298.0, Folding: 29.8 | 31,220 | UniprotID: P76535 ECnumber: EC 4.2.1.126 |
FUNCTION: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Is required for growth on MurNAc as the sole source of carbon and energy. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. {ECO:0000269|PubMed:15983044, ECO:0000269|PubMed:16452451}. |
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| b3403 | b3403 | Phosphoenolpyruvate carboxykinase (ATP) (PCK) (PEP carboxykinase) (PEPCK) (EC 4.1.1.49) | Cytoplasm | R_PPCK_enzyme | R_PPCK | 540 | Translation: 540.0, Folding: 54.0 | 59,643 | UniprotID: P22259 ECnumber: EC 4.1.1.49 |
FUNCTION: Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. {ECO:0000255|HAMAP-Rule:MF_00453, ECO:0000269|PubMed:1701430, ECO:0000269|PubMed:6986370, ECO:0000269|PubMed:8226637}. | |
| b3956 | b3956 | Phosphoenolpyruvate carboxylase (PEPC) (PEPCase) (EC 4.1.1.31) | Cytoplasm | R_PPC_enzyme | R_PPC | 883 | Translation: 883.0, Folding: 88.3 | 99,063 | UniprotID: P00864 ECnumber: EC 4.1.1.31 |
FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. | |
| b3957 | b3957 | Acetylornithine deacetylase (AO) (Acetylornithinase) (EC 3.5.1.16) (N-acetylornithinase) (NAO) | Cytoplasm | R_ACODA_enzyme R_NACODA_enzyme |
R_ACODA R_NACODA |
383 | Translation: 383.0, Folding: 38.3 | 42,347 | UniprotID: P23908 ECnumber: EC 3.5.1.16 |
FUNCTION: Displays a broad specificity and can also deacylate substrates such as acetylarginine, acetylhistidine or acetylglutamate semialdehyde. | |
| b3958 | b3958 | N-acetyl-gamma-glutamyl-phosphate reductase (AGPR) (EC 1.2.1.38) (N-acetyl-glutamate semialdehyde dehydrogenase) (NAGSA dehydrogenase) | Cytoplasm | R_AGPR_enzyme | R_AGPR | 334 | Translation: 334.0, Folding: 33.4 | 35,952 | UniprotID: P11446 ECnumber: EC 1.2.1.38 |
FUNCTION: Catalyzes the NADPH-dependent reduction of N-acetyl-5-glutamyl phosphate to yield N-acetyl-L-glutamate 5-semialdehyde. {ECO:0000255|HAMAP-Rule:MF_00150, ECO:0000269|PubMed:13863980}. | |
| b2130 | b2130 | Glycine betaine uptake system permease protein YehY | Cell_inner_membrane | R_CHLabcpp_enzyme R_GLYBabcpp_enzyme |
R_CHLabcpp R_GLYBabcpp |
385 | Secretion: 385.0, Translation: 385.0, Folding: 38.5 | 41,139 | UniprotID: P33361 | FUNCTION: Part of an ABC transporter complex involved in low-affinity glycine betaine uptake. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:26325238}. | |
| b2133 | b2133 | Quinone-dependent D-lactate dehydrogenase (EC 1.1.5.12) ((R)-lactate:quinone 2-oxidoreductase) (D-lactate dehydrogenase) (D-LDH) (Respiratory D-lactate dehydrogenase) | Cell_inner_membrane | R_LDH_D_enzyme R_LDH_D2_enzyme |
R_LDH_D R_LDH_D2 |
571 | Secretion: 571.0, Translation: 571.0, Folding: 57.1 | 64,612 | UniprotID: P06149 ECnumber: EC 1.1.5.12 |
FUNCTION: Catalyzes the oxidation of D-lactate to pyruvate. Electrons derived from D-lactate oxidation are transferred to the ubiquinone/cytochrome electron transfer chain, where they may be used to provide energy for the active transport of a variety of amino acids and sugars across the membrane. {ECO:0000269|PubMed:2185834, ECO:0000269|PubMed:3013300, ECO:0000269|PubMed:4575624, ECO:0000269|PubMed:4582730, ECO:0000269|PubMed:7578233}. |
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| b2132 | b2132 | Periplasmic beta-glucosidase (EC 3.2.1.21) (Beta-D-glucoside glucohydrolase) (Cellobiase) (Gentiobiase) | Periplasm | R_LACZpp_enzyme | R_LACZpp | 765 | Secretion: 765.0, Translation: 765.0, Folding: 76.5 | 83,460 | UniprotID: P33363 ECnumber: EC 3.2.1.21 |
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| b2134 | b2134 | D-alanyl-D-alanine endopeptidase (DD-endopeptidase) (EC 3.4.21.-) (Penicillin-binding protein 7) (PBP-7) | Periplasm | R_MDDEP1pp_duplicate_3_enzyme R_MDDEP2pp_duplicate_3_enzyme R_MDDEP3pp_duplicate_3_enzyme R_MDDEP4pp_duplicate_3_enzyme |
R_MDDEP1pp_duplicate_3 R_MDDEP2pp_duplicate_3 R_MDDEP3pp_duplicate_3 R_MDDEP4pp_duplicate_3 |
310 | Secretion: 310.0, Translation: 310.0, Folding: 31.0 | 33,887 | UniprotID: P0AFI5 ECnumber: EC 3.4.21.- |
FUNCTION: Cell wall formation. May play a specialized role in remodeling the cell wall. Specifically hydrolyzes the DD-diaminopimelate-alanine bonds in high-molecular-mass murein sacculi. | |
| b2425 | b2425 | Thiosulfate-binding protein | Periplasm | R_MOBDabcpp_duplicate_3_enzyme R_SELtpp_enzyme R_SLNTtpp_enzyme R_SULabcpp_duplicate_2_enzyme R_TSULabcpp_enzyme |
R_MOBDabcpp_duplicate_3 R_SELtpp R_SLNTtpp R_SULabcpp_duplicate_2 R_TSULabcpp |
338 | Secretion: 338.0, Translation: 338.0, Folding: 33.8 | 37,615 | UniprotID: P16700 | FUNCTION: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. This protein specifically binds thiosulfate and is involved in its transmembrane transport. | |
| b3409 | b3409 | Fe(2+) transporter FeoB (Ferrous iron transport protein B) | Cell_inner_membrane | R_FE2abcpp_enzyme | R_FE2abcpp | 773 | Secretion: 773.0, Translation: 773.0, Folding: 77.3 | 84,474 | UniprotID: P33650 | FUNCTION: Transporter of a GTP-driven Fe(2+) uptake system, probably couples GTP-binding to channel opening and Fe(2+) uptake (PubMed:12446835, PubMed:19629046). A guanine nucleotide-binding protein (G proteins) in which the guanine nucleotide binding site alternates between an active, GTP-bound state and an inactive, GDP-bound state. This protein has fast intrinsic GDP release, mediated by the G5 loop (about residues 149-158). Presumably GTP hydrolysis leads to conformational changes and channel closing (PubMed:19629046). A GDP release mechanism involving a conformational change of the G5 loop (and thus the removal of the nucleotide-binding and stabilizing interactions) would significantly reduce the affinity for GDP, and conceivably be sufficient for catalysing nucleotide release (PubMed:25374115). {ECO:0000269|PubMed:12446835, ECO:0000269|PubMed:19629046, ECO:0000269|PubMed:23104801, ECO:0000269|PubMed:25374115, ECO:0000269|PubMed:25517170, ECO:0000269|PubMed:8407793}. |
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| b3794 | b3794 | UDP-N-acetyl-D-mannosaminuronic acid transferase (UDP-ManNAcA transferase) (EC 2.4.1.180) | Cytoplasm | R_ACMAMUT_enzyme | R_ACMAMUT | 246 | Translation: 246.0, Folding: 24.6 | 27,928 | UniprotID: P27836 ECnumber: EC 2.4.1.180 |
FUNCTION: Catalyzes the synthesis of Und-PP-GlcNAc-ManNAcA (Lipid II), the second lipid-linked intermediate involved in enterobacterial common antigen (ECA) synthesis. {ECO:0000255|HAMAP-Rule:MF_01001, ECO:0000269|PubMed:1730666}. | |
| b3792 | b3792 | Lipid III flippase | Cell_inner_membrane | R_ECAtpp_enzyme | R_ECAtpp | 416 | Secretion: 416.0, Translation: 416.0, Folding: 41.6 | 44,960 | UniprotID: P0AAA7 | FUNCTION: Mediates the transbilayer movement of Und-PP-GlcNAc-ManNAcA-Fuc4NAc (lipid III) from the inner to the outer leaflet of the cytoplasmic membrane during the assembly of enterobacterial common antigen (ECA). Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)). Could also mediate the translocation of Und-PP-GlcNAc. {ECO:0000269|PubMed:12621029, ECO:0000269|PubMed:16199561}. |
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| b3793 | b3793 | Probable ECA polymerase | Cell_inner_membrane | R_ECAP1pp_enzyme R_ECAP2pp_enzyme R_ECAP3pp_enzyme |
R_ECAP1pp R_ECAP2pp R_ECAP3pp |
450 | Secretion: 450.0, Translation: 450.0, Folding: 45.0 | 51,517 | UniprotID: P27835 | FUNCTION: Probably involved in the polymerization of enterobacterial common antigen (ECA) trisaccharide repeat units. Required for the assembly of the phosphoglyceride-linked form of ECA (ECA(PG)) and the water-soluble cyclic form of ECA (ECA(CYC)). {ECO:0000269|PubMed:16199561}. | |
| b3790 | b3790 | dTDP-fucosamine acetyltransferase (EC 2.3.1.210) (TDP-fucosamine acetyltransferase) (dTDP-4-amino-4,6-dideoxy-D-galactose acyltransferase) | Cytoplasm | R_TDPADGAT_enzyme | R_TDPADGAT | 224 | Translation: 224.0, Folding: 22.4 | 24,220 | UniprotID: P27832 ECnumber: EC 2.3.1.210 |
FUNCTION: Catalyzes the acetylation of dTDP-fucosamine (dTDP-4-amino-4,6-dideoxy-D-galactose) to dTDP-Fuc4NAc, which is utilized in the biosynthesis of the enterobacterial common antigen (ECA). {ECO:0000255|HAMAP-Rule:MF_02027}. | |
| b3791 | b3791 | dTDP-4-amino-4,6-dideoxygalactose transaminase (EC 2.6.1.59) | Cytoplasm | R_TDPAGTA_enzyme | R_TDPAGTA | 376 | Translation: 376.0, Folding: 37.6 | 41,901 | UniprotID: P27833 ECnumber: EC 2.6.1.59 |
FUNCTION: Catalyzes the synthesis of dTDP-4-amino-4,6-dideoxy-D-galactose (dTDP-Fuc4N) from dTDP-4-keto-6-deoxy-D-glucose (dTDP-D-Glc4O) and L-glutamate. {ECO:0000255|HAMAP-Rule:MF_02026, ECO:0000269|PubMed:15271350}. | |
| b2957 | b2957 | L-asparaginase 2 (EC 3.5.1.1) (L-asparaginase II) (L-ASNase II) (L-asparagine amidohydrolase II) (Colaspase) | Periplasm | R_ASNNpp_enzyme R_GLUNpp_enzyme |
R_ASNNpp R_GLUNpp |
348 | Secretion: 348.0, Translation: 348.0, Folding: 34.8 | 36,851 | UniprotID: P00805 ECnumber: EC 3.5.1.1 |
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| b2954 | b2954 | dITP/XTP pyrophosphatase (EC 3.6.1.66) (Deoxyribonucleoside triphosphate pyrophosphohydrolase) (Inosine triphosphate pyrophosphatase) (ITPase) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) | Cytoplasm | R_NTPP10_enzyme R_NTPP11_enzyme R_NTPP9_enzyme |
R_NTPP10 R_NTPP11 R_NTPP9 |
197 | Translation: 197.0, Folding: 19.7 | 21,039 | UniprotID: P52061 ECnumber: EC 3.6.1.66 |
FUNCTION: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP (PubMed:12297000, PubMed:17976651). Can also efficiently hydrolyze 2-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP) (PubMed:17090528). Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions (PubMed:12297000, PubMed:12730170, PubMed:17090528). To a much lesser extent, is also able to hydrolyze GTP, dGTP and dUTP, but shows very low activity toward the canonical nucleotides dATP, dCTP and dTTP and toward 8-oxo-dGTP, purine deoxyribose triphosphate, 2-aminopurine deoxyribose triphosphate and 2,6-diaminopurine deoxyribose triphosphate (PubMed:12297000, PubMed:17090528). {ECO:0000255|HAMAP-Rule:MF_01405, ECO:0000269|PubMed:12297000, ECO:0000269|PubMed:12730170, ECO:0000269|PubMed:17090528, ECO:0000269|PubMed:17976651}. |
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| b2558 | b2558 | Membrane-bound lytic murein transglycosylase F (EC 4.2.2.n1) (Murein lyase F) | Cell_outer_membrane | R_MLTGY1pp_duplicate_3_enzyme R_MLTGY2pp_duplicate_4_enzyme R_MLTGY3pp_duplicate_2_enzyme R_MLTGY4pp_duplicate_5_enzyme |
R_MLTGY1pp_duplicate_3 R_MLTGY2pp_duplicate_4 R_MLTGY3pp_duplicate_2 R_MLTGY4pp_duplicate_5 |
518 | Secretion: 518.0, Translation: 518.0, Folding: 51.8 | 58,302 | UniprotID: P0AGC5 ECnumber: EC 4.2.2.n1 |
FUNCTION: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella. |
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| b2557 | b2557 | Phosphoribosylformylglycinamidine synthase (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) | Cytoplasm | R_PRFGS_enzyme | R_PRFGS | 1295 | Translation: 1295.0, Folding: 129.5 | 141,403 | UniprotID: P15254 ECnumber: EC 6.3.5.3 |
FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. {ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:2659070}. | |
| b2224 | b2224 | Acetyl-CoA acetyltransferase (EC 2.3.1.9) (Acetoacetyl-CoA thiolase) | Cytoplasm | R_ACACT1r_duplicate_2_enzyme | R_ACACT1r_duplicate_2 | 394 | Translation: 394.0, Folding: 39.4 | 40,352 | UniprotID: P76461 ECnumber: EC 2.3.1.9 |
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| b2221 | b2221 | Acetate CoA-transferase subunit alpha (EC 2.8.3.8) (Acetyl-CoA:acetoacetate-CoA transferase subunit alpha) | Cytoplasm | R_ACACCT_enzyme R_BUTCT_enzyme R_HXCT_enzyme |
R_ACACCT R_BUTCT R_HXCT |
220 | Translation: 220.0, Folding: 22.0 | 23,526 | UniprotID: P76458 ECnumber: EC 2.8.3.8 |
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| b2552 | b2552 | Flavohemoprotein (Flavohemoglobin) (HMP) (Hemoglobin-like protein) (Nitric oxide dioxygenase) (NO oxygenase) (NOD) (EC 1.14.12.17) | Cytoplasm | R_NODOx_enzyme R_NODOy_enzyme |
R_NODOx R_NODOy |
396 | Translation: 396.0, Folding: 39.6 | 43,868 | UniprotID: P24232 ECnumber: EC 1.14.12.17 |
FUNCTION: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.; FUNCTION: In the presence of oxygen and NADH, HMP has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2), both in vitro and in vivo, and it has been suggested that HMP might act as an amplifier of superoxide stress. Under anaerobic conditions, HMP also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity.; FUNCTION: Various electron acceptors are also reduced by HMP in vitro, including dihydropterine, ferrisiderophores, ferric citrate, cytochrome c, nitrite, S-nitrosoglutathione, and alkylhydroperoxides. However, it is unknown if these reactions are of any biological significance in vivo. |
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| b2551 | b2551 | Serine hydroxymethyltransferase (SHMT) (Serine methylase) (EC 2.1.2.1) | Cytoplasm | R_ALATA_D2_enzyme R_ALATA_L2_duplicate_2_enzyme R_GHMT2r_enzyme R_THFAT_enzyme R_THRA2_enzyme R_THRA_enzyme |
R_ALATA_D2 R_ALATA_L2_duplicate_2 R_GHMT2r R_THFAT R_THRA2 R_THRA |
417 | Translation: 417.0, Folding: 41.7 | 45,317 | UniprotID: P0A825 ECnumber: EC 2.1.2.1 |
FUNCTION: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-methenyltetrahydrofolate to 5-formyltetrahydrofolate. {ECO:0000269|PubMed:6190704}. |
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| b2222 | b2222 | Acetate CoA-transferase subunit beta (EC 2.8.3.8) (Acetyl-CoA:acetoacetate CoA-transferase subunit beta) | Cytoplasm | R_ACACCT_enzyme R_BUTCT_enzyme R_HXCT_enzyme |
R_ACACCT R_BUTCT R_HXCT |
216 | Translation: 216.0, Folding: 21.6 | 22,960 | UniprotID: P76459 ECnumber: EC 2.8.3.8 |
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| b2045 | b2045 | Colanic acid biosynthesis protein WcaK (EC 2.-.-.-) | Cytoplasm | R_GALKr_enzyme | R_GALKr | 426 | Translation: 426.0, Folding: 42.6 | 47,344 | UniprotID: P71242 ECnumber: EC 2.-.-.- |
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| b1059 | b1059 | N-methyl-L-tryptophan oxidase (MTOX) (EC 1.5.3.-) | Cytoplasm | R_MTRPOX_enzyme R_SARCOX_enzyme |
R_MTRPOX R_SARCOX |
372 | Translation: 372.0, Folding: 37.2 | 40,902 | UniprotID: P40874 ECnumber: EC 1.5.3.- |
FUNCTION: Catalyzes the oxidative demethylation of N-methyl-L-tryptophan. Can also use other N-methyl amino acids, including sarcosine, which, however, is a poor substrate. | |
| b2041 | b2041 | dTDP-glucose 4,6-dehydratase 1 (EC 4.2.1.46) | Cytoplasm | R_TDPGDH_duplicate_2_enzyme | R_TDPGDH_duplicate_2 | 361 | Translation: 361.0, Folding: 36.1 | 40,558 | UniprotID: P37759 ECnumber: EC 4.2.1.46 |
FUNCTION: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction. {ECO:0000250|UniProtKB:P27830}. | |
| b2040 | b2040 | dTDP-4-dehydrorhamnose reductase (EC 1.1.1.133) (dTDP-4-keto-L-rhamnose reductase) (dTDP-6-deoxy-L-lyxo-4-hexulose reductase) (dTDP-6-deoxy-L-mannose dehydrogenase) (dTDP-L-rhamnose synthase) | Cytoplasm | R_TDPDRR_enzyme | R_TDPDRR | 299 | Translation: 299.0, Folding: 29.9 | 32,694 | UniprotID: P37760 ECnumber: EC 1.1.1.133 |
FUNCTION: Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose. RmlD uses NADH and NADPH nearly equally well (By similarity). {ECO:0000250}. | |
| b2049 | b2049 | Mannose-1-phosphate guanylyltransferase (EC 2.7.7.13) (GDP-mannose pyrophosphorylase) (GMP) (GMPP) | Cytoplasm | R_MAN1PT2_enzyme | R_MAN1PT2 | 478 | Translation: 478.0, Folding: 47.8 | 53,016 | UniprotID: P24174 ECnumber: EC 2.7.7.13 |
FUNCTION: Involved in the biosynthesis of the capsular polysaccharide colanic acid. | |
| b2048 | b2048 | Phosphomannomutase (PMM) (EC 5.4.2.8) | Cytoplasm | R_PMANM_enzyme | R_PMANM | 456 | Translation: 456.0, Folding: 45.6 | 50,463 | UniprotID: P24175 ECnumber: EC 5.4.2.8 |
FUNCTION: Involved in the biosynthesis of the capsular polysaccharide colanic acid. | |
| b1054 | b1054 | Lipid A biosynthesis lauroyltransferase (EC 2.3.1.241) (Kdo(2)-lipid IV(A) lauroyltransferase) | Cell_inner_membrane | R_EDTXS1_enzyme | R_EDTXS1 | 306 | Secretion: 306.0, Translation: 306.0, Folding: 30.6 | 35,407 | UniprotID: P0ACV0 ECnumber: EC 2.3.1.241 |
FUNCTION: Catalyzes the transfer of laurate from lauroyl-acyl carrier protein (ACP) to Kdo(2)-lipid IV(A) to form Kdo(2)-(lauroyl)-lipid IV(A). Has 10 fold selectivity for lauroyl-ACP over myristoyl-ACP. In vitro, can also catalyze a slow second acylation reaction leading to the formation of Kdo(2)-(dilauroyl)-lipid IV(A). {ECO:0000269|PubMed:18656959, ECO:0000269|PubMed:2203778, ECO:0000269|PubMed:8662613}. |
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| b1702 | b1702 | Phosphoenolpyruvate synthase (PEP synthase) (EC 2.7.9.2) (Pyruvate, water dikinase) | Cytoplasm | R_PPS_enzyme | R_PPS | 792 | Translation: 792.0, Folding: 79.2 | 87,435 | UniprotID: P23538 ECnumber: EC 2.7.9.2 |
FUNCTION: Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. {ECO:0000269|PubMed:4319237}. | |
| b4311 | b4311 | Probable N-acetylneuraminic acid outer membrane channel protein NanC (NanR-regulated channel) (Porin NanC) | Cell_outer_membrane | R_ACNAMtex_duplicate_2_enzyme | R_ACNAMtex_duplicate_2 | 238 | Secretion: 238.0, Translation: 238.0, Folding: 23.8 | 27,888 | UniprotID: P69856 | FUNCTION: Outer membrane channel protein allowing the entry of N-acetylneuraminic acid (Neu5Ac, the most abundant sialic acid on host cell surfaces) into the bacteria (Probable). NanC proteins form high-conductance channels which are open at low membrane potentials and which have a weak anion selectivity. {ECO:0000269|PubMed:15743943, ECO:0000305}. | |
| b1709 | b1709 | Vitamin B12 import ATP-binding protein BtuD (EC 3.6.3.33) (Vitamin B12-transporting ATPase) | Cell_inner_membrane | R_ADOCBLabcpp_enzyme R_CBIuabcpp_enzyme R_CBL1abcpp_enzyme |
R_ADOCBLabcpp R_CBIuabcpp R_CBL1abcpp |
249 | Secretion: 249.0, Translation: 249.0, Folding: 24.9 | 27,081 | UniprotID: P06611 ECnumber: EC 3.6.3.33 |
FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01005}. | |
| b0832 | b0832 | Glutathione transport system permease protein GsiD | Cell_inner_membrane | R_GTHRDabcpp_enzyme | R_GTHRDabcpp | 303 | Secretion: 303.0, Translation: 303.0, Folding: 30.3 | 33,238 | UniprotID: P75799 | FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane (Probable). {ECO:0000305|PubMed:16109926}. | |
| b0830 | b0830 | Glutathione-binding protein GsiB | Periplasm | R_GTHRDabcpp_enzyme | R_GTHRDabcpp | 512 | Secretion: 512.0, Translation: 512.0, Folding: 51.2 | 56,470 | UniprotID: P75797 | FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. {ECO:0000269|PubMed:16109926}. | |
| b0831 | b0831 | Glutathione transport system permease protein GsiC | Cell_inner_membrane | R_GTHRDabcpp_enzyme | R_GTHRDabcpp | 306 | Secretion: 306.0, Translation: 306.0, Folding: 30.6 | 34,066 | UniprotID: P75798 | FUNCTION: Part of the ABC transporter complex GsiABCD involved in glutathione import. Probably responsible for the translocation of the substrate across the membrane (Probable). {ECO:0000305|PubMed:16109926}. | |
| b0837 | b0837 | Aldose sugar dehydrogenase YliI (Asd) (EC 1.1.5.-) (Soluble aldose sugar dehydrogenase YliI) | Cell_outer_membrane | R_GLCDpp_duplicate_2_enzyme | R_GLCDpp_duplicate_2 | 371 | Secretion: 371.0, Translation: 371.0, Folding: 37.1 | 41,054 | UniprotID: P75804 ECnumber: EC 1.1.5.- |
FUNCTION: Aldose sugar dehydrogenase with broad substrate specificity. The physiological substrate is unknown. Can oxidize glucose to gluconolactone. Can also utilize D-arabinose, L-arabinose and 2-deoxy-glucose. Has higher activity towards oligomeric sugars, such as maltose, maltotriose or cellobiose. It may function to input sugar-derived electrons into the respiratory network. {ECO:0000269|PubMed:16864586}. |
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| b0839 | b0839 | D-alanyl-D-alanine carboxypeptidase DacC (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (Penicillin-binding protein 6) (PBP-6) | Cell_inner_membrane | R_MDDCP1pp_enzyme R_MDDCP2pp_enzyme R_MDDCP3pp_enzyme R_MDDCP4pp_enzyme R_MDDCP5pp_enzyme |
R_MDDCP1pp R_MDDCP2pp R_MDDCP3pp R_MDDCP4pp R_MDDCP5pp |
400 | Secretion: 400.0, Translation: 400.0, Folding: 40.0 | 43,609 | UniprotID: P08506 ECnumber: EC 3.4.16.4 |
FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | |
| b1302 | b1302 | 4-aminobutyrate aminotransferase PuuE (EC 2.6.1.19) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (Glutamate:succinic semialdehyde transaminase) | Cytoplasm | R_ABTA_duplicate_2_enzyme | R_ABTA_duplicate_2 | 421 | Translation: 421.0, Folding: 42.1 | 44,729 | UniprotID: P50457 ECnumber: EC 2.6.1.19 |
FUNCTION: Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). PuuE is important for utilization of putrescine as the sole nitrogen or carbon source. {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:20639325}. | |
| b1301 | b1301 | Gamma-glutamylputrescine oxidoreductase (Gamma-Glu-Put oxidase) (Gamma-glutamylputrescine oxidase) (EC 1.4.3.-) | Cytoplasm | R_GGPTRCO_enzyme | R_GGPTRCO | 426 | Translation: 426.0, Folding: 42.6 | 47,170 | UniprotID: P37906 ECnumber: EC 1.4.3.- |
FUNCTION: Involved in the breakdown of putrescine via the oxidation of L-glutamylputrescine. {ECO:0000269|PubMed:15590624}. | |
| b1300 | b1300 | NADP/NAD-dependent aldehyde dehydrogenase PuuC (ALDH) (EC 1.2.1.5) (3-hydroxypropionaldehyde dehydrogenase) (Gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase) (Gamma-Glu-gamma-aminobutyraldehyde dehydrogenase) | Cytoplasm | R_ALDD2x_enzyme R_GGGABADr_enzyme |
R_ALDD2x R_GGGABADr |
495 | Translation: 495.0, Folding: 49.5 | 53,419 | UniprotID: P23883 ECnumber: EC 1.2.1.5 |
FUNCTION: Catalyzes the oxidation of 3-hydroxypropionaldehyde (3-HPA) to 3-hydroxypropionic acid (3-HP) (PubMed:18668238). It acts preferentially with NAD but can also use NADP (PubMed:18668238). 3-HPA appears to be the most suitable substrate for PuuC followed by isovaleraldehyde, propionaldehyde, butyraldehyde, and valeraldehyde (PubMed:18668238). It might play a role in propionate and/or acetic acid metabolisms (PubMed:18668238). Also involved in the breakdown of putrescine through the oxidation of gamma-Glu-gamma-aminobutyraldehyde to gamma-Glu-gamma-aminobutyrate (gamma-Glu-GABA) (PubMed:15590624). {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:18668238, ECO:0000305|PubMed:1840553}. |
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| b2800 | b2800 | L-fuculose phosphate aldolase (EC 4.1.2.17) (L-fuculose-1-phosphate aldolase) | Cytoplasm | R_FCLPA_duplicate_2_enzyme | R_FCLPA_duplicate_2 | 215 | Translation: 215.0, Folding: 21.5 | 23,775 | UniprotID: P0AB87 ECnumber: EC 4.1.2.17 |
FUNCTION: Catalyzes the cleavage of L-fuculose 1-phosphate to glycerone phosphate and L-lactaldehyde. {ECO:0000255|HAMAP-Rule:MF_00987, ECO:0000269|PubMed:13898172}. | |
| b1308 | b1308 | Thiosulfate sulfurtransferase PspE (TST) (EC 2.8.1.1) (Phage shock protein E) | Periplasm | R_CYANSTpp_enzyme | R_CYANSTpp | 104 | Secretion: 104.0, Translation: 104.0, Folding: 10.4 | 11,475 | UniprotID: P23857 ECnumber: EC 2.8.1.1 |
FUNCTION: The phage shock protein (psp) operon (pspABCDE) may play a significant role in the competition for survival under nutrient- or energy-limited conditions. PspE catalyzes the sulfur-transfer reaction from thiosulfate to cyanide, to form sulfite and thiocyanate. Also able to use dithiol (dithiothreitol) as an alternate sulfur acceptor. Also possesses a very low mercaptopyruvate sulfurtransferase activity. |
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| b3945 | b3945 | Glycerol dehydrogenase (GDH) (GLDH) (EC 1.1.1.6) | Cytoplasm | R_ALR4x_enzyme R_APPLDHr_enzyme R_GLYCDx_enzyme R_LALDO2x_enzyme |
R_ALR4x R_APPLDHr R_GLYCDx R_LALDO2x |
367 | Translation: 367.0, Folding: 36.7 | 38,712 | UniprotID: P0A9S5 ECnumber: EC 1.1.1.6 |
FUNCTION: Catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). Allows microorganisms to utilize glycerol as a source of carbon under anaerobic conditions. In E.coli, an important role of GldA is also likely to regulate the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. Possesses a broad substrate specificity, since it is also able to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively. {ECO:0000269|PubMed:18179582, ECO:0000269|PubMed:18632294, ECO:0000269|PubMed:40950, ECO:0000269|PubMed:8132480}. |
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| b0185 | b0185 | Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha (ACCase subunit alpha) (Acetyl-CoA carboxylase carboxyltransferase subunit alpha) (EC 6.4.1.2) | Cytoplasm | R_ACCOAC_enzyme | R_ACCOAC | 319 | Translation: 319.0, Folding: 31.9 | 35,242 | UniprotID: P0ABD5 ECnumber: EC 6.4.1.2 |
FUNCTION: Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00823, ECO:0000269|PubMed:15066985}. | |
| b4268 | b4268 | Thermosensitive gluconokinase (EC 2.7.1.12) (Gluconate kinase 1) | Cytoplasm | R_GNK_enzyme | R_GNK | 187 | Translation: 187.0, Folding: 18.7 | 21,004 | UniprotID: P39208 ECnumber: EC 2.7.1.12 |
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| b4262 | b4262 | Lipopolysaccharide export system permease protein LptG | Cell_inner_membrane | 360 | Secretion: 360.0, Translation: 360.0, Folding: 36.0 | 39,619 | UniprotID: P0ADC6 | FUNCTION: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. {ECO:0000269|PubMed:18375759}. | |||
| b4261 | b4261 | Lipopolysaccharide export system permease protein LptF | Cell_inner_membrane | 366 | Secretion: 366.0, Translation: 366.0, Folding: 36.6 | 40,358 | UniprotID: P0AF98 | FUNCTION: Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. {ECO:0000269|PubMed:18375759}. | |||
| b4260 | b4260 | Cytosol aminopeptidase (EC 3.4.11.1) (Aminopeptidase A/I) (Leucine aminopeptidase) (LAP) (EC 3.4.11.10) (Leucyl aminopeptidase) | Cytoplasm | R_AMPTASECG_enzyme R_AMPTASEPG_duplicate_2_enzyme |
R_AMPTASECG R_AMPTASEPG_duplicate_2 |
503 | Translation: 503.0, Folding: 50.3 | 54,880 | UniprotID: P68767 ECnumber: EC 3.4.11.1; 3.4.11.10 |
FUNCTION: Probably involved in the processing and regular turnover of intracellular proteins (PubMed:20067529). Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place (PubMed:8057849). {ECO:0000269|PubMed:8057849, ECO:0000305|PubMed:20067529}. |
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| b4267 | b4267 | L-idonate 5-dehydrogenase (NAD(P)(+)) (EC 1.1.1.264) | Cytoplasm | R_IDOND_enzyme R_IDOND2_enzyme |
R_IDOND R_IDOND2 |
343 | Translation: 343.0, Folding: 34.3 | 37,147 | UniprotID: P39346 ECnumber: EC 1.1.1.264 |
FUNCTION: Catalyzes the NADH/NADPH-dependent oxidation of L-idonate to 5-ketogluconate (5KG). {ECO:0000269|PubMed:9658018}. | |
| b4266 | b4266 | 5-keto-D-gluconate 5-reductase (EC 1.1.1.69) | Cytoplasm | R_5DGLCNR_enzyme | R_5DGLCNR | 254 | Translation: 254.0, Folding: 25.4 | 27,563 | UniprotID: P0A9P9 ECnumber: EC 1.1.1.69 |
FUNCTION: Catalyzes the reduction of 5-keto-D-gluconate to D-gluconate, using either NADH or NADPH. Is likely involved in an L-idonate degradation pathway that allows E.coli to utilize L-idonate as the sole carbon and energy source. Is also able to catalyze the reverse reaction in vitro, but the D-gluconate oxidation by the enzyme can only proceed with NAD. {ECO:0000269|PubMed:9658018}. | |
| b4265 | b4265 | Gnt-II system L-idonate transporter (L-Ido transporter) (5-keto-D-gluconate transporter) | Cell_inner_membrane | R_5DGLCNt2rpp_enzyme R_GLCNt2rpp_duplicate_4_enzyme R_IDONt2rpp_enzyme |
R_5DGLCNt2rpp R_GLCNt2rpp_duplicate_4 R_IDONt2rpp |
439 | Secretion: 439.0, Translation: 439.0, Folding: 43.9 | 46,041 | UniprotID: P39344 | FUNCTION: Transports L-idonate, D-gluconate and 5-keto-D-gluconate, from the periplasm across the inner membrane. {ECO:0000269|PubMed:17088549, ECO:0000269|PubMed:9658018}. | |
| b3942 | b3942 | Catalase-peroxidase (CP) (EC 1.11.1.21) (Hydroperoxidase I) (HPI) (Peroxidase/catalase) | Cytoplasm | R_CAT_duplicate_2_enzyme | R_CAT_duplicate_2 | 726 | Translation: 726.0, Folding: 72.6 | 80,024 | UniprotID: P13029 ECnumber: EC 1.11.1.21 |
FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity. {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:23416055, ECO:0000269|PubMed:374409}. | |
| b2418 | b2418 | Pyridoxine/pyridoxal/pyridoxamine kinase (PN/PL/PM kinase) (EC 2.7.1.35) (B6-vitamer kinase) (Pyridoxal kinase 1) (PL kinase 1) | Cytoplasm | R_HMPK1_duplicate_2_enzyme R_PYDAMK_enzyme R_PYDXK_duplicate_2_enzyme R_PYDXNK_enzyme |
R_HMPK1_duplicate_2 R_PYDAMK R_PYDXK_duplicate_2 R_PYDXNK |
283 | Translation: 283.0, Folding: 28.3 | 30,847 | UniprotID: P40191 ECnumber: EC 2.7.1.35 |
FUNCTION: B6-vitamer kinase involved in the salvage pathway of pyridoxal 5-phosphate (PLP). Catalyzes the phosphorylation of pyridoxine (PN), pyridoxal (PL), and pyridoxamine (PM), forming their respective 5-phosphorylated esters, i.e. PNP, PLP and PMP. {ECO:0000269|PubMed:15249053, ECO:0000269|PubMed:9537380}. | |
| b3940 | b3940 | Bifunctional aspartokinase/homoserine dehydrogenase 2 (Aspartokinase II/homoserine dehydrogenase II) (AKII-HDII) [Includes: Aspartokinase (EC 2.7.2.4); Homoserine dehydrogenase (EC 1.1.1.3) | Cytoplasm | R_ASPK_enzyme R_HSDy_enzyme |
R_ASPK R_HSDy |
810 | Translation: 810.0, Folding: 81.0 | 88,888 | UniprotID: P00562 ECnumber: EC 2.7.2.4; 1.1.1.3 |
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| b0638 | b0638 | Adenosylcobalamin/alpha-ribazole phosphatase (EC 3.1.3.73) (Adenosylcobalamin phosphatase) (Alpha-ribazole-5-phosphate phosphatase) | Cytoplasm | R_RZ5PP_enzyme | R_RZ5PP | 203 | Translation: 203.0, Folding: 20.3 | 23,308 | UniprotID: P52086 ECnumber: EC 3.1.3.73 |
FUNCTION: Catalyzes the conversion of adenosylcobalamin 5-phosphate to adenosylcobalamin (vitamin B12); involved in the assembly of the nucleotide loop of cobalamin. Also catalyzes the hydrolysis of the phospho group from alpha-ribazole 5-phosphate to form alpha-ribazole. {ECO:0000250|UniProtKB:P39701}. | |
| b1236 | b1236 | UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Alpha-D-glucosyl-1-phosphate uridylyltransferase) (UDP-glucose pyrophosphorylase) (UDPGP) (Uridine diphosphoglucose pyrophosphorylase) | Cytoplasm | R_GALUi_enzyme | R_GALUi | 302 | Translation: 302.0, Folding: 30.2 | 32,942 | UniprotID: P0AEP3 ECnumber: EC 2.7.7.9 |
FUNCTION: May play a role in stationary phase survival. | |
| b1232 | b1232 | Formyltetrahydrofolate deformylase (EC 3.5.1.10) (Formyl-FH(4) hydrolase) | Cytoplasm | R_FTHFD_enzyme | R_FTHFD | 280 | Translation: 280.0, Folding: 28.0 | 31,935 | UniprotID: P37051 ECnumber: EC 3.5.1.10 |
FUNCTION: Catalyzes the hydrolysis of 10-formyltetrahydrofolate (formyl-FH4) to formate and tetrahydrofolate (FH4). Provides the major source of formate for the PurT-dependent synthesis of 5-phosphoribosyl-N-formylglycinamide (FGAR) during aerobic growth. Has a role in regulating the one-carbon pool. {ECO:0000255|HAMAP-Rule:MF_01927, ECO:0000269|PubMed:7868604}. | |
| b0630 | b0630 | Octanoyltransferase (EC 2.3.1.181) (Lipoate-protein ligase B) (Lipoyl/octanoyl transferase) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase) | Cytoplasm | R_LIPOCT_enzyme | R_LIPOCT | 213 | Translation: 213.0, Folding: 21.3 | 23,883 | UniprotID: P60720 ECnumber: EC 2.3.1.181 |
FUNCTION: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate. {ECO:0000255|HAMAP-Rule:MF_00013, ECO:0000269|PubMed:15642479, ECO:0000269|PubMed:16342964}. | |
| b0632 | b0632 | D-alanyl-D-alanine carboxypeptidase DacA (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (Beta-lactamase) (EC 3.5.2.6) (Penicillin-binding protein 5) (PBP-5) | Cell_inner_membrane | R_MDDCP1pp_duplicate_2 R_MDDCP2pp_duplicate_2 R_MDDCP3pp_duplicate_2 R_MDDCP4pp_duplicate_2 R_MDDCP5pp_duplicate_2 |
403 | Secretion: 403.0, Translation: 403.0, Folding: 40.3 | 44,444 | UniprotID: P0AEB2 ECnumber: EC 3.4.16.4; 3.5.2.6 |
FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | ||
| b0635 | b0635 | Peptidoglycan D,D-transpeptidase MrdA (EC 3.4.16.4) (Penicillin-binding protein 2) (PBP-2) | Cell_inner_membrane | R_MCTP1App_duplicate_3_enzyme R_MCTP2App_duplicate_3_enzyme |
R_MCTP1App_duplicate_3 R_MCTP2App_duplicate_3 |
633 | Secretion: 633.0, Translation: 633.0, Folding: 63.3 | 70,857 | UniprotID: P0AD65 ECnumber: EC 3.4.16.4 |
FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall (PubMed:3009484). Responsible for the determination of the rod shape of the cell (PubMed:1103132). Is probably required for lateral peptidoglycan synthesis and maintenance of the correct diameter during lateral and centripetal growth (PubMed:12519203). {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:12519203, ECO:0000269|PubMed:3009484}. |
|
| b1238 | b1238 | Thymidine kinase (EC 2.7.1.21) | Cytoplasm | R_DURIK1_enzyme R_TMDK1_enzyme |
R_DURIK1 R_TMDK1 |
205 | Translation: 205.0, Folding: 20.5 | 23,457 | UniprotID: P23331 ECnumber: EC 2.7.1.21 |
FUNCTION: Phosphorylates both thymidine and deoxyuridine. | |
| b2415 | b2415 | Phosphocarrier protein HPr (Histidine-containing protein) | Cytoplasm | R_ACGAptspp_enzyme R_ACGAptspp_duplicate_2_enzyme R_ACMANAptspp_enzyme R_ACMUMptspp_enzyme R_ARBTptspp_enzyme R_ARBTptspp_duplicate_2_enzyme R_ASCBptspp_enzyme R_DHAPT_enzyme R_FRUpts2pp_enzyme R_FRUptspp_enzyme R_GALTptspp_enzyme R_GAMptspp_enzyme R_GLCptspp_enzyme R_GLCptspp_duplicate_2_enzyme R_GLCptspp_duplicate_3_enzyme R_MALTptspp_enzyme R_MANGLYCptspp_enzyme R_MANptspp_enzyme R_MNLptspp_enzyme R_SBTptspp_enzyme R_SUCptspp_enzyme R_TREptspp_enzyme |
85 | Translation: 85.0, Folding: 8.5 | 9,119 | UniprotID: P0AA04 | FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl group from phosphoenolpyruvate (PEP) is transferred to the phosphoryl carrier protein HPr by enzyme I. Phospho-HPr then transfers it to the PTS EIIA domain. |
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| b4042 | b4042 | Diacylglycerol kinase (DAGK) (EC 2.7.1.107) (Diglyceride kinase) (DGK) | Cell_inner_membrane | R_DAGK120 R_DAGK140 R_DAGK141 R_DAGK160 R_DAGK161 R_DAGK180 R_DAGK181 |
122 | Secretion: 122.0, Translation: 122.0, Folding: 12.2 | 13,245 | UniprotID: P0ABN1 ECnumber: EC 2.7.1.107 |
FUNCTION: Recycling of diacylglycerol produced during the turnover of membrane phospholipid. | ||
| b4041 | b4041 | Glycerol-3-phosphate acyltransferase (GPAT) (EC 2.3.1.15) | Cell_inner_membrane | R_G3PAT120 R_G3PAT140 R_G3PAT141 R_G3PAT160 R_G3PAT161 R_G3PAT180 R_G3PAT181 |
807 | Secretion: 807.0, Translation: 807.0, Folding: 80.7 | 91,381 | UniprotID: P0A7A7 ECnumber: EC 2.3.1.15 |
FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor. {ECO:0000269|PubMed:17645809, ECO:0000269|PubMed:6997313}. | ||
| b4040 | b4040 | 4-hydroxybenzoate octaprenyltransferase (EC 2.5.1.-) (4-HB polyprenyltransferase) | Cell_inner_membrane | R_HBZOPT_enzyme | R_HBZOPT | 290 | Secretion: 290.0, Translation: 290.0, Folding: 29.0 | 32,512 | UniprotID: P0AGK1 ECnumber: EC 2.5.1.- |
FUNCTION: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-octaprenyl-4-hydroxybenzoate. {ECO:0000255|HAMAP-Rule:MF_01635, ECO:0000269|PubMed:7765507, ECO:0000269|PubMed:8155731}. |
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| b0019 | b0019 | Na(+)/H(+) antiporter NhaA (Sodium/proton antiporter NhaA) | Cell_inner_membrane | R_NAt3_2pp_enzyme | R_NAt3_2pp | 388 | Secretion: 388.0, Translation: 388.0, Folding: 38.8 | 41,356 | UniprotID: P13738 | FUNCTION: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons. Catalyzes the exchange of 2 H(+) per Na(+). Can mediate sodium uptake when a transmembrane pH gradient is applied. Active at alkaline pH. Activity is strongly down-regulated below pH 6.5. {ECO:0000269|PubMed:1645730}. | |
| b2143 | b2143 | Cytidine deaminase (EC 3.5.4.5) (Cytidine aminohydrolase) (CDA) | Cytoplasm | R_CYTD_enzyme R_DCYTD_enzyme |
R_CYTD R_DCYTD |
294 | Translation: 294.0, Folding: 29.4 | 31,540 | UniprotID: P0ABF6 ECnumber: EC 3.5.4.5 |
FUNCTION: This enzyme scavenges exogenous and endogenous cytidine and 2-deoxycytidine for UMP synthesis. | |
| b0494 | b0494 | Thioesterase 1/protease 1/lysophospholipase L1 (TAP) (Acyl-CoA thioesterase 1) (TESA) (EC 3.1.2.2) (Acyl-CoA thioesterase I) (Arylesterase) (EC 3.1.1.2) (Lysophospholipase L1) (EC 3.1.1.5) (Oleoyl-[acyl-carrier-protein] hydrolase) (EC 3.1.2.14) (Phospholipid degradation C) (Pldc) (Protease 1) (EC 3.4.21.-) (Protease I) (Thioesterase I/protease I) (TEP-I) | Periplasm | R_LPLIPAL1A120pp_enzyme R_LPLIPAL1A140pp_enzyme R_LPLIPAL1A141pp_enzyme R_LPLIPAL1A160pp_enzyme R_LPLIPAL1A161pp_enzyme R_LPLIPAL1A180pp_enzyme R_LPLIPAL1A181pp_enzyme R_LPLIPAL1E120pp_enzyme R_LPLIPAL1E140pp_enzyme R_LPLIPAL1E141pp_enzyme R_LPLIPAL1E160pp_enzyme R_LPLIPAL1E161pp_enzyme R_LPLIPAL1E180pp_enzyme R_LPLIPAL1E181pp_enzyme R_LPLIPAL1G120pp_enzyme R_LPLIPAL1G140pp_enzyme R_LPLIPAL1G141pp_enzyme R_LPLIPAL1G160pp_enzyme R_LPLIPAL1G161pp_enzyme R_LPLIPAL1G180pp_enzyme R_LPLIPAL1G181pp_enzyme |
R_LPLIPAL1A120pp R_LPLIPAL1A140pp R_LPLIPAL1A141pp R_LPLIPAL1A160pp R_LPLIPAL1A161pp R_LPLIPAL1A180pp R_LPLIPAL1A181pp R_LPLIPAL1E120pp R_LPLIPAL1E140pp R_LPLIPAL1E141pp R_LPLIPAL1E160pp R_LPLIPAL1E161pp R_LPLIPAL1E180pp R_LPLIPAL1E181pp R_LPLIPAL1G120pp R_LPLIPAL1G140pp R_LPLIPAL1G141pp R_LPLIPAL1G160pp R_LPLIPAL1G161pp R_LPLIPAL1G180pp R_LPLIPAL1G181pp |
208 | Secretion: 208.0, Translation: 208.0, Folding: 20.8 | 23,622 | UniprotID: P0ADA1 ECnumber: EC 3.1.2.2; 3.1.1.2; 3.1.1.5; 3.1.2.14; 3.4.21.- |
FUNCTION: TesA is a multifunctional esterase that can act as a thioesterase, lysophospholipase and protease (PubMed:8098033, PubMed:8432696, PubMed:1864840, PubMed:4945109, PubMed:4554913, PubMed:238979, PubMed:791643, PubMed:8132479, PubMed:9070299, PubMed:10423542). TesA functions as a thioesterase specific for fatty acyl thioesters of greater than ten carbons, with highest activity on palmitoyl-CoA, cis-vaccenyl-CoA and palmitoleoyl-CoA (PubMed:8098033, PubMed:4554913, PubMed:8132479, PubMed:9070299, PubMed:10423542). TesA also possesses an arylesterase activity towards short acyl-chain aromatic esters such as alpha-naphthyl acetate, alpha-naphthyl butyrate, benzyl acetate and phenyl acetate (PubMed:9070299). Also able to hydrolyze short acyl-chain triacylglycerols such as triacetin and tributyrin, and p-nitrophenyl esters such as p-nitrophenyl hexanoate and p-nitrophenyl butyrate (PubMed:9070299). The protease activity is mainly active on small peptides (PubMed:8432696, PubMed:9070299). TesA is also able to hydrolyze p-nitrophenyl esters of N-substituted amino acids such as N-benzyloxycarbonyl-L-Phe-p-nitrophenyl ester (Z-L-Phe-ONp) and N-benzyloxycarbonyl-L-Tyr-p-nitrophenyl ester (Z-L-Tyr-ONp), however it is unable to hydrolyze N-acetyl-L-Phe ethyl ester and its Tyr analog (PubMed:8432696, PubMed:791643, PubMed:10423542). TesA also hydrolyzes N-benzyloxycarbonyl-L-Phe beta-nitrophenyl ester (Cbz-Phe-ONap) and N-acetyl-DL-Phe-2-naphthyl ester (chymotrypsin-like specificity) (PubMed:8432696, PubMed:4945109). Shows a slow proteolytic activity against denatured casein (PubMed:4945109). The lysophospholipase activity of TesA is able to hydrolyze 1-palmitoyl-sn-glycero-3-phosphocholine, 1-acyl-sn-glycero-3-phosphoglycerol, 1- and 2-acyl-sn-glycero-3-phosphoethanolamine (PubMed:1864840, PubMed:238979, PubMed:10423542). {ECO:0000269|PubMed:10423542, ECO:0000269|PubMed:1864840, ECO:0000269|PubMed:238979, ECO:0000269|PubMed:4554913, ECO:0000269|PubMed:4945109, ECO:0000269|PubMed:791643, ECO:0000269|PubMed:8098033, ECO:0000269|PubMed:8132479, ECO:0000269|PubMed:8432696, ECO:0000269|PubMed:9070299}. |
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| b0124 | b0124 | Quinoprotein glucose dehydrogenase (EC 1.1.5.2) (Glucose dehydrogenase [pyrroloquinoline-quinone]) | Cell_inner_membrane | R_GLCDpp_enzyme | R_GLCDpp | 796 | Secretion: 796.0, Translation: 796.0, Folding: 79.6 | 86,747 | UniprotID: P15877 ECnumber: EC 1.1.5.2 |
FUNCTION: GDH is probably involved in energy conservation rather than in sugar metabolism. | |
| b0125 | b0125 | Hypoxanthine phosphoribosyltransferase (HPRT) (EC 2.4.2.8) | Cytoplasm | R_GUAPRT_duplicate_2_enzyme R_HXPRT_duplicate_2_enzyme |
R_GUAPRT_duplicate_2 R_HXPRT_duplicate_2 |
178 | Translation: 178.0, Folding: 17.8 | 20,115 | UniprotID: P0A9M2 ECnumber: EC 2.4.2.8 |
FUNCTION: Acts preferentially on hypoxanthine; has very low activity towards guanine. Inactive towards xanthine. {ECO:0000269|PubMed:12070315}. | |
| b0126 | b0126 | Carbonic anhydrase 2 (EC 4.2.1.1) (Carbonate dehydratase 2) | Cytoplasm | R_HCO3E_enzyme | R_HCO3E | 220 | Translation: 220.0, Folding: 22.0 | 25,097 | UniprotID: P61517 ECnumber: EC 4.2.1.1 |
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| b0120 | b0120 | S-adenosylmethionine decarboxylase proenzyme (AdoMetDC) (SAMDC) (EC 4.1.1.50) [Cleaved into: S-adenosylmethionine decarboxylase beta chain; S-adenosylmethionine decarboxylase alpha chain | Cytoplasm | R_ADMDC_enzyme | R_ADMDC | 264 | Translation: 264.0, Folding: 26.4 | 30,385 | UniprotID: P0A7F6 ECnumber: EC 4.1.1.50 |
FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine. | |
| b0121 | b0121 | Polyamine aminopropyltransferase (Cadaverine aminopropyltransferase) (EC 2.5.1.-) (Putrescine aminopropyltransferase) (PAPT) (Spermidine aminopropyltransferase) (EC 2.5.1.79) (Spermidine synthase) (SPDS) (SPDSY) (EC 2.5.1.16) (Spermine synthase) (EC 2.5.1.22) (Thermospermine synthase) | Cytoplasm | R_APCS_enzyme R_SPMS_enzyme |
R_APCS R_SPMS |
288 | Translation: 288.0, Folding: 28.8 | 32,321 | UniprotID: P09158 ECnumber: EC 2.5.1.-; 2.5.1.79; 2.5.1.16; 2.5.1.22 |
FUNCTION: Involved in the biosynthesis of polyamines which play a significant role in the structural and functional organization in the chromoid of E.coli by compacting DNA and neutralizing negative charges. Catalyzes the irreversible transfer (ping-pong mechanism) of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. Cadaverine (1,5-diaminopentane) and spermidine can also be used as the propylamine acceptor. {ECO:0000269|PubMed:23001854, ECO:0000269|PubMed:4572733}. |
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| b0123 | b0123 | Blue copper oxidase CueO (Copper efflux oxidase) | Periplasm | R_CU1Opp_enzyme R_FEROpp_enzyme |
R_CU1Opp R_FEROpp |
516 | Secretion: 516.0, Translation: 516.0, Folding: 51.6 | 56,556 | UniprotID: P36649 | FUNCTION: Probably involved in periplasmic detoxification of copper by oxidizing Cu(+) to Cu(2+) and thus preventing its uptake into the cytoplasm. Possesses phenoloxidase and ferroxidase activities and might be involved in the production of polyphenolic compounds and the prevention of oxidative damage in the periplasm. | |
| b0945 | b0945 | Dihydroorotate dehydrogenase (quinone) (EC 1.3.5.2) (DHOdehase) (DHOD) (DHODase) (Dihydroorotate oxidase) | Cell_inner_membrane | R_DHORD2_enzyme R_DHORD5_enzyme |
R_DHORD2 R_DHORD5 |
336 | Secretion: 336.0, Translation: 336.0, Folding: 33.6 | 36,775 | UniprotID: P0A7E1 ECnumber: EC 1.3.5.2 |
FUNCTION: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. {ECO:0000269|PubMed:10074342}. | |
| b0308 | b0308 | Uncharacterized protein YkgG | Cytoplasm | R_L_LACD2_duplicate_2_enzyme R_L_LACD3_duplicate_2_enzyme |
R_L_LACD2_duplicate_2 R_L_LACD3_duplicate_2 |
231 | Translation: 231.0, Folding: 23.1 | 25,213 | UniprotID: P77433 | ||
| b0306 | b0306 | Uncharacterized protein YkgE | Cytoplasm | R_L_LACD2_duplicate_2_enzyme R_L_LACD3_duplicate_2_enzyme |
R_L_LACD2_duplicate_2 R_L_LACD3_duplicate_2 |
239 | Translation: 239.0, Folding: 23.9 | 26,004 | UniprotID: P77252 | ||
| b0307 | b0307 | Uncharacterized electron transport protein YkgF | Cytoplasm | R_L_LACD2_duplicate_2_enzyme R_L_LACD3_duplicate_2_enzyme |
R_L_LACD2_duplicate_2 R_L_LACD3_duplicate_2 |
475 | Translation: 475.0, Folding: 47.5 | 53,052 | UniprotID: P77536 | ||
| b0720 | b0720 | Citrate synthase (EC 2.3.3.16) | Cytoplasm | R_CS_enzyme | R_CS | 427 | Translation: 427.0, Folding: 42.7 | 48,015 | UniprotID: P0ABH7 ECnumber: EC 2.3.3.16 |
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| b2963 | b2963 | Membrane-bound lytic murein transglycosylase C (EC 4.2.2.n1) (Murein lyase C) | Cell_outer_membrane | R_MLTGY1pp_duplicate_4_enzyme R_MLTGY2pp_duplicate_2_enzyme R_MLTGY3pp_duplicate_4_enzyme R_MLTGY4pp_duplicate_2_enzyme |
R_MLTGY1pp_duplicate_4 R_MLTGY2pp_duplicate_2 R_MLTGY3pp_duplicate_4 R_MLTGY4pp_duplicate_2 |
359 | Secretion: 359.0, Translation: 359.0, Folding: 35.9 | 40,113 | UniprotID: P0C066 ECnumber: EC 4.2.2.n1 |
FUNCTION: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. {ECO:0000255|HAMAP-Rule:MF_01616}. | |
| b1388 | b1388 | 1,2-phenylacetyl-CoA epoxidase, subunit A (EC 1.14.13.149) (1,2-phenylacetyl-CoA epoxidase, catalytic subunit alpha) (1,2-phenylacetyl-CoA monooxygenase, subunit A) | Cytoplasm | R_PACCOAE_enzyme | R_PACCOAE | 309 | Translation: 309.0, Folding: 30.9 | 35,499 | UniprotID: P76077 ECnumber: EC 1.14.13.149 |
FUNCTION: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA. {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:21247899, ECO:0000269|PubMed:9748275}. |
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| b0894 | b0894 | Dimethyl sulfoxide reductase DmsA (DMSO reductase) (DMSOR) (Me2SO reductase) (EC 1.8.5.3) | Cell_inner_membrane | R_DMSOR1_duplicate_2_enzyme R_DMSOR2_enzyme R_TMAOR1_enzyme R_TMAOR2_enzyme |
R_DMSOR1_duplicate_2 R_DMSOR2 R_TMAOR1 R_TMAOR2 |
814 | Secretion: 814.0, Translation: 814.0, Folding: 81.4 | 90,399 | UniprotID: P18775 ECnumber: EC 1.8.5.3 |
FUNCTION: Catalyzes the reduction of dimethyl sulfoxide (DMSO) to dimethyl sulfide (DMS). DMSO reductase serves as the terminal reductase under anaerobic conditions, with DMSO being the terminal electron acceptor. Terminal reductase during anaerobic growth on various sulfoxides and N-oxide compounds. Allows E.coli to grow anaerobically on DMSO as respiratory oxidant. {ECO:0000269|PubMed:3062312}. |
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| b0727 | b0727 | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex (EC 2.3.1.61) (2-oxoglutarate dehydrogenase complex component E2) (OGDC-E2) (Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex) | Cytoplasm | R_AKGDH_enzyme | R_AKGDH | 405 | Translation: 405.0, Folding: 40.5 | 44,011 | UniprotID: P0AFG6 ECnumber: EC 2.3.1.61 |
FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). | |
| b0896 | b0896 | Anaerobic dimethyl sulfoxide reductase chain C (DMSO reductase anchor subunit) | Cell_inner_membrane | R_DMSOR1_duplicate_2_enzyme R_DMSOR2_enzyme R_TMAOR1_enzyme R_TMAOR2_enzyme |
R_DMSOR1_duplicate_2 R_DMSOR2 R_TMAOR1 R_TMAOR2 |
287 | Secretion: 287.0, Translation: 287.0, Folding: 28.7 | 30,826 | UniprotID: P18777 | FUNCTION: Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. DmsC anchors the DmsAB dimer to the membrane and stabilizes it. | |
| b1380 | b1380 | D-lactate dehydrogenase (D-LDH) (EC 1.1.1.28) (Fermentative lactate dehydrogenase) | Cytoplasm | R_LDH_D_duplicate_2_enzyme | R_LDH_D_duplicate_2 | 329 | Translation: 329.0, Folding: 32.9 | 36,535 | UniprotID: P52643 ECnumber: EC 1.1.1.28 |
FUNCTION: Fermentative lactate dehydrogenase. | |
| b3543 | b3543 | Dipeptide transport system permease protein DppB | Cell_inner_membrane | R_ALAALAabcpp_duplicate_2_enzyme R_CGLYabcpp_enzyme R_PROGLYabcpp_enzyme |
R_ALAALAabcpp_duplicate_2 R_CGLYabcpp R_PROGLYabcpp |
339 | Secretion: 339.0, Translation: 339.0, Folding: 33.9 | 37,497 | UniprotID: P0AEF8 | FUNCTION: Part of the binding-protein-dependent transport system for dipeptides; probably responsible for the translocation of the substrate across the membrane. | |
| b3542 | b3542 | Dipeptide transport system permease protein DppC | Cell_inner_membrane | R_ALAALAabcpp_duplicate_2_enzyme R_CGLYabcpp_enzyme R_PROGLYabcpp_enzyme |
R_ALAALAabcpp_duplicate_2 R_CGLYabcpp R_PROGLYabcpp |
300 | Secretion: 300.0, Translation: 300.0, Folding: 30.0 | 32,308 | UniprotID: P0AEG1 | FUNCTION: Part of the binding-protein-dependent transport system for dipeptides; probably responsible for the translocation of the substrate across the membrane. | |
| b3541 | b3541 | Dipeptide transport ATP-binding protein DppD | Cell_inner_membrane | R_ALAALAabcpp_duplicate_2_enzyme R_CGLYabcpp_enzyme R_PROGLYabcpp_enzyme |
R_ALAALAabcpp_duplicate_2 R_CGLYabcpp R_PROGLYabcpp |
327 | Secretion: 327.0, Translation: 327.0, Folding: 32.7 | 35,844 | UniprotID: P0AAG0 | FUNCTION: Part of the binding-protein-dependent transport system for dipeptides. Probably responsible for energy coupling to the transport system. | |
| b3540 | b3540 | Dipeptide transport ATP-binding protein DppF | Cell_inner_membrane | R_ALAALAabcpp_duplicate_2_enzyme R_CGLYabcpp_enzyme R_PROGLYabcpp_enzyme |
R_ALAALAabcpp_duplicate_2 R_CGLYabcpp R_PROGLYabcpp |
334 | Secretion: 334.0, Translation: 334.0, Folding: 33.4 | 37,560 | UniprotID: P37313 | FUNCTION: Part of the binding-protein-dependent transport system for dipeptides. Probably responsible for energy coupling to the transport system. | |
| b3546 | b3546 | Kdo(2)-lipid A phosphoethanolamine 7-transferase (EC 2.7.8.42) (Phosphoethanolamine transferase EptB) | Cell_inner_membrane | R_PETNT161pp_enzyme R_PETNT181pp_enzyme |
R_PETNT161pp R_PETNT181pp |
563 | Secretion: 563.0, Translation: 563.0, Folding: 56.3 | 63,804 | UniprotID: P37661 ECnumber: EC 2.7.8.42 |
FUNCTION: Catalyzes the addition of a phosphoethanolamine (pEtN) moiety to the outer 3-deoxy-D-manno-octulosonic acid (Kdo) residue of a Kdo(2)-lipid A. Phosphatidylethanolamines with one unsaturated acyl group functions as pEtN donors and the reaction releases diacylglycerol. {ECO:0000269|PubMed:15795227}. | |
| b3544 | b3544 | Periplasmic dipeptide transport protein (Dipeptide-binding protein) (DBP) | Periplasm | R_ALAALAabcpp_duplicate_2_enzyme R_CGLYabcpp_enzyme R_PROGLYabcpp_enzyme |
R_ALAALAabcpp_duplicate_2 R_CGLYabcpp R_PROGLYabcpp |
535 | Secretion: 535.0, Translation: 535.0, Folding: 53.5 | 60,294 | UniprotID: P23847 | FUNCTION: Dipeptide-binding protein of a transport system that can be subject to osmotic shock. DppA is also required for peptide chemotaxis. | |
| b0576 | b0576 | Phenylalanine-specific permease | Cell_inner_membrane | R_PHEt2rpp_duplicate_3_enzyme R_TYRt2rpp_duplicate_4_enzyme |
R_PHEt2rpp_duplicate_3 R_TYRt2rpp_duplicate_4 |
458 | Secretion: 458.0, Translation: 458.0, Folding: 45.8 | 50,677 | UniprotID: P24207 | FUNCTION: Permease that is involved in the transport across the cytoplasmic membrane of phenylalanine. | |
| b2303 | b2303 | Dihydroneopterin triphosphate 2-epimerase (EC 5.1.99.-) (D-erythro-7,8-dihydroneopterin triphosphate epimerase) | Cytoplasm | R_DHPTPE_enzyme | R_DHPTPE | 120 | Translation: 120.0, Folding: 12.0 | 14,082 | UniprotID: P0AC19 ECnumber: EC 5.1.99.- |
FUNCTION: Catalyzes the epimerization of carbon 2 of the side chain of 7,8-dihydroneopterin triphosphate (H2NTP) to form 7,8-dihydromonapterin triphosphate (H2MTP) (PubMed:9182560) (PubMed:9651328). Is required for tetrahydromonapterin biosynthesis, a major pterin in E.coli (PubMed:19897652). {ECO:0000269|PubMed:19897652, ECO:0000269|PubMed:9182560, ECO:0000269|PubMed:9651328}. | |
| b2306 | b2306 | Histidine transport ATP-binding protein HisP | Cell_inner_membrane | R_ARGabcpp_enzyme R_HISabcpp_enzyme R_LYSabcpp_enzyme R_ORNabcpp_enzyme |
R_ARGabcpp R_HISabcpp R_LYSabcpp R_ORNabcpp |
257 | Secretion: 257.0, Translation: 257.0, Folding: 25.7 | 28,653 | UniprotID: P07109 | FUNCTION: Part of the histidine permease ABC transporter. Also part of a lysine/arginine/ornithine transporter. Responsible for energy coupling to the transport system (By similarity). {ECO:0000250}. | |
| b2307 | b2307 | Histidine transport system permease protein HisM | Cell_inner_membrane | R_ARGabcpp_enzyme R_HISabcpp_enzyme R_LYSabcpp_enzyme R_ORNabcpp_enzyme |
R_ARGabcpp R_HISabcpp R_LYSabcpp R_ORNabcpp |
238 | Secretion: 238.0, Translation: 238.0, Folding: 23.8 | 26,870 | UniprotID: P0AEU3 | FUNCTION: Part of the histidine permease ABC transporter. Also part of a lysine/arginine/ornithine transporter. Probably responsible for the translocation of the substrate across the membrane. Required to relay the ATPase-inducing signal from the solute-binding protein to HisP (By similarity). {ECO:0000250}. | |
| b2308 | b2308 | Histidine transport system permease protein HisQ | Cell_inner_membrane | R_ARGabcpp_enzyme R_HISabcpp_enzyme R_LYSabcpp_enzyme R_ORNabcpp_enzyme |
R_ARGabcpp R_HISabcpp R_LYSabcpp R_ORNabcpp |
228 | Secretion: 228.0, Translation: 228.0, Folding: 22.8 | 24,649 | UniprotID: P52094 | FUNCTION: Part of the histidine permease ABC transporter. Also part of a lysine/arginine/ornithine transporter. Probably responsible for the translocation of the substrate across the membrane. Required to relay the ATPase-inducing signal from the solute-binding protein to HisP (By similarity). {ECO:0000250}. | |
| b2309 | b2309 | Histidine-binding periplasmic protein (HBP) | Periplasm | R_HISabcpp_enzyme | R_HISabcpp | 260 | Secretion: 260.0, Translation: 260.0, Folding: 26.0 | 28,483 | UniprotID: P0AEU0 | FUNCTION: Part of the histidine permease ABC transporter. Binds histidine. Interacts with HisQMP and stimulates ATPase activity of HisP, which results in histidine translocation (By similarity). {ECO:0000250}. | |
| b3433 | b3433 | Aspartate-semialdehyde dehydrogenase (ASA dehydrogenase) (ASADH) (EC 1.2.1.11) (Aspartate-beta-semialdehyde dehydrogenase) | Cytoplasm | R_ASAD_enzyme | R_ASAD | 367 | Translation: 367.0, Folding: 36.7 | 40,018 | UniprotID: P0A9Q9 ECnumber: EC 1.2.1.11 |
FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate. {ECO:0000269|PubMed:11368768, ECO:0000269|PubMed:6102909}. | |
| b3432 | b3432 | 1,4-alpha-glucan branching enzyme GlgB (EC 2.4.1.18) (1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase) (Alpha-(1->4)-glucan branching enzyme) (Glycogen branching enzyme) (BE) | Cytoplasm | R_GLBRAN2_enzyme | R_GLBRAN2 | 728 | Translation: 728.0, Folding: 72.8 | 84,337 | UniprotID: P07762 ECnumber: EC 2.4.1.18 |
FUNCTION: Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position. {ECO:0000250}. | |
| b2128 | b2128 | Glycine betaine uptake system permease protein YehW | Cell_inner_membrane | R_CHLabcpp_enzyme R_GLYBabcpp_enzyme |
R_CHLabcpp R_GLYBabcpp |
243 | Secretion: 243.0, Translation: 243.0, Folding: 24.3 | 25,515 | UniprotID: P33359 | FUNCTION: Part of an ABC transporter complex involved in low-affinity glycine betaine uptake. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:26325238}. | |
| b2129 | b2129 | Glycine betaine uptake system ATP-binding protein YehX (EC 3.6.3.-) | Cytoplasm | R_CHLabcpp_enzyme R_GLYBabcpp_enzyme |
R_CHLabcpp R_GLYBabcpp |
308 | Translation: 308.0, Folding: 30.8 | 34,425 | UniprotID: P33360 ECnumber: EC 3.6.3.- |
FUNCTION: Part of an ABC transporter complex involved in low-affinity glycine betaine uptake. Probably responsible for energy coupling to the transport system. {ECO:0000269|PubMed:26325238}. | |
| b3437 | b3437 | Thermoresistant gluconokinase (EC 2.7.1.12) (Gluconate kinase 2) | Cytoplasm | R_GNK_duplicate_2_enzyme | R_GNK_duplicate_2 | 175 | Translation: 175.0, Folding: 17.5 | 19,543 | UniprotID: P46859 ECnumber: EC 2.7.1.12 |
||
| b2942 | b2942 | S-adenosylmethionine synthase (AdoMet synthase) (EC 2.5.1.6) (MAT) (Methionine adenosyltransferase) | Cytoplasm | R_METAT_enzyme | R_METAT | 384 | Translation: 384.0, Folding: 38.4 | 41,952 | UniprotID: P0A817 ECnumber: EC 2.5.1.6 |
FUNCTION: Catalyzes the formation of S-adenosylmethionine (AdoMet) from methionine and ATP. The overall synthetic reaction is composed of two sequential steps, AdoMet formation and the subsequent tripolyphosphate hydrolysis which occurs prior to release of AdoMet from the enzyme (PubMed:6251075, PubMed:7629147, PubMed:7629176, PubMed:9753435, PubMed:10551856, PubMed:10660564). Is essential for growth (PubMed:11952912). {ECO:0000269|PubMed:10551856, ECO:0000269|PubMed:10660564, ECO:0000269|PubMed:11952912, ECO:0000269|PubMed:6251075, ECO:0000269|PubMed:7629147, ECO:0000269|PubMed:7629176, ECO:0000269|PubMed:9753435}. |
|
| b2943 | b2943 | Galactose-proton symporter (Galactose transporter) | Cell_inner_membrane | R_GALt2pp_enzyme R_GLCt2pp_enzyme |
R_GALt2pp R_GLCt2pp |
464 | Secretion: 464.0, Translation: 464.0, Folding: 46.4 | 50,983 | UniprotID: P0AEP1 | FUNCTION: Uptake of galactose across the boundary membrane with the concomitant transport of protons into the cell (symport system). | |
| b1855 | b1855 | Lipid A biosynthesis myristoyltransferase (EC 2.3.1.243) (Kdo(2)-lauroyl-lipid IV(A) myristoyltransferase) | Cell_inner_membrane | R_EDTXS2_enzyme R_EDTXS4_enzyme |
R_EDTXS2 R_EDTXS4 |
323 | Secretion: 323.0, Translation: 323.0, Folding: 32.3 | 37,410 | UniprotID: P24205 ECnumber: EC 2.3.1.243 |
FUNCTION: Catalyzes the transfer of myristate from myristoyl-acyl carrier protein (ACP) to Kdo(2)-(lauroyl)-lipid IV(A) to form Kdo(2)-lipid A. Can probably also catalyze the transfer of myristate to Kdo(2)-(palmitoleoyl)-lipid IV(A) to form the cold-adapted Kdo(2)-lipid A. In vitro, can acylate Kdo(2)-lipid IV(A), but acylation of (KDO)2-(lauroyl)-lipid IV(A) is about 100 times faster. In vitro, can use lauroyl-ACP but displays a slight kinetic preference for myristoyl-ACP. {ECO:0000269|PubMed:9099672, ECO:0000305|PubMed:10092655}. |
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| b3893 | b3893 | Formate dehydrogenase-O iron-sulfur subunit (Aerobic formate dehydrogenase iron-sulfur subunit) (FDH-Z subunit beta) (Formate dehydrogenase-O subunit beta) | Cell_inner_membrane | R_FDH4pp_enzyme R_FDH5pp_duplicate_2_enzyme |
R_FDH4pp R_FDH5pp_duplicate_2 |
300 | Secretion: 300.0, Translation: 300.0, Folding: 30.0 | 33,100 | UniprotID: P0AAJ5 | FUNCTION: Allows to use formate as major electron donor during aerobic respiration. The beta chain is an electron transfer unit containing 4 cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit (By similarity). {ECO:0000250}. | |
| b3892 | b3892 | Formate dehydrogenase, cytochrome b556(fdo) subunit (Aerobic formate dehydrogenase cytochrome b556 subunit) (FDH-Z subunit gamma) (Formate dehydrogenase-O subunit gamma) | Cell_inner_membrane | R_FDH4pp_enzyme R_FDH5pp_duplicate_2_enzyme |
R_FDH4pp R_FDH5pp_duplicate_2 |
211 | Secretion: 211.0, Translation: 211.0, Folding: 21.1 | 24,606 | UniprotID: P0AEL0 | FUNCTION: Allows to use formate as major electron donor during aerobic respiration. Subunit gamma is probably the cytochrome b556(FDO) component of the formate dehydrogenase. | |
| b3894 | b3894 | Formate dehydrogenase-O major subunit (EC 1.17.1.9) (Aerobic formate dehydrogenase major subunit) (FDH-Z subunit alpha) (Formate dehydrogenase-O subunit alpha) | Periplasm | R_FDH4pp_enzyme R_FDH5pp_duplicate_2_enzyme |
R_FDH4pp R_FDH5pp_duplicate_2 |
1016 | Secretion: 1015.0, Translation: 1015.0, Folding: 101.5 | 112,549 | UniprotID: P32176 ECnumber: EC 1.17.1.9 |
FUNCTION: Allows to use formate as major electron donor during aerobic respiration. Subunit alpha possibly forms the active site. | |
| b2239 | b2239 | Glycerophosphodiester phosphodiesterase, periplasmic (Glycerophosphoryl diester phosphodiesterase, periplasmic) (EC 3.1.4.46) | Periplasm | R_GPDDA1pp_enzyme R_GPDDA2pp_enzyme R_GPDDA3pp_enzyme R_GPDDA4pp_enzyme R_GPDDA5pp_enzyme |
R_GPDDA1pp R_GPDDA2pp R_GPDDA3pp R_GPDDA4pp R_GPDDA5pp |
358 | Secretion: 358.0, Translation: 358.0, Folding: 35.8 | 40,843 | UniprotID: P09394 ECnumber: EC 3.1.4.46 |
FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols. | |
| b2540 | b2540 | 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin subunit | Cytoplasm | R_CINNDO_enzyme R_PPPNDO_enzyme |
R_CINNDO R_PPPNDO |
106 | Translation: 106.0, Folding: 10.6 | 11,329 | UniprotID: P0ABW0 | FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively. This protein seems to be a 2Fe-2S ferredoxin. | |
| b2541 | b2541 | 3-phenylpropionate-dihydrodiol/cinnamic acid-dihydrodiol dehydrogenase (EC 1.3.1.87) (2,3-dihydroxy-2,3-dihydrophenylpropionate dehydrogenase) (3-(cis-5,6-dihydroxycyclohexa-1,3-dien-1-yl)propanoate dehydrogenase) (CI-dihydrodiol dehydrogenase) (Cis-3-(2-carboxyethenyl)-3,5-cyclohexadiene-1,2-diol dehydrogenase) (Cis-3-(2-carboxyethyl)-3,5-cyclohexadiene-1,2-diol dehydrogenase) (PP-dihydrodiol dehydrogenase) |
Cytoplasm | R_DHCIND_enzyme R_DHPPD_enzyme |
R_DHCIND R_DHPPD |
270 | Translation: 270.0, Folding: 27.0 | 28,500 | UniprotID: P0CI31 ECnumber: EC 1.3.1.87 |
FUNCTION: Converts 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol) into 3-(2,3-dihydroxylphenyl)propanoic acid (DHPP) and 2,3-dihydroxicinnamic acid (DHCI), respectively. {ECO:0000250, ECO:0000269|PubMed:9603882}. | |
| b2542 | b2542 | 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component (EC 1.18.1.3) | Cytoplasm | R_CINNDO_enzyme R_PPPNDO_enzyme |
R_CINNDO R_PPPNDO |
400 | Translation: 400.0, Folding: 40.0 | 43,978 | UniprotID: P77650 ECnumber: EC 1.18.1.3 |
FUNCTION: Part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively. | |
| b2235 | b2235 | Ribonucleoside-diphosphate reductase 1 subunit beta (EC 1.17.4.1) (Protein B2) (Protein R2) (Ribonucleotide reductase 1) | Cytoplasm | 376 | Translation: 376.0, Folding: 37.6 | 43,517 | UniprotID: P69924 ECnumber: EC 1.17.4.1 |
FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2 contains the tyrosyl radical required for catalysis. | |||
| b2232 | b2232 | Ubiquinone biosynthesis O-methyltransferase (2-octaprenyl-6-hydroxyphenol methylase) (EC 2.1.1.222) (3-demethylubiquinone-8 3-O-methyltransferase) (EC 2.1.1.64) | Cytoplasm | R_DMQMT_enzyme R_OHPHM_enzyme |
R_DMQMT R_OHPHM |
240 | Translation: 240.0, Folding: 24.0 | 26,555 | UniprotID: P17993 ECnumber: EC 2.1.1.222; 2.1.1.64 |
FUNCTION: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway. {ECO:0000255|HAMAP-Rule:MF_00472, ECO:0000269|PubMed:10419476}. | |
| b2052 | b2052 | GDP-L-fucose synthase (EC 1.1.1.271) (GDP-4-keto-6-deoxy-D-mannose-3,5-epimerase-4-reductase) | Cytoplasm | R_GDMANE_enzyme R_GOFUCR_enzyme |
R_GDMANE R_GOFUCR |
321 | Translation: 321.0, Folding: 32.1 | 36,141 | UniprotID: P32055 ECnumber: EC 1.1.1.271 |
FUNCTION: Catalyzes the two-step NADP-dependent conversion of GDP-4-dehydro-6-deoxy-D-mannose to GDP-fucose, involving an epimerase and a reductase reaction. {ECO:0000255|HAMAP-Rule:MF_00956, ECO:0000269|PubMed:10480878, ECO:0000269|PubMed:11021971, ECO:0000269|PubMed:9473059}. | |
| b2053 | b2053 | GDP-mannose 4,6-dehydratase (EC 4.2.1.47) (GDP-D-mannose dehydratase) | Cytoplasm | R_GMAND_enzyme | R_GMAND | 373 | Translation: 373.0, Folding: 37.3 | 42,047 | UniprotID: P0AC88 ECnumber: EC 4.2.1.47 |
FUNCTION: Catalyzes the conversion of GDP-D-mannose to GDP-4-dehydro-6-deoxy-D-mannose. {ECO:0000255|HAMAP-Rule:MF_00955, ECO:0000269|PubMed:9257704}. | |
| b2051 | b2051 | GDP-mannose mannosyl hydrolase (GDPMH) (EC 3.6.1.-) (Colanic acid biosynthesis protein WcaH) | Cytoplasm | R_GDPMNH_enzyme | R_GDPMNH | 159 | Translation: 159.0, Folding: 15.9 | 18,273 | UniprotID: P32056 ECnumber: EC 3.6.1.- |
FUNCTION: Hydrolyzes both GDP-mannose and GDP-glucose. Could participate in the regulation of cell wall biosynthesis by influencing the concentration of GDP-mannose or GDP-glucose in the cell. Might also be involved in the biosynthesis of the slime polysaccharide colanic acid. {ECO:0000269|PubMed:10913267, ECO:0000269|PubMed:7592609}. | |
| b3959 | b3959 | Acetylglutamate kinase (EC 2.7.2.8) (N-acetyl-L-glutamate 5-phosphotransferase) (NAG kinase) (NAGK) | Cytoplasm | R_ACGK_enzyme | R_ACGK | 258 | Translation: 258.0, Folding: 25.8 | 27,160 | UniprotID: P0A6C8 ECnumber: EC 2.7.2.8 |
FUNCTION: Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate. {ECO:0000255|HAMAP-Rule:MF_00082, ECO:0000269|PubMed:10393305, ECO:0000269|PubMed:14623187}. | |
| b2435 | b2435 | N-acetylmuramoyl-L-alanine amidase AmiA (EC 3.5.1.28) | Periplasm | R_AGM3PApp_duplicate_2_enzyme R_AGM4PApp_duplicate_2_enzyme |
R_AGM3PApp_duplicate_2 R_AGM4PApp_duplicate_2 |
289 | Secretion: 289.0, Translation: 289.0, Folding: 28.9 | 31,412 | UniprotID: P36548 ECnumber: EC 3.5.1.28 |
FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors. {ECO:0000269|PubMed:11454209, ECO:0000269|PubMed:18390656}. | |
| b2436 | b2436 | Oxygen-dependent coproporphyrinogen-III oxidase (CPO) (Coprogen oxidase) (Coproporphyrinogenase) (EC 1.3.3.3) | Cytoplasm | R_CPPPGO_enzyme | R_CPPPGO | 299 | Translation: 299.0, Folding: 29.9 | 34,323 | UniprotID: P36553 ECnumber: EC 1.3.3.3 |
FUNCTION: Involved in the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX. {ECO:0000255|HAMAP-Rule:MF_00333, ECO:0000269|PubMed:12975365, ECO:0000269|PubMed:13129604}. | |
| b4301 | b4301 | Protein SgcE (EC 5.1.3.-) | Cytoplasm | R_RPE_enzyme | R_RPE | 210 | Translation: 210.0, Folding: 21.0 | 23,214 | UniprotID: P39362 ECnumber: EC 5.1.3.- |
FUNCTION: Probable pentose-5-phosphate 3-epimerase. | |
| b0809 | b0809 | Glutamine transport ATP-binding protein GlnQ | Cell_inner_membrane | R_GLNabcpp_enzyme | R_GLNabcpp | 240 | Secretion: 240.0, Translation: 240.0, Folding: 24.0 | 26,731 | UniprotID: P10346 | FUNCTION: Part of the binding-protein-dependent transport system for glutamine. Probably responsible for energy coupling to the transport system. | |
| b0805 | b0805 | Catecholate siderophore receptor Fiu (Ferric iron uptake protein) (TonB-dependent receptor Fiu) | Cell_outer_membrane | R_FE3DHBZStonex_enzyme | R_FE3DHBZStonex | 760 | Secretion: 760.0, Translation: 760.0, Folding: 76.0 | 81,960 | UniprotID: P75780 | FUNCTION: Involved in the active transport across the outer membrane of iron complexed with catecholate siderophores such as dihydroxybenzoylserine and dihydroxybenzoate. It derives its energy for transport by interacting with the trans-periplasmic membrane protein TonB. Can also transport catechol-substituted cephalosporins. Receptor for microcins M, H47 and E492. {ECO:0000269|PubMed:12949180, ECO:0000269|PubMed:16718603, ECO:0000269|PubMed:2139424, ECO:0000269|PubMed:2407721, ECO:0000269|PubMed:3072926}. |
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| b3624 | b3624 | Lipopolysaccharide core biosynthesis protein RfaZ | Cytoplasm | R_MOAT3C_enzyme | R_MOAT3C | 283 | Translation: 283.0, Folding: 28.3 | 32,920 | UniprotID: P27241 | ||
| b3625 | b3625 | Lipopolysaccharide core heptose(II) kinase RfaY (EC 2.7.1.-) | Cytoplasm | R_HEPK2_enzyme | R_HEPK2 | 232 | Translation: 232.0, Folding: 23.2 | 27,461 | UniprotID: P27240 ECnumber: EC 2.7.1.- |
FUNCTION: Catalyzes the phosphorylation of heptose(II) of the outer membrane lipopolysaccharide core. {ECO:0000250}. | |
| b1319 | b1319 | Outer membrane protein G | Cell_outer_membrane | R_H2Otex_duplicate_7_enzyme | R_H2Otex_duplicate_7 | 301 | Secretion: 301.0, Translation: 301.0, Folding: 30.1 | 34,913 | UniprotID: P76045 | FUNCTION: Forms channels functionally larger than those of classical porins. {ECO:0000269|PubMed:11758943}.; FUNCTION: May act as a regulator of the RCS-phosphorelay signal transduction pathway. {ECO:0000269|PubMed:11758943}. | |
| b2414 | b2414 | Cysteine synthase A (CSase A) (EC 2.5.1.47) (O-acetylserine (thiol)-lyase A) (OAS-TL A) (O-acetylserine sulfhydrylase A) (S-carboxymethylcysteine synthase) (EC 4.5.1.5) (Sulfate starvation-induced protein 5) (SSI5) | Cytoplasm | R_CYSS_enzyme | R_CYSS | 323 | Translation: 323.0, Folding: 32.3 | 34,490 | UniprotID: P0ABK5 ECnumber: EC 2.5.1.47; 4.5.1.5 |
FUNCTION: In addition to its role in cysteine synthesis, stimulates the tRNase activity of CdiA-CT from E.coli strain 536 / UPEC; stimulation does not require O-acetylserine sulfhydrylase activity. CdiA is the toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion (experiments done in strains BW25113 and X90, both K12 derivatives). This protein is not required for CDI of strain EC93, whose toxin may function by forming inner cell membrane pores. {ECO:0000269|PubMed:22333533}. |
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| b1223 | b1223 | Nitrate/nitrite transporter NarK (Nitrite extrusion protein 1) (Nitrite facilitator 1) | Cell_inner_membrane | R_NO2t2rpp_duplicate_2_enzyme R_NO3t7pp_enzyme |
R_NO2t2rpp_duplicate_2 R_NO3t7pp |
463 | Secretion: 463.0, Translation: 463.0, Folding: 46.3 | 49,693 | UniprotID: P10903 | FUNCTION: Catalyzes nitrate uptake, nitrite uptake and nitrite export across the cytoplasmic membrane. Functions as a nitrate/nitrite exchanger, and protons are probably not co-transported with the substrate. {ECO:0000269|PubMed:11967075, ECO:0000269|PubMed:15667293, ECO:0000269|PubMed:16804183, ECO:0000269|PubMed:23665960, ECO:0000269|PubMed:2668029}. | |
| b1224 | b1224 | Respiratory nitrate reductase 1 alpha chain (EC 1.7.99.4) (Nitrate reductase A subunit alpha) (Quinol-nitrate oxidoreductase subunit alpha) | Cell_inner_membrane | R_NO3R1pp_duplicate_2_enzyme R_NO3R2pp_duplicate_2_enzyme |
R_NO3R1pp_duplicate_2 R_NO3R2pp_duplicate_2 |
1247 | Secretion: 1247.0, Translation: 1247.0, Folding: 124.7 | 140,489 | UniprotID: P09152 ECnumber: EC 1.7.99.4 |
FUNCTION: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The alpha chain is the actual site of nitrate reduction. | |
| b1225 | b1225 | Respiratory nitrate reductase 1 beta chain (EC 1.7.99.4) (Nitrate reductase A subunit beta) (Quinol-nitrate oxidoreductase subunit beta) | Cell_inner_membrane | R_NO3R1pp_duplicate_2_enzyme R_NO3R2pp_duplicate_2_enzyme |
R_NO3R1pp_duplicate_2 R_NO3R2pp_duplicate_2 |
512 | Secretion: 512.0, Translation: 512.0, Folding: 51.2 | 58,066 | UniprotID: P11349 ECnumber: EC 1.7.99.4 |
FUNCTION: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The beta chain is an electron transfer unit containing four cysteine clusters involved in the formation of iron-sulfur centers. Electrons are transferred from the gamma chain to the molybdenum cofactor of the alpha subunit. | |
| b1226 | b1226 | Nitrate reductase molybdenum cofactor assembly chaperone NarJ (Redox enzyme maturation protein NarJ) | Cytoplasm | R_NO3R1pp_duplicate_2_enzyme R_NO3R2pp_duplicate_2_enzyme |
R_NO3R1pp_duplicate_2 R_NO3R2pp_duplicate_2 |
236 | Translation: 236.0, Folding: 23.6 | 26,449 | UniprotID: P0AF26 | FUNCTION: Chaperone required for proper molybdenum cofactor insertion and final assembly of the membrane-bound respiratory nitrate reductase 1. Required for the insertion of the molybdenum into the apo-NarG subunit, maybe by keeping NarG in an appropriate competent-open conformation for the molybdenum cofactor insertion to occur. NarJ maintains the apoNarGH complex in a soluble state. Upon insertion of the molybdenum cofactor, NarJ seems to dissociate from the activated soluble NarGH complex, before its association with the NarI subunit on the membrane. {ECO:0000269|PubMed:16286471, ECO:0000269|PubMed:1732220, ECO:0000269|PubMed:9305880, ECO:0000269|PubMed:9632249}. |
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| b1227 | b1227 | Respiratory nitrate reductase 1 gamma chain (EC 1.7.99.4) (Cytochrome B-NR) (Nitrate reductase A subunit gamma) (Quinol-nitrate oxidoreductase subunit gamma) | Cell_inner_membrane | R_NO3R1pp_duplicate_2_enzyme R_NO3R2pp_duplicate_2_enzyme |
R_NO3R1pp_duplicate_2 R_NO3R2pp_duplicate_2 |
225 | Secretion: 225.0, Translation: 225.0, Folding: 22.5 | 25,497 | UniprotID: P11350 ECnumber: EC 1.7.99.4 |
FUNCTION: The nitrate reductase enzyme complex allows E.coli to use nitrate as an electron acceptor during anaerobic growth. The gamma chain is a membrane-embedded heme-iron unit resembling cytochrome b, which transfers electrons from quinones to the beta subunit. | |
| b0573 | b0573 | Cation efflux system protein CusF | Periplasm | R_AGt3_enzyme R_CUt3_enzyme |
R_AGt3 R_CUt3 |
110 | Secretion: 110.0, Translation: 110.0, Folding: 11.0 | 12,251 | UniprotID: P77214 | FUNCTION: Part of a cation efflux system that mediates resistance to copper and silver. Binds one copper per polypeptide (PubMed:11399769, PubMed:24917681). {ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:24917681}. | |
| b0572 | b0572 | Cation efflux system protein CusC | Cell_outer_membrane | R_AGt3_enzyme R_CUt3_enzyme |
R_AGt3 R_CUt3 |
457 | Secretion: 457.0, Translation: 457.0, Folding: 45.7 | 50,270 | UniprotID: P77211 | FUNCTION: Forms pores that allow passive diffusion of cations across the outer membrane. Part of a cation efflux system that mediates resistance to copper and silver. In pathogenic strains it allows the bacteria to invade brain microvascular endothelial cells (BMEC) thus allowing it to cross the blood-brain barrier and cause neonatal meningitis. {ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:12813074, ECO:0000269|PubMed:21249122}. |
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| b4053 | b4053 | Alanine racemase, biosynthetic (EC 5.1.1.1) | Cytoplasm | R_ALAR_duplicate_2_enzyme | R_ALAR_duplicate_2 | 359 | Translation: 359.0, Folding: 35.9 | 39,153 | UniprotID: P0A6B4 ECnumber: EC 5.1.1.1 |
FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. {ECO:0000269|PubMed:18434499}. | |
| b4054 | b4054 | Aromatic-amino-acid aminotransferase (ARAT) (AROAT) (EC 2.6.1.57) (Beta-methylphenylalanine transaminase) (EC 2.6.1.107) | Cytoplasm | R_LEUTAi_duplicate_2_enzyme R_PHETA1_duplicate_2_enzyme R_TYRTA_enzyme |
R_LEUTAi_duplicate_2 R_PHETA1_duplicate_2 R_TYRTA |
397 | Translation: 397.0, Folding: 39.7 | 43,538 | UniprotID: P04693 ECnumber: EC 2.6.1.57; 2.6.1.107 |
FUNCTION: Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085. {ECO:0000269|PubMed:19731276}. |
|
| b4055 | b4055 | Class B acid phosphatase (CBAP) (EC 3.1.3.2) | Periplasm | R_G2PPpp_enzyme R_NTD10pp_duplicate_2_enzyme R_NTD11pp_duplicate_2_enzyme R_NTD12pp_duplicate_2_enzyme R_NTD1pp_duplicate_2_enzyme R_NTD2pp_duplicate_2_enzyme R_NTD3pp_duplicate_2_enzyme R_NTD4pp_duplicate_2_enzyme R_NTD5pp_duplicate_2_enzyme R_NTD6pp_duplicate_2_enzyme R_NTD7pp_duplicate_2_enzyme R_NTD8pp_duplicate_2_enzyme R_NTD9pp_duplicate_2_enzyme R_PSP_Lpp_enzyme R_PTHRpp_enzyme R_R5PPpp_enzyme R_TYRPpp_enzyme |
237 | Secretion: 237.0, Translation: 237.0, Folding: 23.7 | 26,104 | UniprotID: P0AE22 ECnumber: EC 3.1.3.2 |
FUNCTION: Dephosphorylates several organic phosphate monoesters including 3- and 5-nucleotides, 2-deoxy-5-nucleotides, pNPP, phenyl phosphate, glycerol 2-phosphate, ribose 5-phosphate, O-phospho-L-amino acids and phytic acid, showing the highest activity with aryl phosphoesters (pNPP, phenyl phosphate and O-phospho-L-tyrosine), and to a lesser extent with 3- and 5-nucleotides. No activity toward ATP, phosphodiesters, glycerol-1-phosphate, glucose 1-phosphate, glucose 6-phosphate, NADP, GTP or 3,5-cAMP, ADP or ATP. Also has a phosphotransferase activity catalyzing the transfer of low-energy phosphate groups from organic phosphate monoesters to free hydroxyl groups of various organic compounds. Capable of transferring phosphate from either pNPP or UMP to adenosine or uridine. Does not exhibit nucleotide phosphomutase activity. {ECO:0000269|PubMed:16297670, ECO:0000269|PubMed:9011040}. |
||
| b0575 | b0575 | Cation efflux system protein CusA | Cell_inner_membrane | R_AGt3_enzyme R_CUt3_enzyme |
R_AGt3 R_CUt3 |
1047 | Secretion: 1047.0, Translation: 1047.0, Folding: 104.7 | 114,707 | UniprotID: P38054 | FUNCTION: Part of a cation efflux system that mediates resistance to copper and silver. {ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:12813074}. | |
| b0574 | b0574 | Cation efflux system protein CusB | Cytoplasm | R_AGt3_enzyme R_CUt3_enzyme |
R_AGt3 R_CUt3 |
407 | Translation: 407.0, Folding: 40.7 | 44,305 | UniprotID: P77239 | FUNCTION: Part of a cation efflux system that mediates resistance to copper and silver. {ECO:0000269|PubMed:11399769, ECO:0000269|PubMed:12813074}. | |
| b0578 | b0578 | Oxygen-insensitive NAD(P)H nitroreductase (EC 1.-.-.-) (Dihydropteridine reductase) (EC 1.5.1.34) (FMN-dependent nitroreductase) | Cytoplasm | R_DHPTDNR_enzyme R_DHPTDNRN_enzyme |
R_DHPTDNR R_DHPTDNRN |
217 | Translation: 217.0, Folding: 21.7 | 23,905 | UniprotID: P38489 ECnumber: EC 1.-.-.-; 1.5.1.34 |
FUNCTION: Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species. {ECO:0000269|PubMed:15684426}. | |
| b0974 | b0974 | Probable Ni/Fe-hydrogenase 1 B-type cytochrome subunit | Cell_inner_membrane | R_HYD1pp_duplicate_2_enzyme R_HYD2pp_enzyme R_HYD3pp_enzyme |
R_HYD1pp_duplicate_2 R_HYD2pp R_HYD3pp |
235 | Secretion: 235.0, Translation: 235.0, Folding: 23.5 | 27,597 | UniprotID: P0AAM1 | FUNCTION: Probable b-type cytochrome. | |
| b0973 | b0973 | Hydrogenase-1 large chain (HYD1) (EC 1.12.99.6) (Membrane-bound hydrogenase 1 large subunit) (NiFe hydrogenase) | Cell_inner_membrane | R_HYD1pp_duplicate_2_enzyme R_HYD2pp_enzyme R_HYD3pp_enzyme |
R_HYD1pp_duplicate_2 R_HYD2pp R_HYD3pp |
597 | Secretion: 597.0, Translation: 597.0, Folding: 59.7 | 66,253 | UniprotID: P0ACD8 ECnumber: EC 1.12.99.6 |
FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth. | |
| b0972 | b0972 | Hydrogenase-1 small chain (HYD1) (EC 1.12.99.6) (Membrane-bound hydrogenase 1 small subunit) (NiFe hydrogenase) | Cell_inner_membrane | R_HYD1pp_duplicate_2_enzyme R_HYD2pp_enzyme R_HYD3pp_enzyme |
R_HYD1pp_duplicate_2 R_HYD2pp R_HYD3pp |
372 | Secretion: 372.0, Translation: 372.0, Folding: 37.2 | 40,681 | UniprotID: P69739 ECnumber: EC 1.12.99.6 |
FUNCTION: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD1 is believed to have a role in hydrogen cycling during fermentative growth. | |
| b0979 | b0979 | Cytochrome bd-II ubiquinol oxidase subunit 2 (EC 1.10.3.10) (Cytochrome bd-II oxidase subunit II) | Cell_inner_membrane | R_CYTBD2pp_enzyme R_CYTBDpp_enzyme |
R_CYTBD2pp R_CYTBDpp |
378 | Secretion: 378.0, Translation: 378.0, Folding: 37.8 | 42,424 | UniprotID: P26458 ECnumber: EC 1.10.3.10 |
FUNCTION: A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested (PubMed:8626304). Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791, ECO:0000269|PubMed:22843529, ECO:0000269|PubMed:8626304}. |
|
| b0978 | b0978 | Cytochrome bd-II ubiquinol oxidase subunit 1 (EC 1.10.3.10) (Cytochrome bd-II oxidase subunit I) | Cell_inner_membrane | R_CYTBD2pp_enzyme R_CYTBDpp_enzyme |
R_CYTBD2pp R_CYTBDpp |
514 | Secretion: 514.0, Translation: 514.0, Folding: 51.4 | 57,920 | UniprotID: P26459 ECnumber: EC 1.10.3.10 |
FUNCTION: A terminal oxidase that catalyzes quinol-dependent, Na(+)-independent oxygen uptake. Prefers menadiol over other quinols although ubiquinol was not tested (PubMed:8626304). Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791, ECO:0000269|PubMed:22843529, ECO:0000269|PubMed:8626304}. |
|
| b0151 | b0151 | Iron(3+)-hydroxamate import ATP-binding protein FhuC (EC 3.6.3.34) (Ferric hydroxamate uptake protein C) (Ferrichrome transport ATP-binding protein FhuC) (Iron(III)-hydroxamate import ATP-binding protein FhuC) | Cell_inner_membrane | R_ARBTNabcpp_enzyme R_CPGNabcpp_enzyme R_FE3HOXabcpp_enzyme R_FECRMabcpp_enzyme R_FEOXAMabcpp_enzyme |
R_ARBTNabcpp R_CPGNabcpp R_FE3HOXabcpp R_FECRMabcpp R_FEOXAMabcpp |
265 | Secretion: 265.0, Translation: 265.0, Folding: 26.5 | 28,886 | UniprotID: P07821 ECnumber: EC 3.6.3.34 |
FUNCTION: Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for energy coupling to the transport system. {ECO:0000269|PubMed:1551849}. | |
| b0150 | b0150 | Ferrichrome-iron receptor (Ferric hydroxamate receptor) (Ferric hydroxamate uptake) | Cell_outer_membrane | R_FE3HOXtonex_enzyme R_FECRMtonex_enzyme R_FEOXAMtonex_enzyme |
R_FE3HOXtonex R_FECRMtonex R_FEOXAMtonex |
747 | Secretion: 747.0, Translation: 747.0, Folding: 74.7 | 82,182 | UniprotID: P06971 | FUNCTION: This receptor binds the ferrichrome-iron ligand. It interacts with the TonB protein, which is responsible for energy coupling of the ferrichrome-promoted iron transport system. Acts as a receptor for bacteriophage T5 as well as T1, phi80 and colicin M. Binding of T5 triggers the opening of a high conductance ion channel. Can also transport the antibiotic albomycin. {ECO:0000269|PubMed:8617231}. |
|
| b0153 | b0153 | Iron(3+)-hydroxamate import system permease protein FhuB (Ferric hydroxamate uptake protein B) (Ferrichrome transport system permease protein FhuB) (Ferrichrome uptake protein FhuB) (Iron(III)-hydroxamate import system permease protein FhuB) | Cell_inner_membrane | R_ARBTNabcpp_enzyme R_CPGNabcpp_enzyme R_FE3HOXabcpp_enzyme R_FECRMabcpp_enzyme R_FEOXAMabcpp_enzyme |
R_ARBTNabcpp R_CPGNabcpp R_FE3HOXabcpp R_FECRMabcpp R_FEOXAMabcpp |
660 | Secretion: 660.0, Translation: 660.0, Folding: 66.0 | 70,423 | UniprotID: P06972 | FUNCTION: Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:1551849, ECO:0000269|PubMed:3020380}. | |
| b0152 | b0152 | Iron(3+)-hydroxamate-binding protein FhuD (Ferric hydroxamate uptake protein D) (Ferrichrome-binding periplasmic protein) (Iron(III)-hydroxamate-binding protein FhuD) | Periplasm | R_ARBTNabcpp_enzyme R_CPGNabcpp_enzyme R_FE3HOXabcpp_enzyme R_FECRMabcpp_enzyme R_FEOXAMabcpp_enzyme |
R_ARBTNabcpp R_CPGNabcpp R_FE3HOXabcpp R_FECRMabcpp R_FEOXAMabcpp |
296 | Secretion: 296.0, Translation: 296.0, Folding: 29.6 | 32,998 | UniprotID: P07822 | FUNCTION: Part of the ABC transporter complex FhuCDB involved in iron(3+)-hydroxamate import. Binds the iron(3+)-hydroxamate complex and transfers it to the membrane-bound permease. Required for the transport of all iron(3+)-hydroxamate siderophores such as ferrichrome, gallichrome, desferrioxamine, coprogen, aerobactin, shizokinen, rhodotorulic acid and the antibiotic albomycin. {ECO:0000269|PubMed:10742172, ECO:0000269|PubMed:11805094, ECO:0000269|PubMed:2254301, ECO:0000269|PubMed:8522527}. |
|
| b0155 | b0155 | H(+)/Cl(-) exchange transporter ClcA (ClC-ec1) | Cell_inner_membrane | R_CLt3_2pp_enzyme | R_CLt3_2pp | 473 | Secretion: 473.0, Translation: 473.0, Folding: 47.3 | 50,349 | UniprotID: P37019 | FUNCTION: Proton-coupled chloride transporter. Functions as antiport system and exchanges two chloride ions for 1 proton. Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response. {ECO:0000269|PubMed:12384697, ECO:0000269|PubMed:14985752, ECO:0000269|PubMed:16341087, ECO:0000269|PubMed:16905147, ECO:0000269|PubMed:18678918}. |
|
| b0154 | b0154 | Glutamate-1-semialdehyde 2,1-aminomutase (GSA) (EC 5.4.3.8) (Glutamate-1-semialdehyde aminotransferase) (GSA-AT) | Cytoplasm | R_G1SAT_enzyme | R_G1SAT | 426 | Translation: 426.0, Folding: 42.6 | 45,366 | UniprotID: P23893 ECnumber: EC 5.4.3.8 |
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| b0159 | b0159 | 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase (MTA/SAH nucleosidase) (MTAN) (EC 3.2.2.9) (5-methylthioadenosine nucleosidase) (MTA nucleosidase) (P46) (S-adenosylhomocysteine nucleosidase) (AdoHcy nucleosidase) (SAH nucleosidase) (SRH nucleosidase) | Cytoplasm | R_5DOAN_enzyme R_AHCYSNS_enzyme R_MTAN_enzyme |
R_5DOAN R_AHCYSNS R_MTAN |
232 | Translation: 232.0, Folding: 23.2 | 24,354 | UniprotID: P0AF12 ECnumber: EC 3.2.2.9 |
FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in both 5-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5-methylthioribose and S-ribosylhomocysteine, respectively. Can also use 5-isobutylthioadenosine, 5-n-butylthioadenosine, S-adenosyl-D-homocysteine, decarboxylated adenosylhomocysteine, deaminated adenosylhomocysteine and S-2-aza-adenosylhomocysteine as substrates. {ECO:0000269|PubMed:16101288}. |
|
| b0158 | b0158 | Vitamin B12-binding protein | Periplasm | R_ADOCBLabcpp_enzyme R_CBIuabcpp_enzyme R_CBL1abcpp_enzyme |
R_ADOCBLabcpp R_CBIuabcpp R_CBL1abcpp |
266 | Secretion: 266.0, Translation: 266.0, Folding: 26.6 | 29,367 | UniprotID: P37028 | FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC. {ECO:0000255|HAMAP-Rule:MF_01000, ECO:0000269|PubMed:11790740}. | |
| b4024 | b4024 | Lysine-sensitive aspartokinase 3 (EC 2.7.2.4) (Aspartate kinase III) (AKIII) (Lysine-sensitive aspartokinase III) | Cytoplasm | R_ASPK_duplicate_3_enzyme | R_ASPK_duplicate_3 | 449 | Translation: 449.0, Folding: 44.9 | 48,532 | UniprotID: P08660 ECnumber: EC 2.7.2.4 |
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| b0207 | b0207 | 2,5-diketo-D-gluconic acid reductase B (2,5-DKG reductase B) (2,5-DKGR B) (25DKGR-B) (EC 1.1.1.346) (AKR5D) | Cytoplasm | R_ALR2_duplicate_3_enzyme R_DKGLCNR1_enzyme |
R_ALR2_duplicate_3 R_DKGLCNR1 |
267 | Translation: 267.0, Folding: 26.7 | 29,437 | UniprotID: P30863 ECnumber: EC 1.1.1.346 |
FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). | |
| b0200 | b0200 | D-glycero-beta-D-manno-heptose-1,7-bisphosphate 7-phosphatase (EC 3.1.3.82) (D,D-heptose 1,7-bisphosphate phosphatase) (HBP phosphatase) | Cytoplasm | R_GMHEPPA_enzyme | R_GMHEPPA | 191 | Translation: 191.0, Folding: 19.1 | 21,294 | UniprotID: P63228 ECnumber: EC 3.1.3.82 |
FUNCTION: Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate (beta-HBP) intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position. {ECO:0000269|PubMed:11751812, ECO:0000269|PubMed:16990279, ECO:0000269|PubMed:20050615}. | |
| b3089 | b3089 | Serine/threonine transporter SstT (Na(+)/serine-threonine symporter) | Cell_inner_membrane | R_SERt4pp_enzyme R_THRt4pp_enzyme |
R_SERt4pp R_THRt4pp |
414 | Secretion: 414.0, Translation: 414.0, Folding: 41.4 | 43,478 | UniprotID: P0AGE4 | FUNCTION: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system). {ECO:0000269|PubMed:12097162, ECO:0000269|PubMed:9852024}. | |
| b3551 | b3551 | Biotin sulfoxide reductase (BDS reductase) (BSO reductase) (EC 1.-.-.-) (L-methionine-(S)-sulfoxide reductase) (Met-S-SO reductase) (EC 1.8.4.13) | Cytoplasm | R_BSORx_enzyme R_BSORy_enzyme R_METSOXR1_enzyme R_METSOXR1_duplicate_4_enzyme |
R_BSORx R_BSORy R_METSOXR1 R_METSOXR1_duplicate_4 |
777 | Translation: 777.0, Folding: 77.7 | 85,851 | UniprotID: P20099 ECnumber: EC 1.-.-.-; 1.8.4.13 |
FUNCTION: This enzyme may serve as a scavenger, allowing the cell to utilize biotin sulfoxide as a biotin source. It reduces a spontaneous oxidation product of biotin, D-biotin D-sulfoxide (BSO or BDS), back to biotin. Also exhibits methionine-(S)-sulfoxide (Met-S-SO) reductase activity, acting specifically on the (S) enantiomer in the free, but not the protein-bound form. It thus plays a role in assimilation of oxidized methionines. {ECO:0000269|PubMed:15601707, ECO:0000269|PubMed:2180922}. |
|
| b3553 | b3553 | Glyoxylate/hydroxypyruvate reductase B (EC 1.1.1.79) (EC 1.1.1.81) (2-ketoaldonate reductase) (2-ketogluconate reductase) (2KR) (EC 1.1.1.215) | Cytoplasm | 324 | Translation: 324.0, Folding: 32.4 | 35,396 | UniprotID: P37666 ECnumber: EC 1.1.1.79; 1.1.1.81; 1.1.1.215 |
FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Can also reduce 2,5-diketo-D-gluconate (25DKG) to 5-keto-D-gluconate (5KDG), 2-keto-D-gluconate (2KDG) to D-gluconate, and 2-keto-L-gulonate (2KLG) to L-idonate (IA), but it is not its physiological function. Inactive towards 2-oxoglutarate, oxaloacetate, pyruvate, 5-keto-D-gluconate, D-fructose and L-sorbose. Activity with NAD is very low. |
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| b3559 | b3559 | Glycine--tRNA ligase beta subunit (EC 6.1.1.14) (Glycyl-tRNA synthetase beta subunit) (GlyRS) | Cytoplasm | R_GLYTRS_enzyme | R_GLYTRS | 689 | Translation: 689.0, Folding: 68.9 | 76,813 | UniprotID: P00961 ECnumber: EC 6.1.1.14 |
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| b2687 | b2687 | S-ribosylhomocysteine lyase (EC 4.4.1.21) (AI-2 synthesis protein) (Autoinducer-2 production protein LuxS) | Cytoplasm | R_RHCCE_enzyme | R_RHCCE | 171 | Translation: 171.0, Folding: 17.1 | 19,416 | UniprotID: P45578 ECnumber: EC 4.4.1.21 |
FUNCTION: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD). {ECO:0000269|PubMed:9618536, ECO:0000269|PubMed:9990077}. |
|
| b2930 | b2930 | Fructose-1,6-bisphosphatase 2 class 2 (FBPase 2 class 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2 class 2) | Cytoplasm | R_FBP_duplicate_3_enzyme | R_FBP_duplicate_3 | 321 | Translation: 321.0, Folding: 32.1 | 34,323 | UniprotID: P21437 ECnumber: EC 3.1.3.11 |
FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Also displays a low activity toward glucose 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate, fructose 2,6-bisphosphate, or fructose 1-phosphate. {ECO:0000269|PubMed:19073594}. | |
| b2935 | b2935 | Transketolase 1 (TK 1) (EC 2.2.1.1) | Cytoplasm | R_TKT1_enzyme R_TKT2_enzyme |
R_TKT1 R_TKT2 |
663 | Translation: 663.0, Folding: 66.3 | 72,212 | UniprotID: P27302 ECnumber: EC 2.2.1.1 |
FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. {ECO:0000269|PubMed:17914867, ECO:0000269|PubMed:7607225}. |
|
| b2682 | b2682 | Inner membrane protein YgaZ | Cell_inner_membrane | R_VALt2rpp_duplicate_2_enzyme | R_VALt2rpp_duplicate_2 | 245 | Secretion: 245.0, Translation: 245.0, Folding: 24.5 | 26,108 | UniprotID: P76630 | ||
| b2937 | b2937 | Agmatinase (EC 3.5.3.11) (Agmatine ureohydrolase) (AUH) | Cytoplasm | R_AGMT_enzyme | R_AGMT | 306 | Translation: 306.0, Folding: 30.6 | 33,557 | UniprotID: P60651 ECnumber: EC 3.5.3.11 |
FUNCTION: Catalyzes the formation of putrescine from agmatine. {ECO:0000269|PubMed:10527864}. | |
| b2913 | b2913 | D-3-phosphoglycerate dehydrogenase (PGDH) (EC 1.1.1.95) (2-oxoglutarate reductase) (EC 1.1.1.399) | Cytoplasm | R_PGCD_enzyme | R_PGCD | 410 | Translation: 410.0, Folding: 41.0 | 44,176 | UniprotID: P0A9T0 ECnumber: EC 1.1.1.95; 1.1.1.399 |
FUNCTION: Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate. {ECO:0000269|PubMed:8550422}. | |
| b3426 | b3426 | Aerobic glycerol-3-phosphate dehydrogenase (EC 1.1.5.3) | Cytoplasm | R_G3PD5_duplicate_2_enzyme | R_G3PD5_duplicate_2 | 501 | Translation: 501.0, Folding: 50.1 | 56,751 | UniprotID: P13035 ECnumber: EC 1.1.5.3 |
FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor. | |
| b2688 | b2688 | Glutamate--cysteine ligase (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase) | Cytoplasm | R_GLUCYS_enzyme | R_GLUCYS | 518 | Translation: 518.0, Folding: 51.8 | 58,269 | UniprotID: P0A6W9 ECnumber: EC 6.3.2.2 |
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| b3882 | b3882 | 3-sulfolactaldehyde reductase (SLA reductase) (EC 1.1.1.373) | Cytoplasm | R_GHBDHx_enzyme | R_GHBDHx | 298 | Translation: 298.0, Folding: 29.8 | 31,158 | UniprotID: P0A9V8 ECnumber: EC 1.1.1.373 |
FUNCTION: Reduces 3-sulfolactaldehyde (SLA) to 2,3-dihydroxypropane 1-sulfonate (DHPS). {ECO:0000255|HAMAP-Rule:MF_01913, ECO:0000269|PubMed:24463506}. | |
| b2203 | b2203 | Periplasmic nitrate reductase, electron transfer subunit (Diheme cytochrome c NapB) | Periplasm | R_NO3R1bpp_enzyme R_NO3R2bpp_enzyme |
R_NO3R1bpp R_NO3R2bpp |
149 | Secretion: 149.0, Translation: 149.0, Folding: 14.9 | 16,297 | UniprotID: P0ABL3 | FUNCTION: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor. {ECO:0000269|PubMed:10234835, ECO:0000269|PubMed:10548535, ECO:0000269|PubMed:17130127}. |
|
| b2202 | b2202 | Cytochrome c-type protein NapC | Cell_inner_membrane | R_NO3R1bpp_enzyme R_NO3R2bpp_enzyme |
R_NO3R1bpp R_NO3R2bpp |
200 | Secretion: 200.0, Translation: 200.0, Folding: 20.0 | 23,101 | UniprotID: P0ABL5 | FUNCTION: Mediates electron flow from quinones to the NapAB complex. | |
| b2201 | b2201 | Cytochrome c biogenesis ATP-binding export protein CcmA (EC 3.6.3.41) (Heme exporter protein A) | Cell_inner_membrane | R_PHEMEabcpp_enzyme | R_PHEMEabcpp | 207 | Secretion: 207.0, Translation: 207.0, Folding: 20.7 | 23,053 | UniprotID: P33931 ECnumber: EC 3.6.3.41 |
FUNCTION: Part of the ABC transporter complex CcmAB involved in the biogenesis of c-type cytochromes; once thought to export heme, this seems not to be the case, but its exact role is uncertain. Responsible for energy coupling to the transport system. | |
| b2200 | b2200 | Heme exporter protein B (Cytochrome c-type biogenesis protein CcmB) | Cell_inner_membrane | R_PHEMEabcpp_enzyme | R_PHEMEabcpp | 220 | Secretion: 220.0, Translation: 220.0, Folding: 22.0 | 23,619 | UniprotID: P0ABL8 | FUNCTION: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes. | |
| b2206 | b2206 | Periplasmic nitrate reductase (EC 1.9.6.1) | Periplasm | R_NO3R1bpp_enzyme R_NO3R2bpp_enzyme |
R_NO3R1bpp R_NO3R2bpp |
828 | Secretion: 828.0, Translation: 828.0, Folding: 82.8 | 93,042 | UniprotID: P33937 ECnumber: EC 1.9.6.1 |
FUNCTION: Catalytic subunit of the periplasmic nitrate reductase (NAP). Only expressed at high levels during aerobic growth. NapAB complex receives electrons from the membrane-anchored tetraheme protein NapC, thus allowing electron flow between membrane and periplasm. Essential function for nitrate assimilation and may have a role in anaerobic metabolism. {ECO:0000250}. | |
| b2205 | b2205 | Ferredoxin-type protein NapG | Cytoplasm | R_NO3R1bpp_enzyme | R_NO3R1bpp | 231 | Translation: 231.0, Folding: 23.1 | 24,925 | UniprotID: P0AAL3 | FUNCTION: Involved in electron transfer. {ECO:0000305}. | |
| b2204 | b2204 | Ferredoxin-type protein NapH | Cell_inner_membrane | R_NO3R1bpp_enzyme | R_NO3R1bpp | 287 | Secretion: 287.0, Translation: 287.0, Folding: 28.7 | 31,874 | UniprotID: P33934 | FUNCTION: Involved in electron transfer. | |
| b2066 | b2066 | Uridine kinase (EC 2.7.1.48) (Cytidine monophosphokinase) (Uridine monophosphokinase) | Cytoplasm | R_CYTDK2_enzyme R_URIK2_enzyme |
R_CYTDK2 R_URIK2 |
213 | Translation: 213.0, Folding: 21.3 | 24,353 | UniprotID: P0A8F4 ECnumber: EC 2.7.1.48 |
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| b2065 | b2065 | dCTP deaminase (EC 3.5.4.13) (Deoxycytidine triphosphate deaminase) | Cytoplasm | R_DCTPD_enzyme | R_DCTPD | 193 | Translation: 193.0, Folding: 19.3 | 21,249 | UniprotID: P28248 ECnumber: EC 3.5.4.13 |
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| b2599 | b2599 | P-protein [Includes: Chorismate mutase (CM) (EC 5.4.99.5); Prephenate dehydratase (PDT) (EC 4.2.1.51) | Cytoplasm | R_CHORM_enzyme R_PPNDH_enzyme |
R_CHORM R_PPNDH |
386 | Translation: 386.0, Folding: 38.6 | 43,111 | UniprotID: P0A9J8 ECnumber: EC 5.4.99.5; 4.2.1.51 |
FUNCTION: Catalyzes the Claisen rearrangement of chorismate to prephenate and the decarboxylation/dehydration of prephenate to phenylpyruvate. {ECO:0000269|PubMed:4261395}. | |
| b2841 | b2841 | Arabinose-proton symporter (Arabinose transporter) | Cell_inner_membrane | R_ARBt2rpp_enzyme | R_ARBt2rpp | 472 | Secretion: 472.0, Translation: 472.0, Folding: 47.2 | 51,684 | UniprotID: P0AE24 | FUNCTION: Uptake of arabinose across the boundary membrane with the concomitant transport of protons into the cell (symport system). | |
| b2441 | b2441 | Ethanolamine ammonia-lyase heavy chain (EC 4.3.1.7) (Ethanolamine ammonia-lyase large subunit) | Cytoplasm | R_ETHAAL_enzyme | R_ETHAAL | 453 | Translation: 453.0, Folding: 45.3 | 49,403 | UniprotID: P0AEJ6 ECnumber: EC 4.3.1.7 |
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| b2440 | b2440 | Ethanolamine ammonia-lyase light chain (EC 4.3.1.7) (Ethanolamine ammonia-lyase small subunit) | Cytoplasm | R_ETHAAL_enzyme | R_ETHAAL | 295 | Translation: 295.0, Folding: 29.5 | 31,782 | UniprotID: P19636 ECnumber: EC 4.3.1.7 |
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| b2114 | b2114 | Methionine--tRNA ligase (EC 6.1.1.10) (Methionyl-tRNA synthetase) (MetRS) | Cytoplasm | R_METTRS_enzyme | R_METTRS | 677 | Translation: 677.0, Folding: 67.7 | 76,255 | UniprotID: P00959 ECnumber: EC 6.1.1.10 |
FUNCTION: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation. | |
| b1106 | b1106 | Thiamine kinase (EC 2.7.1.89) | Cytoplasm | R_TMK_enzyme | R_TMK | 274 | Translation: 274.0, Folding: 27.4 | 32,397 | UniprotID: P75948 ECnumber: EC 2.7.1.89 |
FUNCTION: Catalyzes the phosphorylation of thiamine to thiamine phosphate. | |
| b1817 | b1817 | PTS system mannose-specific EIIAB component (EC 2.7.1.191) (EIIAB-Man) (EIII-Man) [Includes: Mannose-specific phosphotransferase enzyme IIA component (PTS system mannose-specific EIIA component); Mannose-specific phosphotransferase enzyme IIB component (PTS system mannose-specific EIIB component) | Cytoplasm | R_ACMANAptspp_enzyme R_FRUpts2pp_enzyme R_GAMptspp_enzyme R_GLCptspp_duplicate_3_enzyme R_MANptspp_enzyme |
R_ACMANAptspp R_FRUpts2pp R_GAMptspp R_GLCptspp_duplicate_3 R_MANptspp |
323 | Translation: 323.0, Folding: 32.3 | 35,048 | UniprotID: P69797 ECnumber: EC 2.7.1.191 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:2951378, PubMed:2999119, PubMed:2681202, PubMed:8262947). The enzyme II ManXYZ PTS system is involved in mannose transport (PubMed:2951378, PubMed:2999119, PubMed:2681202, PubMed:8262947). Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA (PubMed:4604906, PubMed:353494). {ECO:0000269|PubMed:2681202, ECO:0000269|PubMed:2951378, ECO:0000269|PubMed:2999119, ECO:0000269|PubMed:353494, ECO:0000269|PubMed:4604906, ECO:0000269|PubMed:8262947}. |
|
| b1814 | b1814 | L-serine dehydratase 1 (SDH 1) (EC 4.3.1.17) (L-serine deaminase 1) (L-SD1) | Cytoplasm | R_SERD_L_duplicate_3_enzyme | R_SERD_L_duplicate_3 | 454 | Translation: 454.0, Folding: 45.4 | 48,907 | UniprotID: P16095 ECnumber: EC 4.3.1.17 |
FUNCTION: Deaminates also threonine, particularly when it is present in high concentration. | |
| b1812 | b1812 | Aminodeoxychorismate synthase component 1 (ADC synthase) (ADCS) (EC 2.6.1.85) (4-amino-4-deoxychorismate synthase component 1) | Cytoplasm | R_ADCS_enzyme R_GLUN_duplicate_2_enzyme |
R_ADCS R_GLUN_duplicate_2 |
453 | Translation: 453.0, Folding: 45.3 | 50,970 | UniprotID: P05041 ECnumber: EC 2.6.1.85 |
FUNCTION: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabB, in the absence of PabA, can catalyze the formation of ADC in the presence of exogenous ammonia. {ECO:0000269|PubMed:16605270, ECO:0000269|PubMed:2251281, ECO:0000269|PubMed:4914080}. |
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| b0810 | b0810 | Glutamine transport system permease protein GlnP | Cell_inner_membrane | R_GLNabcpp_enzyme | R_GLNabcpp | 219 | Secretion: 219.0, Translation: 219.0, Folding: 21.9 | 24,364 | UniprotID: P0AEQ6 | FUNCTION: Part of the binding-protein-dependent transport system for glutamine; probably responsible for the translocation of the substrate across the membrane. | |
| b0811 | b0811 | Glutamine-binding periplasmic protein (GlnBP) | Periplasm | R_GLNabcpp_enzyme | R_GLNabcpp | 248 | Secretion: 248.0, Translation: 248.0, Folding: 24.8 | 27,190 | UniprotID: P0AEQ3 | FUNCTION: Involved in a glutamine-transport system GlnHPQ. {ECO:0000269|PubMed:3027504}. | |
| b0813 | b0813 | Threonine/homoserine exporter RhtA | Cell_inner_membrane | R_HOMt2pp_enzyme R_THRt2pp_enzyme |
R_HOMt2pp R_THRt2pp |
295 | Secretion: 295.0, Translation: 295.0, Folding: 29.5 | 31,168 | UniprotID: P0AA67 | FUNCTION: Involved in the efflux of threonine and homoserine. Can also export other amino acids such as proline, serine, histidine and cysteine. {ECO:0000269|PubMed:12648727}. | |
| b1819 | b1819 | PTS system mannose-specific EIID component (EII-M-Man) (EIID-Man) (Mannose permease IID component) | Cell_inner_membrane | R_ACMANAptspp_enzyme R_FRUpts2pp_enzyme R_GAMptspp_enzyme R_GLCptspp_duplicate_3_enzyme R_MANptspp_enzyme |
R_ACMANAptspp R_FRUpts2pp R_GAMptspp R_GLCptspp_duplicate_3 R_MANptspp |
283 | Secretion: 283.0, Translation: 283.0, Folding: 28.3 | 30,955 | UniprotID: P69805 | FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:2951378, PubMed:2999119). The enzyme II ManXYZ PTS system is involved in mannose transport (PubMed:2951378, PubMed:2999119). Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA (PubMed:4604906, PubMed:353494). {ECO:0000269|PubMed:2951378, ECO:0000269|PubMed:2999119, ECO:0000269|PubMed:353494, ECO:0000269|PubMed:4604906}. |
|
| b1818 | b1818 | PTS system mannose-specific EIIC component (EII-P-Man) (EIIC-Man) (Mannose permease IIC component) | Cell_inner_membrane | R_ACMANAptspp_enzyme R_FRUpts2pp_enzyme R_GAMptspp_enzyme R_GLCptspp_duplicate_3_enzyme R_MANptspp_enzyme |
R_ACMANAptspp R_FRUpts2pp R_GAMptspp R_GLCptspp_duplicate_3 R_MANptspp |
266 | Secretion: 266.0, Translation: 266.0, Folding: 26.6 | 27,636 | UniprotID: P69801 | FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:2951378, PubMed:2999119). The enzyme II ManXYZ PTS system is involved in mannose transport (PubMed:2951378, PubMed:2999119). Also functions as a receptor for bacterial chemotaxis and is required for infection of the cell by bacteriophage lambda where it most likely functions as a pore for penetration of lambda DNA (PubMed:4604906, PubMed:353494). {ECO:0000269|PubMed:2951378, ECO:0000269|PubMed:2999119, ECO:0000269|PubMed:353494, ECO:0000269|PubMed:4604906}. |
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| b1033 | b1033 | Glyoxylate/hydroxypyruvate reductase A (EC 1.1.1.79) (EC 1.1.1.81) (2-ketoacid reductase) | Cytoplasm | R_GLYCLTDx_duplicate_2_enzyme R_GLYCLTDy_enzyme R_HPYRRx_enzyme R_HPYRRy_enzyme |
R_GLYCLTDx_duplicate_2 R_GLYCLTDy R_HPYRRx R_HPYRRy |
312 | Translation: 312.0, Folding: 31.2 | 35,343 | UniprotID: P75913 ECnumber: EC 1.1.1.79; 1.1.1.81 |
FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low. | |
| b0781 | b0781 | GTP 3,8-cyclase (EC 4.1.99.22) (Molybdenum cofactor biosynthesis protein A) | Cytoplasm | R_CPMPS_enzyme | R_CPMPS | 329 | Translation: 329.0, Folding: 32.9 | 37,346 | UniprotID: P30745 ECnumber: EC 4.1.99.22 |
FUNCTION: Catalyzes, together with MoaC, the conversion of 5-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).; FUNCTION: Catalyzes the cyclization of GTP to (8S)-3,8-cyclo-7,8-dihydroguanosine 5-triphosphate. {ECO:0000255|HAMAP-Rule:MF_01225}. | |
| b0783 | b0783 | Cyclic pyranopterin monophosphate synthase (EC 4.6.1.17) (Molybdenum cofactor biosynthesis protein C) | Cytoplasm | R_CPMPS_enzyme | R_CPMPS | 161 | Translation: 161.0, Folding: 16.1 | 17,467 | UniprotID: P0A738 ECnumber: EC 4.6.1.17 |
FUNCTION: Catalyzes the conversion of (8S)-3,8-cyclo-7,8-dihydroguanosine 5-triphosphate to cyclic pyranopterin monophosphate (cPMP). {ECO:0000255|HAMAP-Rule:MF_01224, ECO:0000269|PubMed:25941396}. | |
| b0784 | b0784 | Molybdopterin synthase sulfur carrier subunit (MPT synthase subunit 1) (Molybdenum cofactor biosynthesis protein D) (Molybdopterin-converting factor small subunit) (Molybdopterin-converting factor subunit 1) (Sulfur carrier protein MoaD) | Cytoplasm | R_MOADSUx_enzyme R_MPTS_enzyme |
R_MOADSUx R_MPTS |
81 | Translation: 81.0, Folding: 8.1 | 8,758 | UniprotID: P30748 | FUNCTION: Involved in sulfur transfer in the conversion of molybdopterin precursor Z to molybdopterin. {ECO:0000269|PubMed:17223713}. | |
| b0785 | b0785 | Molybdopterin synthase catalytic subunit (EC 2.8.1.12) (MPT synthase subunit 2) (Molybdenum cofactor biosynthesis protein E) (Molybdopterin-converting factor large subunit) (Molybdopterin-converting factor subunit 2) | Cytoplasm | R_MPTS_enzyme | R_MPTS | 150 | Translation: 150.0, Folding: 15.0 | 16,981 | UniprotID: P30749 ECnumber: EC 2.8.1.12 |
FUNCTION: Converts molybdopterin precursor Z to molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD. | |
| b4209 | b4209 | Iron-sulfur cluster repair protein YtfE (Regulator of cell morphogenesis and NO signaling) (RCMNS) | Cytoplasm | R_FESR_enzyme | R_FESR | 220 | Translation: 220.0, Folding: 22.0 | 24,883 | UniprotID: P69506 | FUNCTION: Di-iron-containing protein involved in the repair of iron-sulfur clusters damaged by oxidative and nitrosative stress conditions. {ECO:0000269|PubMed:16553864, ECO:0000269|PubMed:17289666, ECO:0000269|PubMed:18357473}. | |
| b4208 | b4208 | D-serine/D-alanine/glycine transporter | Cell_inner_membrane | R_ALAt2pp_copy1_enzyme R_BALAt2pp_enzyme R_DALAt2pp_enzyme R_DSERt2pp_enzyme R_GLYt2pp_copy1_enzyme |
R_ALAt2pp_copy1 R_BALAt2pp R_DALAt2pp R_DSERt2pp R_GLYt2pp_copy1 |
470 | Secretion: 470.0, Translation: 470.0, Folding: 47.0 | 51,660 | UniprotID: P0AAE0 | FUNCTION: Permease that is involved in the transport across the cytoplasmic membrane of D-alanine, D-serine and glycine. | |
| b1363 | b1363 | Trk system potassium uptake protein TrkG | Cell_inner_membrane | R_Kt2pp_enzyme | R_Kt2pp | 485 | Secretion: 485.0, Translation: 485.0, Folding: 48.5 | 53,944 | UniprotID: P23849 | FUNCTION: Low-affinity potassium transport system. Interacts with Trk system potassium uptake protein TrkA. Requires TrkE (sapD) for maximal transport activity, low activity is seen in its absence; no further stimulation is seen with SapF (PubMed:11700350). Transport in the absence of SapD is dependent on a high membrane potential and a high cytoplasmic ATP concentration, suggesting this protein may be able to interact with other ATP-binding proteins (PubMed:11700350). Can transport potassium and rubidium (PubMed:7896723). {ECO:0000269|PubMed:11700350, ECO:0000269|PubMed:2022616, ECO:0000269|PubMed:2674131, ECO:0000269|PubMed:7896723}. |
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| b1781 | b1781 | Uncharacterized protein YeaE | Cytoplasm | R_ALR2_enzyme | R_ALR2 | 284 | Translation: 284.0, Folding: 28.4 | 30,987 | UniprotID: P76234 | ||
| b3744 | b3744 | Aspartate--ammonia ligase (EC 6.3.1.1) (Asparagine synthetase A) | Cytoplasm | R_ASNS2_enzyme | R_ASNS2 | 330 | Translation: 330.0, Folding: 33.0 | 36,651 | UniprotID: P00963 ECnumber: EC 6.3.1.1 |
FUNCTION: May amidate Asp of the extracellular death factor precursor Asn-Asn-Trp-Asp-Asn to generate Asn-Asn-Trp-Asn-Asn. {ECO:0000305|PubMed:17962566}. | |
| b1764 | b1764 | Selenide, water dikinase (EC 2.7.9.3) (Selenium donor protein) (Selenophosphate synthase) | Cytoplasm | R_SELNPS_enzyme | R_SELNPS | 347 | Translation: 347.0, Folding: 34.7 | 36,687 | UniprotID: P16456 ECnumber: EC 2.7.9.3 |
FUNCTION: Synthesizes selenophosphate from selenide and ATP. | |
| b1767 | b1767 | L-asparaginase 1 (EC 3.5.1.1) (L-asparaginase I) (L-ASNase I) (L-asparagine amidohydrolase I) | Cytoplasm | R_ASNN_enzyme | R_ASNN | 338 | Translation: 338.0, Folding: 33.8 | 37,127 | UniprotID: P0A962 ECnumber: EC 3.5.1.1 |
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| b1761 | b1761 | NADP-specific glutamate dehydrogenase (NADP-GDH) (EC 1.4.1.4) | Cytoplasm | R_GLUDy_enzyme | R_GLUDy | 447 | Translation: 447.0, Folding: 44.7 | 48,581 | UniprotID: P00370 ECnumber: EC 1.4.1.4 |
FUNCTION: Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia. {ECO:0000269|PubMed:235298, ECO:0000269|PubMed:241744}. | |
| b1768 | b1768 | Nicotinamidase (EC 3.5.1.19) (Nicotinamide deamidase) (NAMase) (Pyrazinamidase) (PZAase) (EC 3.5.1.-) | Cytoplasm | R_NNAM_enzyme | R_NNAM | 213 | Translation: 213.0, Folding: 21.3 | 23,362 | UniprotID: P21369 ECnumber: EC 3.5.1.19; 3.5.1.- |
FUNCTION: Catalyzes the deamidation of nicotinamide (NAM) into nicotinate (PubMed:4399474, PubMed:8726014). Likely functions in the cyclical salvage pathway for production of NAD from nicotinamide (PubMed:4399474). {ECO:0000269|PubMed:4399474, ECO:0000305|PubMed:8726014}.; FUNCTION: Is also able to hydrolyze the first-line antituberculous drug pyrazinamide (PZA) into pyrazinoic acid in vitro, but this reaction is not considered to be physiologically relevant. {ECO:0000305|PubMed:8726014}. |
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| b4513 | b4513 | Potassium-transporting ATPase KdpF subunit (ATP phosphohydrolase [potassium-transporting] F chain) (Potassium-binding and translocating subunit F) (Potassium-translocating ATPase F chain) | Cell_inner_membrane | R_Kabcpp_duplicate_2_enzyme | R_Kabcpp_duplicate_2 | 29 | Secretion: 29.0, Translation: 29.0, Folding: 2.9 | 3,072 | UniprotID: P36937 | FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:23930894). This subunit may be involved in stabilization of the complex (PubMed:10608856). {ECO:0000269|PubMed:10608856, ECO:0000269|PubMed:23930894}. | |
| b0963 | b0963 | Methylglyoxal synthase (MGS) (EC 4.2.3.3) | Cytoplasm | R_MGSA_enzyme | R_MGSA | 152 | Translation: 152.0, Folding: 15.2 | 16,919 | UniprotID: P0A731 ECnumber: EC 4.2.3.3 |
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| b0968 | b0968 | Acylphosphatase (EC 3.6.1.7) (Acylphosphate phosphohydrolase) | Cytoplasm | R_APH120 R_APH140 R_APH141 R_APH160 R_APH161 R_APH180 R_APH181 |
92 | Translation: 92.0, Folding: 9.2 | 10,300 | UniprotID: P0AB65 ECnumber: EC 3.6.1.7 |
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| b0142 | b0142 | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC 2.7.6.3) (6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase) (PPPK) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (HPPK) | Cytoplasm | R_HPPK2_enzyme | R_HPPK2 | 159 | Translation: 159.0, Folding: 15.9 | 18,079 | UniprotID: P26281 ECnumber: EC 2.7.6.3 |
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| b4193 | b4193 | Ascorbate-specific PTS system EIIC component (Ascorbate-specific permease IIC component UlaA) | Cell_inner_membrane | R_ASCBptspp_enzyme | R_ASCBptspp | 465 | Secretion: 465.0, Translation: 465.0, Folding: 46.5 | 50,737 | UniprotID: P39301 | FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. {ECO:0000269|PubMed:12644495, ECO:0000305|PubMed:11741871}. | |
| b4192 | b4192 | Probable L-ascorbate-6-phosphate lactonase UlaG (EC 3.1.1.-) (L-ascorbate utilization protein G) | Cytoplasm | R_ASCBPL_enzyme | R_ASCBPL | 354 | Translation: 354.0, Folding: 35.4 | 40,061 | UniprotID: P39300 ECnumber: EC 3.1.1.- |
FUNCTION: Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions. Also shows phosphodiesterase activity, hydrolyzing phosphodiester bond in the artificial chromogenic substrate bis-p-nitrophenyl phosphate (bis-pNPP). {ECO:0000269|PubMed:12644495, ECO:0000269|PubMed:15808744}. | |
| b4195 | b4195 | Ascorbate-specific PTS system EIIA component (EC 2.7.1.194) (Ascorbate-specific phosphotransferase enzyme IIA component) | Cytoplasm | R_ASCBptspp_enzyme | R_ASCBptspp | 154 | Translation: 154.0, Folding: 15.4 | 17,238 | UniprotID: P69820 ECnumber: EC 2.7.1.194 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. {ECO:0000269|PubMed:12644495, ECO:0000305|PubMed:11741871}. | |
| b4194 | b4194 | Ascorbate-specific PTS system EIIB component (EC 2.7.1.194) (Ascorbate-specific phosphotransferase enzyme IIB component) | Cytoplasm | R_ASCBptspp_enzyme | R_ASCBptspp | 101 | Translation: 101.0, Folding: 10.1 | 10,896 | UniprotID: P69822 ECnumber: EC 2.7.1.194 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate transport. {ECO:0000269|PubMed:12644495, ECO:0000305|PubMed:11741871}. | |
| b4197 | b4197 | L-ribulose-5-phosphate 3-epimerase UlaE (EC 5.1.3.22) (L-ascorbate utilization protein E) (L-xylulose-5-phosphate 3-epimerase) | Cytoplasm | R_X5PL3E_enzyme | R_X5PL3E | 284 | Translation: 284.0, Folding: 28.4 | 32,007 | UniprotID: P39305 ECnumber: EC 5.1.3.22 |
FUNCTION: Catalyzes the isomerization of L-xylulose-5-phosphate to L-ribulose-5-phosphate. Is involved in the anaerobic L-ascorbate utilization. {ECO:0000255|HAMAP-Rule:MF_01951, ECO:0000269|PubMed:11741871}. | |
| b4196 | b4196 | 3-keto-L-gulonate-6-phosphate decarboxylase UlaD (EC 4.1.1.85) (3-dehydro-L-gulonate-6-phosphate decarboxylase) (KGPDC) (L-ascorbate utilization protein D) | Cytoplasm | R_KG6PDC_enzyme | R_KG6PDC | 216 | Translation: 216.0, Folding: 21.6 | 23,578 | UniprotID: P39304 ECnumber: EC 4.1.1.85 |
FUNCTION: Catalyzes the decarboxylation of 3-keto-L-gulonate-6-P into L-xylulose-5-P. Is involved in the anaerobic L-ascorbate utilization. {ECO:0000269|PubMed:11741871}. | |
| b4198 | b4198 | L-ribulose-5-phosphate 4-epimerase UlaF (EC 5.1.3.4) (L-ascorbate utilization protein F) (Phosphoribulose isomerase) | Cytoplasm | R_RBP4E_duplicate_2_enzyme | R_RBP4E_duplicate_2 | 228 | Translation: 228.0, Folding: 22.8 | 25,278 | UniprotID: P39306 ECnumber: EC 5.1.3.4 |
FUNCTION: Catalyzes the isomerization of L-ribulose 5-phosphate to D-xylulose 5-phosphate. Is involved in the anaerobic L-ascorbate utilization. {ECO:0000255|HAMAP-Rule:MF_01952, ECO:0000269|PubMed:11741871}. | |
| b0149 | b0149 | Penicillin-binding protein 1B (PBP-1b) (PBP1b) (Murein polymerase) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase) (Peptidoglycan glycosyltransferase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase) | Cell_inner_membrane | R_MCTP1App_enzyme R_MCTP1Bpp_enzyme R_MCTP2App_duplicate_4_enzyme R_MPTG_enzyme R_MPTG2_enzyme |
R_MCTP1App R_MCTP1Bpp R_MCTP2App_duplicate_4 R_MPTG R_MPTG2 |
844 | Secretion: 844.0, Translation: 844.0, Folding: 84.4 | 94,293 | UniprotID: P02919 ECnumber: EC 2.4.1.129; 3.4.16.4 |
FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). | |
| b4258 | b4258 | Valine--tRNA ligase (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) | Cytoplasm | R_VALTRS_enzyme | R_VALTRS | 951 | Translation: 951.0, Folding: 95.1 | 108,192 | UniprotID: P07118 ECnumber: EC 6.1.1.9 |
FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner. | |
| b0368 | b0368 | Alpha-ketoglutarate-dependent taurine dioxygenase (EC 1.14.11.17) (2-aminoethanesulfonate dioxygenase) (Sulfate starvation-induced protein 3) (SSI3) | Cytoplasm | R_TAUDO_enzyme | R_TAUDO | 283 | Translation: 283.0, Folding: 28.3 | 32,410 | UniprotID: P37610 ECnumber: EC 1.14.11.17 |
FUNCTION: Catalyzes the conversion of taurine and alpha ketoglutarate to sulfite, aminoacetaldehyde and succinate. Required for the utilization of taurine (2-aminoethanesulfonic acid) as an alternative sulfur source. Pentane-sulfonic acid, 3-(N-morpholino)propanesulfonic acid and 1,3-dioxo-2-isoindolineethanesulfonic acid are also substrates for this enzyme. | |
| b0369 | b0369 | Delta-aminolevulinic acid dehydratase (ALAD) (ALADH) (EC 4.2.1.24) (Porphobilinogen synthase) | Cytoplasm | R_PPBNGS_enzyme | R_PPBNGS | 324 | Translation: 324.0, Folding: 32.4 | 35,625 | UniprotID: P0ACB2 ECnumber: EC 4.2.1.24 |
FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. | |
| b0366 | b0366 | Taurine import ATP-binding protein TauB (EC 3.6.3.36) | Cell_inner_membrane | R_BUTSO3abcpp_duplicate_2_enzyme R_ISETACabcpp_enzyme R_TAURabcpp_enzyme |
R_BUTSO3abcpp_duplicate_2 R_ISETACabcpp R_TAURabcpp |
255 | Secretion: 255.0, Translation: 255.0, Folding: 25.5 | 28,297 | UniprotID: Q47538 ECnumber: EC 3.6.3.36 |
FUNCTION: Part of the ABC transporter complex TauABC involved in taurine import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01714, ECO:0000269|PubMed:10781534, ECO:0000269|PubMed:8808933}. | |
| b0367 | b0367 | Taurine transport system permease protein TauC | Cell_inner_membrane | R_BUTSO3abcpp_duplicate_2_enzyme R_ISETACabcpp_enzyme R_TAURabcpp_enzyme |
R_BUTSO3abcpp_duplicate_2 R_ISETACabcpp R_TAURabcpp |
275 | Secretion: 275.0, Translation: 275.0, Folding: 27.5 | 29,812 | UniprotID: Q47539 | FUNCTION: Part of a binding-protein-dependent transport system for taurine. Probably responsible for the translocation of the substrate across the membrane. | |
| b0365 | b0365 | Taurine-binding periplasmic protein (Sulfate starvation-induced protein 1) (SSI1) | Periplasm | R_BUTSO3abcpp_duplicate_2_enzyme R_ISETACabcpp_enzyme R_TAURabcpp_enzyme |
R_BUTSO3abcpp_duplicate_2 R_ISETACabcpp R_TAURabcpp |
320 | Secretion: 320.0, Translation: 320.0, Folding: 32.0 | 34,266 | UniprotID: Q47537 | FUNCTION: Part of a binding-protein-dependent transport system for taurine. | |
| b0212 | b0212 | Hydroxyacylglutathione hydrolase GloB (EC 3.1.2.6) (Glyoxalase II) (Glx II) | Cytoplasm | R_GLYOX_enzyme | R_GLYOX | 251 | Translation: 251.0, Folding: 25.1 | 28,434 | UniprotID: P0AC84 ECnumber: EC 3.1.2.6 |
FUNCTION: Type II glyoxalase that catalyzes the hydrolysis of (R)-S-lactoylglutathione to (R)-lactate and glutathione (PubMed:25670698, PubMed:17196158). Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli (PubMed:25670698). The two isoenzymes have additive effects and ensure maximal MG degradation (PubMed:25670698). {ECO:0000269|PubMed:17196158, ECO:0000269|PubMed:25670698}. |
|
| b2868 | b2868 | Putative xanthine dehydrogenase iron-sulfur-binding subunit XdhC | Cytoplasm | R_HXAND_enzyme R_XAND_enzyme |
R_HXAND R_XAND |
159 | Translation: 159.0, Folding: 15.9 | 16,922 | UniprotID: Q46801 | FUNCTION: Iron-sulfur subunit of the xanthine dehydrogenase complex. | |
| b3849 | b3849 | Trk system potassium uptake protein TrkH | Cell_inner_membrane | R_Kt2pp_duplicate_2_enzyme | R_Kt2pp_duplicate_2 | 483 | Secretion: 483.0, Translation: 483.0, Folding: 48.3 | 52,960 | UniprotID: P0AFZ7 | FUNCTION: Low-affinity potassium transport system. Interacts with Trk system potassium uptake protein TrkA. Requires TrkE (sapD) for transport activity, 20% more uptake is seen with both SapD and SapF (PubMed:11700350). Transport in the absence of SapD and SapF is dependent on a high membrane potential and a high cytoplasmic ATP concentration, suggesting this protein may be able to interact with other ATP-binding proteins (PubMed:11700350). Can transport potassium and rubidium (PubMed:7896723). {ECO:0000250, ECO:0000269|PubMed:11700350, ECO:0000269|PubMed:7896723}. |
|
| b3182 | b3182 | D-alanyl-D-alanine carboxypeptidase DacB (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (D-alanyl-D-alanine endopeptidase) (DD-endopeptidase) (EC 3.4.21.-) (Penicillin-binding protein 4) (PBP-4) | Periplasm | 477 | Secretion: 477.0, Translation: 477.0, Folding: 47.7 | 51,798 | UniprotID: P24228 ECnumber: EC 3.4.16.4; 3.4.21.- |
FUNCTION: Not involved in transpeptidation but exclusively catalyzes a DD-carboxypeptidase and DD-endopeptidase reaction. {ECO:0000269|PubMed:2046551}. | |||
| b3187 | b3187 | Octaprenyl diphosphate synthase (EC 2.5.1.90) (All-trans-octaprenyl-diphosphate synthase) (Octaprenyl pyrophosphate synthase) (OPP synthase) | Cytoplasm | R_OCTDPS_enzyme | R_OCTDPS | 323 | Translation: 323.0, Folding: 32.3 | 35,217 | UniprotID: P0AD57 ECnumber: EC 2.5.1.90 |
FUNCTION: Supplies octaprenyl diphosphate, the precursor for the side chain of the isoprenoid quinones ubiquinone and menaquinone. {ECO:0000269|PubMed:8037730}. | |
| b3634 | b3634 | Phosphopantetheine adenylyltransferase (EC 2.7.7.3) (Dephospho-CoA pyrophosphorylase) (Pantetheine-phosphate adenylyltransferase) (PPAT) | Cytoplasm | R_PTPATi_enzyme | R_PTPATi | 159 | Translation: 159.0, Folding: 15.9 | 17,837 | UniprotID: P0A6I6 ECnumber: EC 2.7.7.3 |
FUNCTION: Reversibly transfers an adenylyl group from ATP to 4-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate (PubMed:10480925, PubMed:17873050). CoA is not a substrate for the enzyme (PubMed:10480925). {ECO:0000255|HAMAP-Rule:MF_00151, ECO:0000269|PubMed:10480925, ECO:0000269|PubMed:17873050}. | |
| b3189 | b3189 | UDP-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) (Enoylpyruvate transferase) (UDP-N-acetylglucosamine enolpyruvyl transferase) (EPT) | Cytoplasm | R_UAGCVT_enzyme | R_UAGCVT | 419 | Translation: 419.0, Folding: 41.9 | 44,818 | UniprotID: P0A749 ECnumber: EC 2.5.1.7 |
FUNCTION: Cell wall formation (PubMed:1512209). Adds enolpyruvyl to UDP-N-acetylglucosamine (PubMed:1512209, PubMed:20392080). Target for the antibiotic fosfomycin. {ECO:0000269|PubMed:1512209, ECO:0000269|PubMed:20392080}. | |
| b3631 | b3631 | Lipopolysaccharide core biosynthesis protein RfaG (EC 2.4.-.-) (Glucosyltransferase I) | Cytoplasm | R_GLCTR1_enzyme | R_GLCTR1 | 374 | Translation: 374.0, Folding: 37.4 | 42,284 | UniprotID: P25740 ECnumber: EC 2.4.-.- |
FUNCTION: Involved in the addition of the first glucose residue to the lipopolysaccharide core. | |
| b3630 | b3630 | Lipopolysaccharide core heptose(I) kinase RfaP (EC 2.7.1.-) | Cytoplasm | R_HEPK1_enzyme | R_HEPK1 | 265 | Translation: 265.0, Folding: 26.5 | 30,872 | UniprotID: P25741 ECnumber: EC 2.7.1.- |
FUNCTION: Catalyzes the phosphorylation of heptose(I) of the outer membrane lipopolysaccharide core. {ECO:0000250}. | |
| b3633 | b3633 | 3-deoxy-D-manno-octulosonic acid transferase (Kdo transferase) (EC 2.4.99.12) (EC 2.4.99.13) (Bifunctional Kdo transferase) (Kdo-lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) (Lipid IV(A) 3-deoxy-D-manno-octulosonic acid transferase) | Cell_inner_membrane | R_MOAT_enzyme R_MOAT2_enzyme |
R_MOAT R_MOAT2 |
425 | Secretion: 425.0, Translation: 425.0, Folding: 42.5 | 47,291 | UniprotID: P0AC75 ECnumber: EC 2.4.99.12; 2.4.99.13 |
FUNCTION: Involved in lipopolysaccharide (LPS) biosynthesis. Catalyzes the transfer of two 3-deoxy-D-manno-octulosonate (Kdo) residues from CMP-Kdo to lipid IV(A), the tetraacyldisaccharide-1,4-bisphosphate precursor of lipid A. {ECO:0000269|PubMed:10951204, ECO:0000269|PubMed:1577828}. | |
| b3632 | b3632 | Lipopolysaccharide core heptosyltransferase RfaQ (EC 2.-.-.-) | Cytoplasm | R_HEPT3_enzyme | R_HEPT3 | 344 | Translation: 344.0, Folding: 34.4 | 38,731 | UniprotID: P25742 ECnumber: EC 2.-.-.- |
FUNCTION: Catalyzes heptose transfer to the lipopolysaccharide core. It transfers a heptose, called heptose(III), to the heptose(II) of the inner core (By similarity). {ECO:0000250}. | |
| b2328 | b2328 | Penicillin-insensitive murein endopeptidase (EC 3.4.24.-) (D-alanyl-D-alanine-endopeptidase) (DD-endopeptidase) | Periplasm | R_MDDEP1pp_enzyme R_MDDEP2pp_enzyme R_MDDEP3pp_enzyme R_MDDEP4pp_enzyme |
R_MDDEP1pp R_MDDEP2pp R_MDDEP3pp R_MDDEP4pp |
274 | Secretion: 274.0, Translation: 274.0, Folding: 27.4 | 30,137 | UniprotID: P0C0T5 ECnumber: EC 3.4.24.- |
FUNCTION: Murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus. {ECO:0000269|PubMed:15292190}. | |
| b2329 | b2329 | Chorismate synthase (CS) (EC 4.2.3.5) (5-enolpyruvylshikimate-3-phosphate phospholyase) (EPSP phospholyase) | Cytoplasm | R_CHORS_enzyme | R_CHORS | 361 | Translation: 361.0, Folding: 36.1 | 39,137 | UniprotID: P12008 ECnumber: EC 4.2.3.5 |
FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system. It uses NADPH to reduce FMN. {ECO:0000255|HAMAP-Rule:MF_00300, ECO:0000269|PubMed:10956653, ECO:0000269|PubMed:11034781, ECO:0000269|PubMed:2969724, ECO:0000269|PubMed:7848266, ECO:0000269|PubMed:7978236, ECO:0000269|PubMed:8703965}. |
|
| b2320 | b2320 | Erythronate-4-phosphate dehydrogenase (EC 1.1.1.290) | Cytoplasm | R_PERD_enzyme | R_PERD | 378 | Translation: 378.0, Folding: 37.8 | 41,368 | UniprotID: P05459 ECnumber: EC 1.1.1.290 |
FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-hydroxy-2-oxo-4-phosphonooxybutanoate. {ECO:0000255|HAMAP-Rule:MF_01825}. | |
| b2323 | b2323 | 3-oxoacyl-[acyl-carrier-protein] synthase 1 (EC 2.3.1.41) (3-oxoacyl-[acyl-carrier-protein] synthase I) (Beta-ketoacyl-ACP synthase I) (KAS I) | Cytoplasm | 406 | Translation: 406.0, Folding: 40.6 | 42,613 | UniprotID: P0A953 ECnumber: EC 2.3.1.41 |
FUNCTION: Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-10 to unsaturated C-16 and C-18 fatty acids. {ECO:0000269|PubMed:3076377}. | |||
| b3526 | b3526 | 2-dehydro-3-deoxygluconokinase (EC 2.7.1.45) (2-keto-3-deoxygluconokinase) (3-deoxy-2-oxo-D-gluconate kinase) (KDG kinase) | Cytoplasm | R_DDGLK_enzyme | R_DDGLK | 309 | Translation: 309.0, Folding: 30.9 | 33,962 | UniprotID: P37647 ECnumber: EC 2.7.1.45 |
FUNCTION: Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). {ECO:0000269|PubMed:4944816}. | |
| b3528 | b3528 | Aerobic C4-dicarboxylate transport protein | Cell_inner_membrane | R_ASPt2_2pp R_FUMt2_2pp R_MALDt2_2pp R_MALt2_2pp R_OROTt2_2pp R_SUCCt2_2pp |
428 | Secretion: 428.0, Translation: 428.0, Folding: 42.8 | 45,436 | UniprotID: P0A830 | FUNCTION: Responsible for the aerobic transport of the dicarboxylates fumarate, L- and D-malate and to a lesser extent succinate, from the periplasm across the inner membrane. {ECO:0000269|PubMed:17088549}. | ||
| b2690 | b2690 | Fructose-1-phosphate phosphatase YqaB (EC 3.1.3.-) (Fructose-1-phosphatase) | Cytoplasm | R_PGMT_enzyme | R_PGMT | 188 | Translation: 188.0, Folding: 18.8 | 20,780 | UniprotID: P77475 ECnumber: EC 3.1.3.- |
FUNCTION: Catalyzes strongly the dephosphorylation of fructose-1-phosphate (Fru1P) and slightly the dephosphorylation of 6-phosphogluconate (6P-Glu). It has low beta-phosphoglucomutase activity. {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16990279}. | |
| b2923 | b2923 | Arginine exporter protein ArgO | Cell_inner_membrane | R_ARGt3pp_enzyme R_LYSt3pp_enzyme |
R_ARGt3pp R_LYSt3pp |
211 | Secretion: 211.0, Translation: 211.0, Folding: 21.1 | 23,176 | UniprotID: P11667 | FUNCTION: Involved in the export of arginine. Important to control the intracellular level of arginine and the correct balance between arginine and lysine. May also be involved in the export of canavanine (a plant-derived antimetabolite). {ECO:0000269|PubMed:15150242}. | |
| b2920 | b2920 | Propionyl-CoA:succinate CoA transferase (EC 2.8.3.-) | Cytoplasm | R_PPCSCT_enzyme | R_PPCSCT | 492 | Translation: 492.0, Folding: 49.2 | 53,824 | UniprotID: P52043 ECnumber: EC 2.8.3.- |
FUNCTION: Catalyzes the transfer of coenzyme A from propionyl-CoA to succinate. Could be part of a pathway that converts succinate to propionate. {ECO:0000269|PubMed:10769117}. | |
| b2926 | b2926 | Phosphoglycerate kinase (EC 2.7.2.3) | Cytoplasm | R_PGK_enzyme | R_PGK | 387 | Translation: 387.0, Folding: 38.7 | 41,118 | UniprotID: P0A799 ECnumber: EC 2.7.2.3 |
||
| b2927 | b2927 | D-erythrose-4-phosphate dehydrogenase (E4PDH) (EC 1.2.1.72) | Cytoplasm | R_E4PD_enzyme | R_E4PD | 339 | Translation: 339.0, Folding: 33.9 | 37,299 | UniprotID: P0A9B6 ECnumber: EC 1.2.1.72 |
FUNCTION: Catalyzes the NAD-dependent conversion of D-erythrose 4-phosphate to 4-phosphoerythronate. {ECO:0000269|PubMed:9182530, ECO:0000269|PubMed:9696782}. | |
| b2697 | b2697 | Alanine--tRNA ligase (EC 6.1.1.7) (Alanyl-tRNA synthetase) (AlaRS) | Cytoplasm | R_ALATRS_enzyme | R_ALATRS | 876 | Translation: 876.0, Folding: 87.6 | 96,032 | UniprotID: P00957 ECnumber: EC 6.1.1.7 |
FUNCTION: Catalyzes the attachment of L-alanine to tRNA(Ala) in a two-step reaction: L-alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller amino acid glycine as well as the sterically larger amino acid L-serine; generates 2-fold more mischarged Gly than Ser (PubMed:28362257). These mischarged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Ala, Gly and Ser) in the charging step. {ECO:0000269|PubMed:28362257}.; FUNCTION: Edits mischarged Ser-tRNA(Ala) and Gly-tRNA(Ala) but not incorrectly charged Ser-tRNA(Thr) (PubMed:12554667, PubMed:18723508). Dtd edits Gly-tRNA(Ala) 4-fold better than does AlaRS (PubMed:28362257). {ECO:0000269|PubMed:12554667, ECO:0000269|PubMed:18723508, ECO:0000269|PubMed:28362257}.; FUNCTION: Attaches Ala to transfer-messenger RNA (tmRNA, also known as 10Sa RNA, the product of the ssrA gene). tmRNA plays a major role in rescue of stalled ribosomes via trans-translation. {ECO:0000269|PubMed:7524073}. |
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| b3451 | b3451 | sn-glycerol-3-phosphate transport system permease protein UgpE | Cell_inner_membrane | R_G3PCabcpp R_G3PEabcpp R_G3PGabcpp R_G3PIabcpp R_G3PSabcpp R_GLYC2Pabcpp R_GLYC3Pabcpp |
281 | Secretion: 281.0, Translation: 281.0, Folding: 28.1 | 31,500 | UniprotID: P10906 | FUNCTION: Part of the binding-protein-dependent transport system for sn-glycerol-3-phosphate; probably responsible for the translocation of the substrate across the membrane. | ||
| b3450 | b3450 | sn-glycerol-3-phosphate import ATP-binding protein UgpC (EC 3.6.3.20) | Cell_inner_membrane | R_G3PCabcpp R_G3PEabcpp R_G3PGabcpp R_G3PIabcpp R_G3PSabcpp R_GLYC2Pabcpp R_GLYC3Pabcpp |
356 | Secretion: 356.0, Translation: 356.0, Folding: 35.6 | 39,524 | UniprotID: P10907 ECnumber: EC 3.6.3.20 |
FUNCTION: Part of the ABC transporter complex UgpABCE involved in sn-glycerol-3-phosphate import. Responsible for energy coupling to the transport system (Probable). Can also transport glycerophosphoryl diesters. {ECO:0000255|HAMAP-Rule:MF_01727, ECO:0000269|PubMed:2842304, ECO:0000269|PubMed:363686, ECO:0000269|PubMed:7042685, ECO:0000269|PubMed:8282692, ECO:0000269|PubMed:8407831, ECO:0000305}. |
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| b3453 | b3453 | sn-glycerol-3-phosphate-binding periplasmic protein UgpB | Periplasm | R_G3PCabcpp R_G3PEabcpp R_G3PGabcpp R_G3PIabcpp R_G3PSabcpp R_GLYC2Pabcpp R_GLYC3Pabcpp |
438 | Secretion: 438.0, Translation: 438.0, Folding: 43.8 | 48,449 | UniprotID: P0AG80 | FUNCTION: sn-glycerol-3-phosphate and glycerophosphoryl diester-binding protein interacts with the binding protein-dependent transport system UgpACE. | ||
| b3452 | b3452 | sn-glycerol-3-phosphate transport system permease protein UgpA | Cell_inner_membrane | R_G3PCabcpp R_G3PEabcpp R_G3PGabcpp R_G3PIabcpp R_G3PSabcpp R_GLYC2Pabcpp R_GLYC3Pabcpp |
295 | Secretion: 295.0, Translation: 295.0, Folding: 29.5 | 33,264 | UniprotID: P10905 | FUNCTION: Part of the binding-protein-dependent transport system for sn-glycerol-3-phosphate; probably responsible for the translocation of the substrate across the membrane. | ||
| b3455 | b3455 | High-affinity branched-chain amino acid transport ATP-binding protein LivG (LIV-I protein G) | Cytoplasm | R_ALAabcpp R_ILEabcpp R_LEUabcpp R_LEUabcpp_duplicate_2 R_THRabcpp R_VALabcpp |
255 | Translation: 255.0, Folding: 25.5 | 28,427 | UniprotID: P0A9S7 | FUNCTION: Component of the leucine-specific transport system. | ||
| b3454 | b3454 | High-affinity branched-chain amino acid transport ATP-binding protein LivF (LIV-I protein F) | Cytoplasm | R_ALAabcpp R_ILEabcpp R_LEUabcpp R_LEUabcpp_duplicate_2 R_THRabcpp R_VALabcpp |
237 | Translation: 237.0, Folding: 23.7 | 26,310 | UniprotID: P22731 | FUNCTION: Component of the leucine-specific transport system. | ||
| b3457 | b3457 | High-affinity branched-chain amino acid transport system permease protein LivH (LIV-I protein H) | Cell_inner_membrane | R_ALAabcpp R_ILEabcpp R_LEUabcpp R_LEUabcpp_duplicate_2 R_THRabcpp R_VALabcpp |
308 | Secretion: 308.0, Translation: 308.0, Folding: 30.8 | 32,982 | UniprotID: P0AEX7 | FUNCTION: Part of the binding-protein-dependent transport system for branched-chain amino acids. Probably responsible for the translocation of the substrates across the membrane. | ||
| b3456 | b3456 | High-affinity branched-chain amino acid transport system permease protein LivM (LIV-I protein M) | Cell_inner_membrane | R_ALAabcpp R_ILEabcpp R_LEUabcpp R_LEUabcpp_duplicate_2 R_THRabcpp R_VALabcpp |
425 | Secretion: 425.0, Translation: 425.0, Folding: 42.5 | 46,269 | UniprotID: P22729 | FUNCTION: Part of the binding-protein-dependent transport system for branched-chain amino acids. Probably responsible for the translocation of the substrates across the membrane. | ||
| b2215 | b2215 | Outer membrane protein C (Outer membrane protein 1B) (Porin OmpC) | Cell_outer_membrane | R_pqqtex_duplicate_4_enzyme R_12PPDRtex_duplicate_4_enzyme R_12PPDStex_duplicate_4_enzyme R_23CAMPtex_duplicate_4_enzyme R_23CCMPtex_duplicate_4_enzyme R_23CGMPtex_duplicate_4_enzyme R_23CUMPtex_duplicate_4_enzyme R_23DAPPAtex_duplicate_4_enzyme R_26DAHtex_duplicate_4_enzyme R_34dhpactex_duplicate_4_enzyme R_3AMPtex_duplicate_4_enzyme R_3CMPtex_duplicate_4_enzyme R_3GMPtex_enzyme R_3HPPtex_enzyme R_3PEPTtex_duplicate_4_enzyme R_3UMPtex_duplicate_4_enzyme R_4HOXPACDtex_duplicate_4_enzyme R_4PEPTtex_duplicate_4_enzyme R_5DGLCNtex_enzyme R_5MTRtex_enzyme R_ABUTtex_duplicate_4_enzyme R_ACACtex_duplicate_4_enzyme R_ACALDtex_duplicate_4_enzyme R_ACGAL1Ptex_duplicate_4_enzyme R_ACGALtex_duplicate_4_enzyme R_ACGAM1Ptex_duplicate_4_enzyme R_ACGAtex_duplicate_4_enzyme R_ACMANAtex_duplicate_4_enzyme R_ACMUMtex_duplicate_4_enzyme R_ACNAMtex_duplicate_3_enzyme R_ACSERtex_duplicate_3_enzyme R_ACtex_duplicate_4_enzyme R_ADEtex_duplicate_4_enzyme R_AGMtex_duplicate_4_enzyme R_AKGtex_duplicate_4_enzyme R_ALAALAtex_duplicate_4_enzyme R_ALAtex_duplicate_4_enzyme R_ALLTNtex_duplicate_4_enzyme R_ALLtex_duplicate_4_enzyme R_AMPtex_duplicate_2_enzyme R_ANHGMtex_duplicate_4_enzyme R_ARBTtex_duplicate_2_enzyme R_ARBtex_duplicate_4_enzyme R_ARGtex_duplicate_4_enzyme R_ASCBtex_duplicate_4_enzyme R_ASNtex_duplicate_4_enzyme R_ASO3tex_duplicate_4_enzyme R_ASPtex_duplicate_4_enzyme R_BALAtex_duplicate_4_enzyme R_BTNtex_duplicate_2_enzyme R_BUTSO3tex_duplicate_4_enzyme R_BUTtex_duplicate_4_enzyme R_CA2tex_duplicate_4_enzyme R_CD2tex_duplicate_4_enzyme R_CGLYtex_duplicate_4_enzyme R_CHLtex_duplicate_4_enzyme R_CHTBStex_duplicate_2_enzyme R_CITtex_duplicate_4_enzyme R_CLtex_duplicate_4_enzyme R_CMPtex_duplicate_4_enzyme R_CMtex_duplicate_3_enzyme R_CO2tex_duplicate_4_enzyme R_COBALT2tex_duplicate_4_enzyme R_CRNDtex_duplicate_3_enzyme R_CRNtex_duplicate_4_enzyme R_CSNtex_duplicate_4_enzyme R_CU2tex_duplicate_2_enzyme R_CUtex_duplicate_4_enzyme R_CYANtex_duplicate_4_enzyme R_CYNTtex_duplicate_4_enzyme R_CYSDtex_duplicate_4_enzyme R_CYStex_duplicate_4_enzyme R_CYTDtex_duplicate_4_enzyme R_D_LACtex_duplicate_4_enzyme R_DALAtex_duplicate_4_enzyme R_DAMPtex_duplicate_4_enzyme R_DAPtex_duplicate_4_enzyme R_DCAtex_duplicate_4_enzyme R_DCMPtex_duplicate_4_enzyme R_DDGLCNtex_enzyme R_DGMPtex_duplicate_4_enzyme R_DGSNtex_duplicate_4_enzyme R_DHAtex_duplicate_4_enzyme R_DIMPtex_duplicate_4_enzyme R_DINStex_duplicate_4_enzyme R_DMSOtex_duplicate_4_enzyme R_DMStex_duplicate_4_enzyme R_DOPAtex_duplicate_4_enzyme R_DOXRBCNtex_duplicate_3_enzyme R_DSERtex_duplicate_4_enzyme R_DTMPtex_duplicate_4_enzyme R_DUMPtex_duplicate_4_enzyme R_ETHAtex_duplicate_4_enzyme R_ETHSO3tex_duplicate_4_enzyme R_ETOHtex_duplicate_4_enzyme R_F6Ptex_duplicate_4_enzyme R_FALDtex_duplicate_4_enzyme R_FE2tex_duplicate_4_enzyme R_FE3tex_duplicate_4_enzyme R_FORtex_duplicate_4_enzyme R_FRULYStex_duplicate_4_enzyme R_FRUURtex_duplicate_4_enzyme R_FRUtex_duplicate_4_enzyme R_FUCtex_duplicate_4_enzyme R_FUMtex_duplicate_4_enzyme R_FUSAtex_duplicate_3_enzyme R_G1Ptex_duplicate_4_enzyme R_G3PCtex_duplicate_4_enzyme R_G3PEtex_enzyme R_G3PGtex_duplicate_4_enzyme R_G3PItex_duplicate_4_enzyme R_G3PStex_duplicate_4_enzyme R_G6Ptex_duplicate_4_enzyme R_GAL1Ptex_duplicate_4_enzyme R_GALBDtex_duplicate_4_enzyme R_GALCTNLtex_duplicate_2_enzyme R_GALCTNtex_duplicate_4_enzyme R_GALCTtex_duplicate_4_enzyme R_GALTtex_duplicate_4_enzyme R_GALURtex_duplicate_4_enzyme R_GALtex_duplicate_4_enzyme R_GAMAN6Ptex_duplicate_4_enzyme R_GAMtex_duplicate_4_enzyme R_GBBTNtex_duplicate_4_enzyme R_GDPtex_duplicate_3_enzyme R_GLCNtex_duplicate_4_enzyme R_GLCRtex_duplicate_4_enzyme R_GLCUR1Ptex_duplicate_4_enzyme R_GLCURtex_duplicate_4_enzyme R_GLCtex_copy1_duplicate_4_enzyme R_GLNtex_duplicate_4_enzyme R_GLUtex_duplicate_4_enzyme R_GLYALDtex_duplicate_4_enzyme R_GLYBtex_duplicate_4_enzyme R_GLYC2Ptex_duplicate_2_enzyme R_GLYC3Ptex_duplicate_4_enzyme R_GLYCAtex_duplicate_4_enzyme R_GLYCLTtex_duplicate_4_enzyme R_GLYCtex_duplicate_4_enzyme R_GLYtex_duplicate_4_enzyme R_GMPtex_duplicate_3_enzyme R_GSNtex_duplicate_4_enzyme R_GTHOXtex_duplicate_4_enzyme R_GTHRDtex_duplicate_4_enzyme R_GTPtex_duplicate_4_enzyme R_H2O2tex_duplicate_4_enzyme R_H2Otex_duplicate_6_enzyme R_H2Stex_duplicate_4_enzyme R_H2tex_duplicate_4_enzyme R_HCINNMtex_duplicate_4_enzyme R_HG2tex_duplicate_4_enzyme R_HIStex_duplicate_4_enzyme R_HOMtex_duplicate_4_enzyme R_HPPPNtex_enzyme R_HXAtex_duplicate_2_enzyme R_HYXNtex_duplicate_4_enzyme R_Htex_enzyme R_IDONtex_duplicate_4_enzyme R_ILEtex_duplicate_4_enzyme R_IMPtex_duplicate_4_enzyme R_INDOLEtex_duplicate_4_enzyme R_INSTtex_duplicate_4_enzyme R_ISETACtex_duplicate_4_enzyme R_Ktex_duplicate_4_enzyme R_L_LACtex_enzyme R_LALADGLUtex_duplicate_2_enzyme R_LALALGLUtex_duplicate_2_enzyme R_LCTStex_duplicate_4_enzyme R_LEUtex_duplicate_4_enzyme R_LIPOtex_duplicate_3_enzyme R_LYStex_duplicate_4_enzyme R_LYXtex_duplicate_4_enzyme R_MALDtex_duplicate_2_enzyme R_MALtex_duplicate_4_enzyme R_MAN6Ptex_duplicate_4_enzyme R_MANGLYCtex_duplicate_4_enzyme R_MANtex_duplicate_4_enzyme R_MELIBtex_duplicate_4_enzyme R_MEOHtex_enzyme R_METDtex_duplicate_4_enzyme R_METSOX1tex_duplicate_4_enzyme R_METSOX2tex_duplicate_4_enzyme R_METtex_duplicate_4_enzyme R_MG2tex_duplicate_4_enzyme R_MINCYCtex_duplicate_3_enzyme R_MMETtex_duplicate_4_enzyme R_MNLtex_duplicate_4_enzyme R_MNtex_duplicate_4_enzyme R_MOBDtex_duplicate_4_enzyme R_MSO3tex_duplicate_4_enzyme R_N2Otex_duplicate_4_enzyme R_NACtex_duplicate_4_enzyme R_NAtex_duplicate_4_enzyme R_NH4tex_duplicate_4_enzyme R_NI2tex_duplicate_4_enzyme R_NMNtex_duplicate_4_enzyme R_NO2tex_duplicate_4_enzyme R_NO3tex_duplicate_4_enzyme R_NOtex_duplicate_4_enzyme R_O2Stex_duplicate_3_enzyme R_O2tex_duplicate_4_enzyme R_OCTAtex_duplicate_4_enzyme R_ORNtex_duplicate_4_enzyme R_OROTtex_duplicate_2_enzyme R_PACALDtex_duplicate_4_enzyme R_PEAMNtex_duplicate_4_enzyme R_PHEtex_duplicate_4_enzyme R_PItex_duplicate_4_enzyme R_PNTOtex_duplicate_4_enzyme R_PPALtex_duplicate_4_enzyme R_PPAtex_enzyme R_PPPNtex_duplicate_4_enzyme R_PPTtex_duplicate_4_enzyme R_PROGLYtex_duplicate_4_enzyme R_PROtex_duplicate_3_enzyme R_PSCLYStex_duplicate_2_enzyme R_PSERtex_duplicate_4_enzyme R_PTRCtex_duplicate_4_enzyme R_PYDAMtex_duplicate_2_enzyme R_PYDXNtex_duplicate_2_enzyme R_PYDXtex_duplicate_2_enzyme R_PYRtex_duplicate_4_enzyme R_QUIN2tex_duplicate_2_enzyme R_R5Ptex_duplicate_4_enzyme R_RIBtex_duplicate_4_enzyme R_RMNtex_duplicate_2_enzyme R_SBTtex_duplicate_4_enzyme R_SELtex_enzyme R_SERtex_duplicate_4_enzyme R_SKMtex_duplicate_4_enzyme R_SLNTtex_enzyme R_SO2tex_duplicate_4_enzyme R_SO3tex_duplicate_4_enzyme R_SO4tex_duplicate_4_enzyme R_SPMDtex_duplicate_4_enzyme R_SUCCtex_duplicate_4_enzyme R_SUCRtex_duplicate_4_enzyme R_SULFACtex_duplicate_3_enzyme R_TARTRDtex_duplicate_3_enzyme R_TARTRtex_duplicate_4_enzyme R_TAURtex_duplicate_4_enzyme R_TCYNTtex_duplicate_4_enzyme R_THMDtex_duplicate_4_enzyme R_THMtex_duplicate_4_enzyme R_THRPtex_duplicate_4_enzyme R_THRtex_duplicate_4_enzyme R_THYMtex_enzyme R_TMAOtex_duplicate_4_enzyme R_TMAtex_duplicate_4_enzyme R_TREtex_duplicate_4_enzyme R_TRPtex_duplicate_4_enzyme R_TSULtex_duplicate_4_enzyme R_TTRCYCtex_duplicate_3_enzyme R_TUNGStex_duplicate_2_enzyme R_TYMtex_duplicate_4_enzyme R_TYRPtex_duplicate_2_enzyme R_TYRtex_duplicate_4_enzyme R_UACGAMtex_duplicate_4_enzyme R_UDPACGALtex_duplicate_4_enzyme R_UDPGALtex_duplicate_4_enzyme R_UDPGLCURtex_duplicate_4_enzyme R_UDPGtex_duplicate_4_enzyme R_UMPtex_enzyme R_URAtex_duplicate_4_enzyme R_UREAtex_duplicate_4_enzyme R_VALtex_duplicate_4_enzyme R_XANtex_duplicate_4_enzyme R_XMPtex_duplicate_4_enzyme R_XTSNtex_duplicate_4_enzyme R_XYLUtex_duplicate_4_enzyme R_XYLtex_duplicate_4_enzyme R_Zn2tex_duplicate_4_enzyme |
R_pqqtex_duplicate_4 R_12PPDRtex_duplicate_4 R_12PPDStex_duplicate_4 R_23CAMPtex_duplicate_4 R_23CCMPtex_duplicate_4 R_23CGMPtex_duplicate_4 R_23CUMPtex_duplicate_4 R_23DAPPAtex_duplicate_4 R_26DAHtex_duplicate_4 R_34dhpactex_duplicate_4 R_3AMPtex_duplicate_4 R_3CMPtex_duplicate_4 R_3GMPtex R_3HPPtex R_3PEPTtex_duplicate_4 R_3UMPtex_duplicate_4 R_4HOXPACDtex_duplicate_4 R_4PEPTtex_duplicate_4 R_5DGLCNtex R_5MTRtex R_ABUTtex_duplicate_4 R_ACACtex_duplicate_4 R_ACALDtex_duplicate_4 R_ACGAL1Ptex_duplicate_4 R_ACGALtex_duplicate_4 R_ACGAM1Ptex_duplicate_4 R_ACGAtex_duplicate_4 R_ACMANAtex_duplicate_4 R_ACMUMtex_duplicate_4 R_ACNAMtex_duplicate_3 R_ACSERtex_duplicate_3 R_ACtex_duplicate_4 R_ADEtex_duplicate_4 R_AGMtex_duplicate_4 R_AKGtex_duplicate_4 R_ALAALAtex_duplicate_4 R_ALAtex_duplicate_4 R_ALLTNtex_duplicate_4 R_ALLtex_duplicate_4 R_AMPtex_duplicate_2 R_ANHGMtex_duplicate_4 R_ARBTtex_duplicate_2 R_ARBtex_duplicate_4 R_ARGtex_duplicate_4 R_ASCBtex_duplicate_4 R_ASNtex_duplicate_4 R_ASO3tex_duplicate_4 R_ASPtex_duplicate_4 R_BALAtex_duplicate_4 R_BTNtex_duplicate_2 R_BUTSO3tex_duplicate_4 R_BUTtex_duplicate_4 R_CA2tex_duplicate_4 R_CD2tex_duplicate_4 R_CGLYtex_duplicate_4 R_CHLtex_duplicate_4 R_CHTBStex_duplicate_2 R_CITtex_duplicate_4 R_CLtex_duplicate_4 R_CMPtex_duplicate_4 R_CMtex_duplicate_3 R_CO2tex_duplicate_4 R_COBALT2tex_duplicate_4 R_CRNDtex_duplicate_3 R_CRNtex_duplicate_4 R_CSNtex_duplicate_4 R_CU2tex_duplicate_2 R_CUtex_duplicate_4 R_CYANtex_duplicate_4 R_CYNTtex_duplicate_4 R_CYSDtex_duplicate_4 R_CYStex_duplicate_4 R_CYTDtex_duplicate_4 R_D_LACtex_duplicate_4 R_DALAtex_duplicate_4 R_DAMPtex_duplicate_4 R_DAPtex_duplicate_4 R_DCAtex_duplicate_4 R_DCMPtex_duplicate_4 R_DDGLCNtex R_DGMPtex_duplicate_4 R_DGSNtex_duplicate_4 R_DHAtex_duplicate_4 R_DIMPtex_duplicate_4 R_DINStex_duplicate_4 R_DMSOtex_duplicate_4 R_DMStex_duplicate_4 R_DOPAtex_duplicate_4 R_DOXRBCNtex_duplicate_3 R_DSERtex_duplicate_4 R_DTMPtex_duplicate_4 R_DUMPtex_duplicate_4 R_ETHAtex_duplicate_4 R_ETHSO3tex_duplicate_4 R_ETOHtex_duplicate_4 R_F6Ptex_duplicate_4 R_FALDtex_duplicate_4 R_FE2tex_duplicate_4 R_FE3tex_duplicate_4 R_FORtex_duplicate_4 R_FRULYStex_duplicate_4 R_FRUURtex_duplicate_4 R_FRUtex_duplicate_4 R_FUCtex_duplicate_4 R_FUMtex_duplicate_4 R_FUSAtex_duplicate_3 R_G1Ptex_duplicate_4 R_G3PCtex_duplicate_4 R_G3PEtex R_G3PGtex_duplicate_4 R_G3PItex_duplicate_4 R_G3PStex_duplicate_4 R_G6Ptex_duplicate_4 R_GAL1Ptex_duplicate_4 R_GALBDtex_duplicate_4 R_GALCTNLtex_duplicate_2 R_GALCTNtex_duplicate_4 R_GALCTtex_duplicate_4 R_GALTtex_duplicate_4 R_GALURtex_duplicate_4 R_GALtex_duplicate_4 R_GAMAN6Ptex_duplicate_4 R_GAMtex_duplicate_4 R_GBBTNtex_duplicate_4 R_GDPtex_duplicate_3 R_GLCNtex_duplicate_4 R_GLCRtex_duplicate_4 R_GLCUR1Ptex_duplicate_4 R_GLCURtex_duplicate_4 R_GLCtex_copy1_duplicate_4 R_GLNtex_duplicate_4 R_GLUtex_duplicate_4 R_GLYALDtex_duplicate_4 R_GLYBtex_duplicate_4 R_GLYC2Ptex_duplicate_2 R_GLYC3Ptex_duplicate_4 R_GLYCAtex_duplicate_4 R_GLYCLTtex_duplicate_4 R_GLYCtex_duplicate_4 R_GLYtex_duplicate_4 R_GMPtex_duplicate_3 R_GSNtex_duplicate_4 R_GTHOXtex_duplicate_4 R_GTHRDtex_duplicate_4 R_GTPtex_duplicate_4 R_H2O2tex_duplicate_4 R_H2Otex_duplicate_6 R_H2Stex_duplicate_4 R_H2tex_duplicate_4 R_HCINNMtex_duplicate_4 R_HG2tex_duplicate_4 R_HIStex_duplicate_4 R_HOMtex_duplicate_4 R_HPPPNtex R_HXAtex_duplicate_2 R_HYXNtex_duplicate_4 R_Htex R_IDONtex_duplicate_4 R_ILEtex_duplicate_4 R_IMPtex_duplicate_4 R_INDOLEtex_duplicate_4 R_INSTtex_duplicate_4 R_ISETACtex_duplicate_4 R_Ktex_duplicate_4 R_L_LACtex R_LALADGLUtex_duplicate_2 R_LALALGLUtex_duplicate_2 R_LCTStex_duplicate_4 R_LEUtex_duplicate_4 R_LIPOtex_duplicate_3 R_LYStex_duplicate_4 R_LYXtex_duplicate_4 R_MALDtex_duplicate_2 R_MALtex_duplicate_4 R_MAN6Ptex_duplicate_4 R_MANGLYCtex_duplicate_4 R_MANtex_duplicate_4 R_MELIBtex_duplicate_4 R_MEOHtex R_METDtex_duplicate_4 R_METSOX1tex_duplicate_4 R_METSOX2tex_duplicate_4 R_METtex_duplicate_4 R_MG2tex_duplicate_4 R_MINCYCtex_duplicate_3 R_MMETtex_duplicate_4 R_MNLtex_duplicate_4 R_MNtex_duplicate_4 R_MOBDtex_duplicate_4 R_MSO3tex_duplicate_4 R_N2Otex_duplicate_4 R_NACtex_duplicate_4 R_NAtex_duplicate_4 R_NH4tex_duplicate_4 R_NI2tex_duplicate_4 R_NMNtex_duplicate_4 R_NO2tex_duplicate_4 R_NO3tex_duplicate_4 R_NOtex_duplicate_4 R_O2Stex_duplicate_3 R_O2tex_duplicate_4 R_OCTAtex_duplicate_4 R_ORNtex_duplicate_4 R_OROTtex_duplicate_2 R_PACALDtex_duplicate_4 R_PEAMNtex_duplicate_4 R_PHEtex_duplicate_4 R_PItex_duplicate_4 R_PNTOtex_duplicate_4 R_PPALtex_duplicate_4 R_PPAtex R_PPPNtex_duplicate_4 R_PPTtex_duplicate_4 R_PROGLYtex_duplicate_4 R_PROtex_duplicate_3 R_PSCLYStex_duplicate_2 R_PSERtex_duplicate_4 R_PTRCtex_duplicate_4 R_PYDAMtex_duplicate_2 R_PYDXNtex_duplicate_2 R_PYDXtex_duplicate_2 R_PYRtex_duplicate_4 R_QUIN2tex_duplicate_2 R_R5Ptex_duplicate_4 R_RIBtex_duplicate_4 R_RMNtex_duplicate_2 R_SBTtex_duplicate_4 R_SELtex R_SERtex_duplicate_4 R_SKMtex_duplicate_4 R_SLNTtex R_SO2tex_duplicate_4 R_SO3tex_duplicate_4 R_SO4tex_duplicate_4 R_SPMDtex_duplicate_4 R_SUCCtex_duplicate_4 R_SUCRtex_duplicate_4 R_SULFACtex_duplicate_3 R_TARTRDtex_duplicate_3 R_TARTRtex_duplicate_4 R_TAURtex_duplicate_4 R_TCYNTtex_duplicate_4 R_THMDtex_duplicate_4 R_THMtex_duplicate_4 R_THRPtex_duplicate_4 R_THRtex_duplicate_4 R_THYMtex R_TMAOtex_duplicate_4 R_TMAtex_duplicate_4 R_TREtex_duplicate_4 R_TRPtex_duplicate_4 R_TSULtex_duplicate_4 R_TTRCYCtex_duplicate_3 R_TUNGStex_duplicate_2 R_TYMtex_duplicate_4 R_TYRPtex_duplicate_2 R_TYRtex_duplicate_4 R_UACGAMtex_duplicate_4 R_UDPACGALtex_duplicate_4 R_UDPGALtex_duplicate_4 R_UDPGLCURtex_duplicate_4 R_UDPGtex_duplicate_4 R_UMPtex R_URAtex_duplicate_4 R_UREAtex_duplicate_4 R_VALtex_duplicate_4 R_XANtex_duplicate_4 R_XMPtex_duplicate_4 R_XTSNtex_duplicate_4 R_XYLUtex_duplicate_4 R_XYLtex_duplicate_4 R_Zn2tex_duplicate_4 |
367 | Secretion: 367.0, Translation: 367.0, Folding: 36.7 | 40,368 | UniprotID: P06996 | FUNCTION: Forms pores that allow passive diffusion of small molecules across the outer membrane. | |
| b2210 | b2210 | Malate:quinone oxidoreductase (EC 1.1.5.4) (MQO) (Malate dehydrogenase [quinone]) | Cytoplasm | R_MDH2_enzyme R_MDH3_enzyme |
R_MDH2 R_MDH3 |
548 | Translation: 548.0, Folding: 54.8 | 60,230 | UniprotID: P33940 ECnumber: EC 1.1.5.4 |
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| b3857 | b3857 | Molybdenum cofactor guanylyltransferase (MoCo guanylyltransferase) (EC 2.7.7.77) (GTP:molybdopterin guanylyltransferase) (Mo-MPT guanylyltransferase) (Molybdopterin guanylyltransferase) (Molybdopterin-guanine dinucleotide biosynthesis protein A) (Molybdopterin-guanine dinucleotide synthase) (MGD synthase) (Protein FA) | Cytoplasm | 194 | Translation: 194.0, Folding: 19.4 | 21,643 | UniprotID: P32173 ECnumber: EC 2.7.7.77 |
FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP cannot be utilized. {ECO:0000269|PubMed:10978348, ECO:0000269|PubMed:1648082, ECO:0000269|PubMed:21081498, ECO:0000269|PubMed:8020507}. |
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| b3856 | b3856 | Molybdopterin-guanine dinucleotide biosynthesis adapter protein (MGD biosynthesis adapter protein) (Molybdenum cofactor biosynthesis adapter protein) (Moco biosynthesis adapter protein) (Molybdopterin-guanine dinucleotide biosynthesis protein B) | Cytoplasm | R_BMOGDS1_duplicate_2 R_BMOGDS2_duplicate_2 R_BWCOGDS1_duplicate_2 R_BWCOGDS2_duplicate_2 R_MOGDS_duplicate_2 |
175 | Translation: 175.0, Folding: 17.5 | 19,363 | UniprotID: P32125 | FUNCTION: GTP-binding protein that is not required for the biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor, and not necessary for the formation of active molybdoenzymes using this form of molybdenum cofactor. May act as an adapter protein to achieve the efficient biosynthesis and utilization of MGD. Displays a weak intrinsic GTPase activity. Is also able to bind the nucleotides ATP, TTP and GDP, but with lower affinity than GTP. {ECO:0000269|PubMed:12682065, ECO:0000269|PubMed:9219527}. |
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| b3850 | b3850 | Protoporphyrinogen IX dehydrogenase [menaquinone] (EC 1.3.5.3) | Cytoplasm | R_PPPGO_enzyme R_PPPGO3_enzyme |
R_PPPGO R_PPPGO3 |
181 | Translation: 181.0, Folding: 18.1 | 21,226 | UniprotID: P0ACB4 ECnumber: EC 1.3.5.3 |
FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX using menaquinone as electron acceptor. | |
| b2585 | b2585 | CDP-diacylglycerol--serine O-phosphatidyltransferase (EC 2.7.8.8) (Phosphatidylserine synthase) | Cytoplasm | R_PSSA120 R_PSSA140 R_PSSA141 R_PSSA160 R_PSSA161 R_PSSA180 R_PSSA181 |
451 | Translation: 451.0, Folding: 45.1 | 52,802 | UniprotID: P23830 ECnumber: EC 2.7.8.8 |
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| b2587 | b2587 | Alpha-ketoglutarate permease | Cell_inner_membrane | R_AKGt2rpp_enzyme | R_AKGt2rpp | 432 | Secretion: 432.0, Translation: 432.0, Folding: 43.2 | 47,052 | UniprotID: P0AEX3 | FUNCTION: Uptake of alpha-ketoglutarate across the boundary membrane with the concomitant import of a cation (symport system). {ECO:0000269|PubMed:2053984}. | |
| b2582 | b2582 | Thioredoxin 2 (Trx-2) (EC 1.8.1.8) (Protein-disulfide reductase) | Cytoplasm | 139 | Translation: 139.0, Folding: 13.9 | 15,555 | UniprotID: P0AGG4 ECnumber: EC 1.8.1.8 |
FUNCTION: Efficient electron donor for the essential enzyme ribonucleotide reductase. Is also able to reduce the interchain disulfide bridges of insulin. | |||
| b2103 | b2103 | Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase (EC 2.7.1.49) (EC 2.7.4.7) (Hydroxymethylpyrimidine kinase) (HMP kinase) (Hydroxymethylpyrimidine phosphate kinase) (HMP-P kinase) (HMP-phosphate kinase) (HMPP kinase) | Cytoplasm | R_HMPK1_enzyme R_PMPK_enzyme |
R_HMPK1 R_PMPK |
266 | Translation: 266.0, Folding: 26.6 | 28,634 | UniprotID: P76422 ECnumber: EC 2.7.1.49; 2.7.4.7 |
FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. {ECO:0000269|PubMed:10075431}. | |
| b2104 | b2104 | Hydroxyethylthiazole kinase (EC 2.7.1.50) (4-methyl-5-beta-hydroxyethylthiazole kinase) (TH kinase) (Thz kinase) | Cytoplasm | R_HETZK_enzyme | R_HETZK | 262 | Translation: 262.0, Folding: 26.2 | 27,339 | UniprotID: P76423 ECnumber: EC 2.7.1.50 |
FUNCTION: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ). {ECO:0000255|HAMAP-Rule:MF_00228, ECO:0000269|PubMed:2542220}. | |
| b2458 | b2458 | Ethanolamine utilization protein EutD | Cytoplasm | R_PTAr_duplicate_2_enzyme | R_PTAr_duplicate_2 | 338 | Translation: 338.0, Folding: 33.8 | 36,067 | UniprotID: P77218 | ||
| b1800 | b1800 | D-malate dehydrogenase [decarboxylating] (EC 1.1.1.83) (D-malate degradation protein A) (D-malate oxidase) | Cytoplasm | R_MALDDH_enzyme | R_MALDDH | 361 | Translation: 361.0, Folding: 36.1 | 40,315 | UniprotID: P76251 ECnumber: EC 1.1.1.83 |
FUNCTION: Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D-malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L-tartrate as a substrate for dehydrogenation instead of D-malate. {ECO:0000269|PubMed:20233924}. |
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| b1801 | b1801 | Uncharacterized transporter YeaV | Cell_inner_membrane | R_CHLt2pp_duplicate_2_enzyme R_GLYBt2pp_enzyme R_GLYt2pp_copy1_duplicate_2_enzyme |
R_CHLt2pp_duplicate_2 R_GLYBt2pp R_GLYt2pp_copy1_duplicate_2 |
481 | Secretion: 481.0, Translation: 481.0, Folding: 48.1 | 52,881 | UniprotID: P0ABD1 | FUNCTION: Probable transporter whose substrate is unknown. Is not involved in aerobic D-malate transport. | |
| b1805 | b1805 | Long-chain-fatty-acid--CoA ligase (EC 6.2.1.3) (Long-chain acyl-CoA synthetase) (Acyl-CoA synthetase) | Cell_inner_membrane | 561 | Secretion: 561.0, Translation: 561.0, Folding: 56.1 | 62,332 | UniprotID: P69451 ECnumber: EC 6.2.1.3 |
FUNCTION: Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms (PubMed:15213221). Is involved in the aerobic beta-oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source (PubMed:12535077). {ECO:0000269|PubMed:12535077, ECO:0000269|PubMed:15213221}. |
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| b4213 | b4213 | 2,3-cyclic-nucleotide 2-phosphodiesterase/3-nucleotidase (EC 3.1.3.6) (EC 3.1.4.16) | Periplasm | 647 | Secretion: 647.0, Translation: 647.0, Folding: 64.7 | 70,832 | UniprotID: P08331 ECnumber: EC 3.1.3.6; 3.1.4.16 |
FUNCTION: This bifunctional enzyme catalyzes two consecutive reactions during ribonucleic acid degradation. Converts a 2,3-cyclic nucleotide to a 3-nucleotide and then the 3-nucleotide to the corresponding nucleoside and phosphate. {ECO:0000269|PubMed:3005231}. | |||
| b1378 | b1378 | Probable pyruvate-flavodoxin oxidoreductase (EC 1.2.7.-) | Cytoplasm | R_POR5_enzyme R_POR5_duplicate_2_enzyme |
R_POR5 R_POR5_duplicate_2 |
1174 | Translation: 1174.0, Folding: 117.4 | 128,824 | UniprotID: P52647 ECnumber: EC 1.2.7.- |
FUNCTION: Oxidoreductase required for the transfer of electrons from pyruvate to flavodoxin. {ECO:0000305}. | |
| b0778 | b0778 | ATP-dependent dethiobiotin synthetase BioD 1 (EC 6.3.3.3) (DTB synthetase 1) (DTBS 1) (Dethiobiotin synthase) | Cytoplasm | R_DBTS_enzyme | R_DBTS | 225 | Translation: 225.0, Folding: 22.5 | 24,140 | UniprotID: P13000 ECnumber: EC 6.3.3.3 |
FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid. {ECO:0000269|PubMed:4892372, ECO:0000269|PubMed:4921568}. | |
| b4214 | b4214 | 3(2),5-bisphosphate nucleotidase CysQ (EC 3.1.3.7) (3(2),5-bisphosphonucleoside 3(2)-phosphohydrolase) (3-phosphoadenosine 5-phosphate phosphatase) (PAP phosphatase) (DPNPase) | Cell_inner_membrane | R_BPNT_enzyme | R_BPNT | 246 | Secretion: 246.0, Translation: 246.0, Folding: 24.6 | 27,176 | UniprotID: P22255 ECnumber: EC 3.1.3.7 |
FUNCTION: Converts adenosine-3,5-bisphosphate (PAP) to AMP. May also convert adenosine 3-phosphate 5-phosphosulfate (PAPS) to adenosine 5-phosphosulfate (APS). Has 10000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2). {ECO:0000269|PubMed:10224133, ECO:0000269|PubMed:16682444, ECO:0000269|PubMed:7493934}. | |
| b0775 | b0775 | Biotin synthase (EC 2.8.1.6) | Cytoplasm | R_BTS5_enzyme | R_BTS5 | 346 | Translation: 346.0, Folding: 34.6 | 38,648 | UniprotID: P12996 ECnumber: EC 2.8.1.6 |
FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. {ECO:0000269|PubMed:8142361}. | |
| b0774 | b0774 | Adenosylmethionine-8-amino-7-oxononanoate aminotransferase (EC 2.6.1.62) (7,8-diamino-pelargonic acid aminotransferase) (DAPA AT) (DAPA aminotransferase) (7,8-diaminononanoate synthase) (DANS) (Diaminopelargonic acid synthase) | Cytoplasm | R_AMAOTr_enzyme | R_AMAOTr | 429 | Translation: 429.0, Folding: 42.9 | 47,336 | UniprotID: P12995 ECnumber: EC 2.6.1.62 |
FUNCTION: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor. {ECO:0000269|PubMed:1092681}. | |
| b0777 | b0777 | Malonyl-[acyl-carrier protein] O-methyltransferase (Malonyl-ACP O-methyltransferase) (EC 2.1.1.197) (Biotin synthesis protein BioC) | Cytoplasm | R_MALCOAMT_enzyme | R_MALCOAMT | 251 | Translation: 251.0, Folding: 25.1 | 28,276 | UniprotID: P12999 ECnumber: EC 2.1.1.197 |
FUNCTION: Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L-methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. {ECO:0000269|PubMed:20693992, ECO:0000269|PubMed:4864413}. |
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| b0776 | b0776 | 8-amino-7-oxononanoate synthase (AONS) (EC 2.3.1.47) (7-keto-8-amino-pelargonic acid synthase) (7-KAP synthase) (KAPA synthase) (8-amino-7-ketopelargonate synthase) | Cytoplasm | R_AOXSr2_enzyme | R_AOXSr2 | 384 | Translation: 384.0, Folding: 38.4 | 41,594 | UniprotID: P12998 ECnumber: EC 2.3.1.47 |
FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate, but it is believed that pimeloyl-ACP rather than pimeloyl-CoA is the physiological substrate of BioF. {ECO:0000269|PubMed:10642176, ECO:0000269|PubMed:20693992}. |
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| b1377 | b1377 | Outer membrane protein N (Porin OmpN) | Cell_outer_membrane | R_pqqtex_duplicate_3_enzyme R_12PPDRtex_enzyme R_12PPDStex_enzyme R_23CAMPtex_enzyme R_23CCMPtex_enzyme R_23CGMPtex_enzyme R_23CUMPtex_enzyme R_23DAPPAtex_enzyme R_26DAHtex_enzyme R_34dhpactex_enzyme R_3AMPtex_enzyme R_3CMPtex_enzyme R_3GMPtex_duplicate_3_enzyme R_3HPPtex_duplicate_2_enzyme R_3PEPTtex_enzyme R_3UMPtex_enzyme R_4HOXPACDtex_enzyme R_4PEPTtex_enzyme R_5DGLCNtex_duplicate_4_enzyme R_5MTRtex_duplicate_2_enzyme R_ABUTtex_enzyme R_ACACtex_enzyme R_ACALDtex_enzyme R_ACGAL1Ptex_enzyme R_ACGALtex_enzyme R_ACGAM1Ptex_enzyme R_ACGAtex_enzyme R_ACMANAtex_enzyme R_ACMUMtex_enzyme R_ACSERtex_duplicate_2_enzyme R_ACtex_enzyme R_ADEtex_enzyme R_AGMtex_enzyme R_AKGtex_enzyme R_ALAALAtex_enzyme R_ALAtex_enzyme R_ALLTNtex_enzyme R_ALLtex_enzyme R_AMPtex_enzyme R_ANHGMtex_enzyme R_ARBTtex_duplicate_3_enzyme R_ARBtex_enzyme R_ARGtex_enzyme R_ASCBtex_enzyme R_ASNtex_enzyme R_ASO3tex_enzyme R_ASPtex_enzyme R_BALAtex_enzyme R_BTNtex_duplicate_3_enzyme R_BUTSO3tex_enzyme R_BUTtex_enzyme R_CA2tex_enzyme R_CD2tex_enzyme R_CGLYtex_enzyme R_CHLtex_enzyme R_CHTBStex_enzyme R_CITtex_enzyme R_CLtex_enzyme R_CMPtex_enzyme R_CMtex_duplicate_2_enzyme R_CO2tex_enzyme R_COBALT2tex_enzyme R_CRNDtex_duplicate_2_enzyme R_CRNtex_enzyme R_CSNtex_enzyme R_CU2tex_duplicate_4_enzyme R_CUtex_enzyme R_CYANtex_enzyme R_CYNTtex_enzyme R_CYSDtex_enzyme R_CYStex_enzyme R_CYTDtex_enzyme R_D_LACtex_enzyme R_DALAtex_enzyme R_DAMPtex_enzyme R_DAPtex_enzyme R_DCAtex_enzyme R_DCMPtex_enzyme R_DDGLCNtex_duplicate_3_enzyme R_DGMPtex_enzyme R_DGSNtex_enzyme R_DHAtex_enzyme R_DIMPtex_enzyme R_DINStex_enzyme R_DMSOtex_enzyme R_DMStex_enzyme R_DOPAtex_enzyme R_DOXRBCNtex_duplicate_2_enzyme R_DSERtex_enzyme R_DTMPtex_enzyme R_DUMPtex_enzyme R_ETHAtex_enzyme R_ETHSO3tex_enzyme R_ETOHtex_enzyme R_F6Ptex_enzyme R_FALDtex_enzyme R_FE2tex_enzyme R_FE3tex_enzyme R_FORtex_enzyme R_FRULYStex_enzyme R_FRUURtex_enzyme R_FRUtex_enzyme R_FUCtex_enzyme R_FUMtex_enzyme R_FUSAtex_duplicate_2_enzyme R_G1Ptex_enzyme R_G3PCtex_enzyme R_G3PEtex_duplicate_3_enzyme R_G3PGtex_enzyme R_G3PItex_enzyme R_G3PStex_enzyme R_G6Ptex_enzyme R_GAL1Ptex_enzyme R_GALBDtex_enzyme R_GALCTNLtex_duplicate_3_enzyme R_GALCTNtex_enzyme R_GALCTtex_enzyme R_GALTtex_enzyme R_GALURtex_enzyme R_GALtex_enzyme R_GAMAN6Ptex_enzyme R_GAMtex_enzyme R_GBBTNtex_enzyme R_GDPtex_duplicate_2_enzyme R_GLCNtex_enzyme R_GLCRtex_enzyme R_GLCUR1Ptex_enzyme R_GLCURtex_enzyme R_GLCtex_copy1_duplicate_3_enzyme R_GLNtex_enzyme R_GLUtex_enzyme R_GLYALDtex_enzyme R_GLYBtex_enzyme R_GLYC2Ptex_duplicate_4_enzyme R_GLYC3Ptex_enzyme R_GLYCAtex_enzyme R_GLYCLTtex_enzyme R_GLYCtex_enzyme R_GLYtex_enzyme R_GMPtex_duplicate_2_enzyme R_GSNtex_enzyme R_GTHOXtex_enzyme R_GTHRDtex_enzyme R_GTPtex_enzyme R_H2O2tex_enzyme R_H2Otex_enzyme R_H2Stex_enzyme R_H2tex_enzyme R_HCINNMtex_enzyme R_HG2tex_enzyme R_HIStex_enzyme R_HOMtex_enzyme R_HPPPNtex_duplicate_3_enzyme R_HXAtex_duplicate_4_enzyme R_HYXNtex_enzyme R_Htex_duplicate_3_enzyme R_IDONtex_enzyme R_ILEtex_enzyme R_IMPtex_enzyme R_INDOLEtex_enzyme R_INSTtex_enzyme R_ISETACtex_enzyme R_Ktex_enzyme R_L_LACtex_duplicate_3_enzyme R_LALADGLUtex_duplicate_3_enzyme R_LALALGLUtex_duplicate_3_enzyme R_LCTStex_enzyme R_LEUtex_enzyme R_LIPOtex_duplicate_2_enzyme R_LYStex_enzyme R_LYXtex_enzyme R_MALDtex_duplicate_3_enzyme R_MALtex_enzyme R_MAN6Ptex_enzyme R_MANGLYCtex_enzyme R_MANtex_enzyme R_MELIBtex_enzyme R_MEOHtex_duplicate_2_enzyme R_METDtex_enzyme R_METSOX1tex_enzyme R_METSOX2tex_enzyme R_METtex_enzyme R_MG2tex_enzyme R_MINCYCtex_duplicate_2_enzyme R_MMETtex_enzyme R_MNLtex_enzyme R_MNtex_enzyme R_MOBDtex_enzyme R_MSO3tex_enzyme R_N2Otex_enzyme R_NACtex_enzyme R_NAtex_enzyme R_NH4tex_enzyme R_NI2tex_enzyme R_NMNtex_enzyme R_NO2tex_enzyme R_NO3tex_duplicate_2_enzyme R_NOtex_enzyme R_O2Stex_duplicate_2_enzyme R_O2tex_enzyme R_OCTAtex_enzyme R_ORNtex_enzyme R_OROTtex_duplicate_3_enzyme R_PACALDtex_enzyme R_PEAMNtex_enzyme R_PHEtex_enzyme R_PItex_enzyme R_PNTOtex_enzyme R_PPALtex_enzyme R_PPAtex_duplicate_2_enzyme R_PPPNtex_enzyme R_PPTtex_enzyme R_PROGLYtex_enzyme R_PROtex_duplicate_2_enzyme R_PSCLYStex_duplicate_3_enzyme R_PSERtex_enzyme R_PTRCtex_enzyme R_PYDAMtex_enzyme R_PYDXNtex_enzyme R_PYDXtex_enzyme R_PYRtex_enzyme R_QUIN2tex_duplicate_3_enzyme R_R5Ptex_enzyme R_RIBtex_enzyme R_RMNtex_duplicate_4_enzyme R_SBTtex_enzyme R_SELtex_duplicate_2_enzyme R_SERtex_enzyme R_SKMtex_enzyme R_SLNTtex_duplicate_2_enzyme R_SO2tex_enzyme R_SO3tex_enzyme R_SO4tex_enzyme R_SPMDtex_enzyme R_SUCCtex_enzyme R_SUCRtex_enzyme R_SULFACtex_duplicate_2_enzyme R_TARTRDtex_duplicate_2_enzyme R_TARTRtex_enzyme R_TAURtex_enzyme R_TCYNTtex_enzyme R_THMDtex_enzyme R_THMtex_enzyme R_THRPtex_enzyme R_THRtex_enzyme R_THYMtex_duplicate_3_enzyme R_TMAOtex_enzyme R_TMAtex_enzyme R_TREtex_enzyme R_TRPtex_enzyme R_TSULtex_enzyme R_TTRCYCtex_duplicate_2_enzyme R_TUNGStex_duplicate_3_enzyme R_TYMtex_enzyme R_TYRPtex_duplicate_4_enzyme R_TYRtex_enzyme R_UACGAMtex_enzyme R_UDPACGALtex_enzyme R_UDPGALtex_enzyme R_UDPGLCURtex_enzyme R_UDPGtex_enzyme R_UMPtex_duplicate_3_enzyme R_URAtex_enzyme R_UREAtex_enzyme R_VALtex_enzyme R_XANtex_enzyme R_XMPtex_enzyme R_XTSNtex_enzyme R_XYLUtex_enzyme R_XYLtex_enzyme R_Zn2tex_enzyme |
R_pqqtex_duplicate_3 R_12PPDRtex R_12PPDStex R_23CAMPtex R_23CCMPtex R_23CGMPtex R_23CUMPtex R_23DAPPAtex R_26DAHtex R_34dhpactex R_3AMPtex R_3CMPtex R_3GMPtex_duplicate_3 R_3HPPtex_duplicate_2 R_3PEPTtex R_3UMPtex R_4HOXPACDtex R_4PEPTtex R_5DGLCNtex_duplicate_4 R_5MTRtex_duplicate_2 R_ABUTtex R_ACACtex R_ACALDtex R_ACGAL1Ptex R_ACGALtex R_ACGAM1Ptex R_ACGAtex R_ACMANAtex R_ACMUMtex R_ACSERtex_duplicate_2 R_ACtex R_ADEtex R_AGMtex R_AKGtex R_ALAALAtex R_ALAtex R_ALLTNtex R_ALLtex R_AMPtex R_ANHGMtex R_ARBTtex_duplicate_3 R_ARBtex R_ARGtex R_ASCBtex R_ASNtex R_ASO3tex R_ASPtex R_BALAtex R_BTNtex_duplicate_3 R_BUTSO3tex R_BUTtex R_CA2tex R_CD2tex R_CGLYtex R_CHLtex R_CHTBStex R_CITtex R_CLtex R_CMPtex R_CMtex_duplicate_2 R_CO2tex R_COBALT2tex R_CRNDtex_duplicate_2 R_CRNtex R_CSNtex R_CU2tex_duplicate_4 R_CUtex R_CYANtex R_CYNTtex R_CYSDtex R_CYStex R_CYTDtex R_D_LACtex R_DALAtex R_DAMPtex R_DAPtex R_DCAtex R_DCMPtex R_DDGLCNtex_duplicate_3 R_DGMPtex R_DGSNtex R_DHAtex R_DIMPtex R_DINStex R_DMSOtex R_DMStex R_DOPAtex R_DOXRBCNtex_duplicate_2 R_DSERtex R_DTMPtex R_DUMPtex R_ETHAtex R_ETHSO3tex R_ETOHtex R_F6Ptex R_FALDtex R_FE2tex R_FE3tex R_FORtex R_FRULYStex R_FRUURtex R_FRUtex R_FUCtex R_FUMtex R_FUSAtex_duplicate_2 R_G1Ptex R_G3PCtex R_G3PEtex_duplicate_3 R_G3PGtex R_G3PItex R_G3PStex R_G6Ptex R_GAL1Ptex R_GALBDtex R_GALCTNLtex_duplicate_3 R_GALCTNtex R_GALCTtex R_GALTtex R_GALURtex R_GALtex R_GAMAN6Ptex R_GAMtex R_GBBTNtex R_GDPtex_duplicate_2 R_GLCNtex R_GLCRtex R_GLCUR1Ptex R_GLCURtex R_GLCtex_copy1_duplicate_3 R_GLNtex R_GLUtex R_GLYALDtex R_GLYBtex R_GLYC2Ptex_duplicate_4 R_GLYC3Ptex R_GLYCAtex R_GLYCLTtex R_GLYCtex R_GLYtex R_GMPtex_duplicate_2 R_GSNtex R_GTHOXtex R_GTHRDtex R_GTPtex R_H2O2tex R_H2Otex R_H2Stex R_H2tex R_HCINNMtex R_HG2tex R_HIStex R_HOMtex R_HPPPNtex_duplicate_3 R_HXAtex_duplicate_4 R_HYXNtex R_Htex_duplicate_3 R_IDONtex R_ILEtex R_IMPtex R_INDOLEtex R_INSTtex R_ISETACtex R_Ktex R_L_LACtex_duplicate_3 R_LALADGLUtex_duplicate_3 R_LALALGLUtex_duplicate_3 R_LCTStex R_LEUtex R_LIPOtex_duplicate_2 R_LYStex R_LYXtex R_MALDtex_duplicate_3 R_MALtex R_MAN6Ptex R_MANGLYCtex R_MANtex R_MELIBtex R_MEOHtex_duplicate_2 R_METDtex R_METSOX1tex R_METSOX2tex R_METtex R_MG2tex R_MINCYCtex_duplicate_2 R_MMETtex R_MNLtex R_MNtex R_MOBDtex R_MSO3tex R_N2Otex R_NACtex R_NAtex R_NH4tex R_NI2tex R_NMNtex R_NO2tex R_NO3tex_duplicate_2 R_NOtex R_O2Stex_duplicate_2 R_O2tex R_OCTAtex R_ORNtex R_OROTtex_duplicate_3 R_PACALDtex R_PEAMNtex R_PHEtex R_PItex R_PNTOtex R_PPALtex R_PPAtex_duplicate_2 R_PPPNtex R_PPTtex R_PROGLYtex R_PROtex_duplicate_2 R_PSCLYStex_duplicate_3 R_PSERtex R_PTRCtex R_PYDAMtex R_PYDXNtex R_PYDXtex R_PYRtex R_QUIN2tex_duplicate_3 R_R5Ptex R_RIBtex R_RMNtex_duplicate_4 R_SBTtex R_SELtex_duplicate_2 R_SERtex R_SKMtex R_SLNTtex_duplicate_2 R_SO2tex R_SO3tex R_SO4tex R_SPMDtex R_SUCCtex R_SUCRtex R_SULFACtex_duplicate_2 R_TARTRDtex_duplicate_2 R_TARTRtex R_TAURtex R_TCYNTtex R_THMDtex R_THMtex R_THRPtex R_THRtex R_THYMtex_duplicate_3 R_TMAOtex R_TMAtex R_TREtex R_TRPtex R_TSULtex R_TTRCYCtex_duplicate_2 R_TUNGStex_duplicate_3 R_TYMtex R_TYRPtex_duplicate_4 R_TYRtex R_UACGAMtex R_UDPACGALtex R_UDPGALtex R_UDPGLCURtex R_UDPGtex R_UMPtex_duplicate_3 R_URAtex R_UREAtex R_VALtex R_XANtex R_XMPtex R_XTSNtex R_XYLUtex R_XYLtex R_Zn2tex |
377 | Secretion: 377.0, Translation: 377.0, Folding: 37.7 | 41,220 | UniprotID: P77747 | FUNCTION: Forms pores that allow passive diffusion of small molecules across the outer membrane (By similarity). Non-specific porin. {ECO:0000250}. | |
| b0511 | b0511 | Putative allantoin permease (Allantoin transport protein) | Cell_inner_membrane | R_ALLTNt2rpp_enzyme | R_ALLTNt2rpp | 484 | Secretion: 484.0, Translation: 484.0, Folding: 48.4 | 52,456 | UniprotID: P75712 | FUNCTION: Transport of allantoin. {ECO:0000250}. | |
| b0512 | b0512 | Allantoinase (EC 3.5.2.5) (Allantoin-utilizing enzyme) | Cytoplasm | R_ALLTN_enzyme | R_ALLTN | 453 | Translation: 453.0, Folding: 45.3 | 49,602 | UniprotID: P77671 ECnumber: EC 3.5.2.5 |
FUNCTION: Catalyzes the conversion of allantoin (5-ureidohydantoin) to allantoic acid by hydrolytic cleavage of the five-member hydantoin ring. {ECO:0000269|PubMed:10601204, ECO:0000269|PubMed:11092864}. | |
| b0514 | b0514 | Glycerate 3-kinase (EC 2.7.1.31) (D-Glycerate-3-kinase) (Glycerate kinase 2) (GK2) | Cytoplasm | 381 | Translation: 381.0, Folding: 38.1 | 38,734 | UniprotID: P77364 ECnumber: EC 2.7.1.31 |
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| b0517 | b0517 | Ureidoglycolate dehydrogenase (NAD(+)) (EC 1.1.1.350) | Cytoplasm | R_URDGLYCD_enzyme | R_URDGLYCD | 349 | Translation: 349.0, Folding: 34.9 | 37,967 | UniprotID: P77555 ECnumber: EC 1.1.1.350 |
FUNCTION: AllD plays a pivotal role as a metabolic branch-point enzyme in nitrogen utilization via the assimilation of allantoin (PubMed:10601204). It is able to utilize allantoin as a sole source of nitrogen under anaerobic conditions (PubMed:10601204). Catalyzes the oxidation of ureidoglycolate to oxalurate (PubMed:23284870). {ECO:0000269|PubMed:10601204, ECO:0000269|PubMed:23284870}. | |
| b0516 | b0516 | Allantoate amidohydrolase (AAH) (EC 3.5.3.9) (Allantoate deiminase) | Cytoplasm | R_ALLTAMH_enzyme | R_ALLTAMH | 411 | Translation: 411.0, Folding: 41.1 | 45,694 | UniprotID: P77425 ECnumber: EC 3.5.3.9 |
FUNCTION: Involved in the anaerobic nitrogen utilization via the assimilation of allantoin (PubMed:10601204, PubMed:20038185). Catalyzes specifically the hydrolysis of allantoate to yield CO2, NH3 and S-ureidoglycine, which is unstable and readily undergoes a second deamination by S-ureidoglycine aminohydrolase AllE to yield S-ureidoglycolate and NH3 (PubMed:20038185). In vivo, the spontaneous release of S-ureidoglycolate and ammonia from S-ureidoglycine appears to be too slow to sustain an efficient flux of nitrogen (PubMed:20038185). {ECO:0000269|PubMed:10601204, ECO:0000269|PubMed:20038185}. |
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| b0688 | b0688 | Phosphoglucomutase (PGM) (EC 5.4.2.2) (Glucose phosphomutase) | Cytoplasm | R_PGMT_duplicate_2_enzyme | R_PGMT_duplicate_2 | 546 | Translation: 546.0, Folding: 54.6 | 58,361 | UniprotID: P36938 ECnumber: EC 5.4.2.2 |
FUNCTION: This enzyme participates in both the breakdown and synthesis of glucose. {ECO:0000269|PubMed:14216423}. | |
| b1773 | b1773 | Uncharacterized protein YdjI | Cytoplasm | R_FBA_enzyme | R_FBA | 278 | Translation: 278.0, Folding: 27.8 | 30,810 | UniprotID: P77704 | ||
| b0680 | b0680 | Glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (GlnRS) | Cytoplasm | R_GLNTRS_enzyme | R_GLNTRS | 554 | Translation: 554.0, Folding: 55.4 | 63,478 | UniprotID: P00962 ECnumber: EC 6.1.1.18 |
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| b0684 | b0684 | Flavodoxin 1 | Cytoplasm | 176 | Translation: 176.0, Folding: 17.6 | 19,737 | UniprotID: P61949 | FUNCTION: Low-potential electron donor to a number of redox enzymes (Potential). Involved in the reactivation of inactive cob(II)alamin in methionine synthase. {ECO:0000269|PubMed:9730838, ECO:0000305}. | |||
| b1778 | b1778 | Peptide methionine sulfoxide reductase MsrB (EC 1.8.4.12) (Peptide-methionine (R)-S-oxide reductase) | Cytoplasm | R_METSOXR2_enzyme R_METSOXR2_duplicate_2_enzyme |
R_METSOXR2 R_METSOXR2_duplicate_2 |
137 | Translation: 137.0, Folding: 13.7 | 15,451 | UniprotID: P0A746 ECnumber: EC 1.8.4.12 |
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| b1779 | b1779 | Glyceraldehyde-3-phosphate dehydrogenase A (GAPDH-A) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase) | Cytoplasm | R_E4PD_duplicate_2_enzyme R_GAPD_enzyme |
R_E4PD_duplicate_2 R_GAPD |
331 | Translation: 331.0, Folding: 33.1 | 35,532 | UniprotID: P0A9B2 ECnumber: EC 1.2.1.12 |
FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. {ECO:0000269|PubMed:2659073}. |
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| b0997 | b0997 | Trimethylamine-N-oxide reductase 1 (TMAO reductase 1) (Trimethylamine oxidase 1) (EC 1.7.2.3) | Periplasm | R_TMAOR1pp_enzyme R_TMAOR2pp_enzyme |
R_TMAOR1pp R_TMAOR2pp |
848 | Secretion: 848.0, Translation: 848.0, Folding: 84.8 | 94,456 | UniprotID: P33225 ECnumber: EC 1.7.2.3 |
FUNCTION: Reduces trimethylamine-N-oxide (TMAO) into trimethylamine; an anaerobic reaction coupled to energy-yielding reactions. | |
| b0996 | b0996 | Cytochrome c-type protein TorC | Cell_inner_membrane | R_TMAOR1pp_enzyme R_TMAOR2pp_enzyme |
R_TMAOR1pp R_TMAOR2pp |
390 | Secretion: 390.0, Translation: 390.0, Folding: 39.0 | 43,607 | UniprotID: P33226 | FUNCTION: Part of the anaerobic respiratory chain of trimethylamine-N-oxide reductase TorA. Acts by transferring electrons from the membranous menaquinones to TorA. This transfer probably involves an electron transfer pathway from menaquinones to the N-terminal domain of TorC, then from the N-terminus to the C-terminus, and finally to TorA. TorC apocytochrome negatively autoregulates the torCAD operon probably by inhibiting the TorS kinase activity. |
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| b1484 | b1484 | Probable D,D-dipeptide transport ATP-binding protein DdpD | Cell_inner_membrane | R_ALAALAabcpp_enzyme | R_ALAALAabcpp | 328 | Secretion: 328.0, Translation: 328.0, Folding: 32.8 | 36,100 | UniprotID: P77268 | FUNCTION: Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport (PubMed:9097039). Probably responsible for energy coupling to the transport system. {ECO:0000305|PubMed:9097039}. | |
| b1485 | b1485 | Probable D,D-dipeptide transport system permease protein DdpC | Cell_inner_membrane | R_ALAALAabcpp_enzyme | R_ALAALAabcpp | 298 | Secretion: 298.0, Translation: 298.0, Folding: 29.8 | 31,971 | UniprotID: P77463 | FUNCTION: Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport. Probably responsible for the translocation of the substrate across the membrane. | |
| b1486 | b1486 | Probable D,D-dipeptide transport system permease protein DdpB | Cell_inner_membrane | R_ALAALAabcpp_enzyme | R_ALAALAabcpp | 340 | Secretion: 340.0, Translation: 340.0, Folding: 34.0 | 37,345 | UniprotID: P77308 | FUNCTION: Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport. Probably responsible for the translocation of the substrate across the membrane. | |
| b1487 | b1487 | Probable D,D-dipeptide-binding periplasmic protein DdpA | Periplasm | R_ALAALAabcpp_enzyme | R_ALAALAabcpp | 516 | Secretion: 516.0, Translation: 516.0, Folding: 51.6 | 57,641 | UniprotID: P76128 | FUNCTION: Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport. | |
| b0179 | b0179 | UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase (UDP-3-O-(3-OHC14)-GlcN N-acyltransferase) (EC 2.3.1.191) (Protein FirA) (Rifampicin resistance protein) (UDP-3-O-(3-hydroxytetradecanoyl)glucosamine N-acyltransferase) | Cytoplasm | R_U23GAAT_enzyme | R_U23GAAT | 341 | Translation: 341.0, Folding: 34.1 | 36,038 | UniprotID: P21645 ECnumber: EC 2.3.1.191 |
FUNCTION: Catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Prefers (3R)-3-hydroxytetradecanoyl-ACP over (3R)-3-hydroxyhexadecanoyl-ACP as the acyl donor in vitro, which is consistent with the structure of E.coli lipid A that contains over 95% (R)-3-hydroxytetradecanoate at the 2 and 2 positions. {ECO:0000269|PubMed:19655786, ECO:0000269|PubMed:8444173}. |
|
| b1483 | b1483 | Probable D,D-dipeptide transport ATP-binding protein DdpF | Cell_inner_membrane | R_ALAALAabcpp_enzyme | R_ALAALAabcpp | 308 | Secretion: 308.0, Translation: 308.0, Folding: 30.8 | 34,621 | UniprotID: P77622 | FUNCTION: Part of the ABC transporter complex DdpABCDF, which is probably involved in D,D-dipeptide transport (PubMed:9097039). Probably responsible for energy coupling to the transport system. {ECO:0000305|PubMed:9097039}. | |
| b0175 | b0175 | Phosphatidate cytidylyltransferase (EC 2.7.7.41) (CDP-DAG synthase) (CDP-DG synthase) (CDP-diacylglycerol synthase) (CDS) (CDP-diglyceride pyrophosphorylase) (CDP-diglyceride synthase) (CTP:phosphatidate cytidylyltransferase) | Cell_inner_membrane | R_DASYN120 R_DASYN140 R_DASYN141 R_DASYN160 R_DASYN161 R_DASYN180 R_DASYN181 |
285 | Secretion: 285.0, Translation: 285.0, Folding: 28.5 | 31,454 | UniprotID: P0ABG1 ECnumber: EC 2.7.7.41 |
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| b0174 | b0174 | Ditrans,polycis-undecaprenyl-diphosphate synthase ((2E,6E)-farnesyl-diphosphate specific) (EC 2.5.1.31) (Ditrans,polycis-undecaprenylcistransferase) (Undecaprenyl diphosphate synthase) (UDS) (Undecaprenyl pyrophosphate synthase) (UPP synthase) | Cytoplasm | R_UDCPDPS_enzyme | R_UDCPDPS | 253 | Translation: 253.0, Folding: 25.3 | 28,444 | UniprotID: P60472 ECnumber: EC 2.5.1.31 |
FUNCTION: Generates ditrans,octacis-undecaprenyl pyrophosphate (UPP) from isopentenyl pyrophosphate (IPP) and farnesyl diphosphate (FPP). UPP is the precursor of glycosyl carrier lipid in the biosynthesis of bacterial cell wall polysaccharide components such as peptidoglycan and lipopolysaccharide. {ECO:0000269|PubMed:12756244}. | |
| b0173 | b0173 | 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXP reductoisomerase) (EC 1.1.1.267) (1-deoxyxylulose-5-phosphate reductoisomerase) (2-C-methyl-D-erythritol 4-phosphate synthase) | Cytoplasm | R_DXPRIi_enzyme | R_DXPRIi | 398 | Translation: 398.0, Folding: 39.8 | 43,388 | UniprotID: P45568 ECnumber: EC 1.1.1.267 |
FUNCTION: Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP). | |
| b1489 | b1489 | Oxygen sensor protein DosP (EC 3.1.4.52) (Direct oxygen-sensing phosphodiesterase) (Direct oxygen sensor protein) (Ec DOS) (Heme-regulated cyclic di-GMP phosphodiesterase) | Cytoplasm | R_PDE1_enzyme R_PDE4_enzyme |
R_PDE1 R_PDE4 |
799 | Translation: 799.0, Folding: 79.9 | 90,260 | UniprotID: P76129 ECnumber: EC 3.1.4.52 |
FUNCTION: Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits. {ECO:0000269|PubMed:11970957, ECO:0000269|PubMed:15995192, ECO:0000269|PubMed:20553324}. |
|
| b0171 | b0171 | Uridylate kinase (UK) (EC 2.7.4.22) (Uridine monophosphate kinase) (UMP kinase) (UMPK) | Cytoplasm | R_UMPK_duplicate_2_enzyme | R_UMPK_duplicate_2 | 241 | Translation: 241.0, Folding: 24.1 | 25,970 | UniprotID: P0A7E9 ECnumber: EC 2.7.4.22 |
FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor. {ECO:0000269|PubMed:7711027}. | |
| b0425 | b0425 | 2-dehydropantoate 2-reductase (EC 1.1.1.169) (Ketopantoate reductase) (KPA reductase) (KPR) | Cytoplasm | R_DPR_enzyme | R_DPR | 303 | Translation: 303.0, Folding: 30.3 | 33,871 | UniprotID: P0A9J4 ECnumber: EC 1.1.1.169 |
FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. | |
| b0356 | b0356 | S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284) (Alcohol dehydrogenase class-3) (EC 1.1.1.1) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) | Cytoplasm | R_ALCD19_enzyme R_ALCD2x_duplicate_3_enzyme R_FALDH2_enzyme |
R_ALCD19 R_ALCD2x_duplicate_3 R_FALDH2 |
369 | Translation: 369.0, Folding: 36.9 | 39,359 | UniprotID: P25437 ECnumber: EC 1.1.1.284; 1.1.1.1; 1.1.1.- |
FUNCTION: Has high formaldehyde dehydrogenase activity in the presence of glutathione and catalyzes the oxidation of normal alcohols in a reaction that is not GSH-dependent. In addition, hemithiolacetals other than those formed from GSH, including omega-thiol fatty acids, also are substrates. {ECO:0000269|PubMed:1731906}. | |
| b0355 | b0355 | S-formylglutathione hydrolase FrmB (FGH) (EC 3.1.2.12) | Cytoplasm | R_SFGTHi_duplicate_2_enzyme | R_SFGTHi_duplicate_2 | 277 | Translation: 277.0, Folding: 27.7 | 31,424 | UniprotID: P51025 ECnumber: EC 3.1.2.12 |
FUNCTION: Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against two pNP-esters (pNP-acetate and pNP-propionate), alpha-naphthyl acetate and lactoylglutathione. {ECO:0000269|PubMed:16567800}. | |
| b0421 | b0421 | Farnesyl diphosphate synthase (FPP synthase) (EC 2.5.1.10) ((2E,6E)-farnesyl diphosphate synthase) (Geranyltranstransferase) | Cytoplasm | R_DMATT_enzyme R_GRTT_enzyme |
R_DMATT R_GRTT |
299 | Translation: 299.0, Folding: 29.9 | 32,160 | UniprotID: P22939 ECnumber: EC 2.5.1.10 |
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| b0352 | b0352 | 4-hydroxy-2-oxovalerate aldolase (HOA) (EC 4.1.3.39) (4-hydroxy-2-keto-pentanoic acid aldolase) (4-hydroxy-2-oxopentanoate aldolase) | Cytoplasm | R_HOPNTAL_enzyme | R_HOPNTAL | 337 | Translation: 337.0, Folding: 33.7 | 36,470 | UniprotID: P51020 ECnumber: EC 4.1.3.39 |
FUNCTION: Catalyzes the retro-aldol cleavage of 4-hydroxy-2-oxopentanoate to pyruvate and acetaldehyde. Is involved in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. {ECO:0000269|PubMed:9758851}. | |
| b0351 | b0351 | Acetaldehyde dehydrogenase (EC 1.2.1.10) (Acetaldehyde dehydrogenase [acetylating]) | Cytoplasm | R_ACALD_enzyme | R_ACALD | 316 | Translation: 316.0, Folding: 31.6 | 33,442 | UniprotID: P77580 ECnumber: EC 1.2.1.10 |
FUNCTION: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of 3-phenylpropanoate. Functions as a chaperone protein for folding of MhpE. {ECO:0000269|PubMed:16782065}. | |
| b0350 | b0350 | 2-keto-4-pentenoate hydratase (EC 4.2.1.80) (2-hydroxypentadienoic acid hydratase) | Cytoplasm | R_OP4ENH_enzyme | R_OP4ENH | 269 | Translation: 269.0, Folding: 26.9 | 28,890 | UniprotID: P77608 ECnumber: EC 4.2.1.80 |
FUNCTION: Catalyzes the conversion of 2-hydroxypentadienoic acid (enolic form of 2-oxopent-4-enoate) to 4-hydroxy-2-ketopentanoic acid. {ECO:0000269|PubMed:9492273}. | |
| b0429 | b0429 | Cytochrome bo(3) ubiquinol oxidase subunit 4 (Cytochrome o ubiquinol oxidase subunit 4) (Cytochrome o subunit 4) (Oxidase bo(3) subunit 4) (Ubiquinol oxidase chain D) (Ubiquinol oxidase polypeptide IV) (Ubiquinol oxidase subunit 4) | Cell_inner_membrane | R_CYTBO3_4pp_enzyme | R_CYTBO3_4pp | 109 | Secretion: 109.0, Translation: 109.0, Folding: 10.9 | 12,029 | UniprotID: P0ABJ6 | FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529, ECO:0000269|PubMed:6308657}. | |
| b0428 | b0428 | Protoheme IX farnesyltransferase (EC 2.5.1.-) (Heme B farnesyltransferase) (Heme O synthase) | Cell_inner_membrane | R_HEMEOS_enzyme | R_HEMEOS | 296 | Secretion: 296.0, Translation: 296.0, Folding: 29.6 | 32,248 | UniprotID: P0AEA5 ECnumber: EC 2.5.1.- |
FUNCTION: Converts heme B (protoheme IX) to heme O by substitution of the vinyl group on carbon 2 of heme B porphyrin ring with a hydroxyethyl farnesyl side group. {ECO:0000269|PubMed:1336371, ECO:0000269|PubMed:8253713}. | |
| b0194 | b0194 | Proline--tRNA ligase (EC 6.1.1.15) (Global RNA synthesis factor) (Prolyl-tRNA synthetase) (ProRS) | Cytoplasm | R_PROTRS_enzyme | R_PROTRS | 572 | Translation: 572.0, Folding: 57.2 | 63,693 | UniprotID: P16659 ECnumber: EC 6.1.1.15 |
FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as pretransfer editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated posttransfer editing and involves deacylation of mischarged Ala-tRNA(Pro). Misacylated Cys-tRNA(Pro) is not edited by ProRS, but instead may be edited in trans by YbaK. |
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| b0197 | b0197 | D-methionine-binding lipoprotein MetQ | Cell_inner_membrane | R_METDabcpp_enzyme R_METabcpp_enzyme |
R_METDabcpp R_METabcpp |
271 | Secretion: 271.0, Translation: 271.0, Folding: 27.1 | 29,432 | UniprotID: P28635 | FUNCTION: This protein is a component of a D-methionine permease, a binding protein-dependent, ATP-driven transport system. {ECO:0000269|PubMed:12169620}. | |
| b0199 | b0199 | Methionine import ATP-binding protein MetN (EC 3.6.3.-) | Cell_inner_membrane | R_METDabcpp_enzyme R_METabcpp_enzyme |
R_METDabcpp R_METabcpp |
343 | Secretion: 343.0, Translation: 343.0, Folding: 34.3 | 37,788 | UniprotID: P30750 ECnumber: EC 3.6.3.- |
FUNCTION: Part of the ABC transporter complex MetNIQ involved in methionine import. Responsible for energy coupling to the transport system (Probable). It has also been shown to be involved in formyl-L-methionine transport. {ECO:0000255|HAMAP-Rule:MF_01719, ECO:0000269|PubMed:12169620, ECO:0000269|PubMed:12819857, ECO:0000305}. | |
| b0198 | b0198 | D-methionine transport system permease protein MetI | Cell_inner_membrane | R_METDabcpp_enzyme R_METabcpp_enzyme |
R_METDabcpp R_METabcpp |
217 | Secretion: 217.0, Translation: 217.0, Folding: 21.7 | 23,256 | UniprotID: P31547 | FUNCTION: Part of the binding-protein-dependent transport system for D-methionine and the toxic methionine analog alpha-methyl-methionine. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:12169620}. | |
| b0957 | b0957 | Outer membrane protein A (Outer membrane protein II*) | Cell_outer_membrane | R_H2Otex_duplicate_5_enzyme | R_H2Otex_duplicate_5 | 346 | Secretion: 346.0, Translation: 346.0, Folding: 34.6 | 37,201 | UniprotID: P0A910 | FUNCTION: Required for the action of colicins K and L and for the stabilization of mating aggregates in conjugation. Serves as a receptor for a number of T-even like phages. Also acts as a porin with low permeability that allows slow penetration of small solutes. | |
| b0222 | b0222 | Phosphoheptose isomerase (EC 5.3.1.28) (Sedoheptulose 7-phosphate isomerase) | Cytoplasm | R_S7PI_enzyme | R_S7PI | 192 | Translation: 192.0, Folding: 19.2 | 20,815 | UniprotID: P63224 ECnumber: EC 5.3.1.28 |
FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000269|PubMed:11751812, ECO:0000269|PubMed:18056714}. | |
| b0221 | b0221 | Acyl-coenzyme A dehydrogenase (ACDH) (EC 1.3.99.-) | Cytoplasm | 814 | Translation: 814.0, Folding: 81.4 | 89,224 | UniprotID: Q47146 ECnumber: EC 1.3.99.- |
FUNCTION: Catalyzes the dehydrogenation of acyl-CoA. {ECO:0000269|PubMed:12057976}. | |||
| b3198 | b3198 | 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase KdsC (EC 3.1.3.45) (KDO 8-P phosphatase) | Cytoplasm | R_KDOPP_enzyme | R_KDOPP | 188 | Translation: 188.0, Folding: 18.8 | 19,997 | UniprotID: P0ABZ4 ECnumber: EC 3.1.3.45 |
FUNCTION: Involved in the biosynthesis of lipopolysaccharides (LPSs), but is not essential (PubMed:16765569). Catalyzes the hydrolysis of 3-deoxy-D-manno-octulosonate 8-phosphate (KDO 8-P) to 3-deoxy-D-manno-octulosonate (KDO) and inorganic phosphate (PubMed:12639950, PubMed:16765569). {ECO:0000269|PubMed:12639950, ECO:0000269|PubMed:16765569}. | |
| b3199 | b3199 | Lipopolysaccharide export system protein LptC | Cell_inner_membrane | 191 | Secretion: 191.0, Translation: 191.0, Folding: 19.1 | 21,703 | UniprotID: P0ADV9 | FUNCTION: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA. {ECO:0000255|HAMAP-Rule:MF_01915, ECO:0000269|PubMed:16765569, ECO:0000269|PubMed:18424520, ECO:0000269|PubMed:20720015, ECO:0000269|PubMed:21169485, ECO:0000269|PubMed:21195693}. |
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| b3628 | b3628 | Lipopolysaccharide 1,6-galactosyltransferase (EC 2.4.1.-) (UDP-D-galactose--(Glucosyl)lipopolysaccharide-alpha-1,3-D-galactosyltransferase) | Cytoplasm | R_GALT1_enzyme | R_GALT1 | 359 | Translation: 359.0, Folding: 35.9 | 40,826 | UniprotID: P27127 ECnumber: EC 2.4.1.- |
FUNCTION: Adds a galactose goup to a glucose group of LPS. | |
| b3629 | b3629 | Lipopolysaccharide core biosynthesis protein RfaS | Cytoplasm | R_RHAT1_enzyme | R_RHAT1 | 311 | Translation: 311.0, Folding: 31.1 | 36,730 | UniprotID: P27126 | ||
| b3626 | b3626 | Lipopolysaccharide 1,2-glucosyltransferase (EC 2.4.1.58) | Cytoplasm | R_GLCTR3_enzyme | R_GLCTR3 | 338 | Translation: 338.0, Folding: 33.8 | 39,040 | UniprotID: P27129 ECnumber: EC 2.4.1.58 |
FUNCTION: Adds the glucose(II) group on the galactose(I) group of LPS. {ECO:0000250|UniProtKB:P19817}. | |
| b3627 | b3627 | Lipopolysaccharide 1,3-galactosyltransferase (EC 2.4.1.44) (Lipopolysaccharide 3-alpha-galactosyltransferase) | Cytoplasm | R_GLCTR2_enzyme | R_GLCTR2 | 339 | Translation: 339.0, Folding: 33.9 | 39,423 | UniprotID: P27128 ECnumber: EC 2.4.1.44 |
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| b3196 | b3196 | Inner membrane protein YrbG | Cell_inner_membrane | R_CAt6pp_enzyme | R_CAt6pp | 325 | Secretion: 325.0, Translation: 325.0, Folding: 32.5 | 34,741 | UniprotID: P45394 | ||
| b3197 | b3197 | Arabinose 5-phosphate isomerase KdsD (API) (L-API) (EC 5.3.1.13) | Cytoplasm | R_A5PISO_enzyme | R_A5PISO | 328 | Translation: 328.0, Folding: 32.8 | 35,196 | UniprotID: P45395 ECnumber: EC 5.3.1.13 |
FUNCTION: Involved in the biosynthesis of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). KdsD is not essential in the KDO biosynthesis and can be substituted by GutQ. Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). {ECO:0000269|PubMed:12805358, ECO:0000269|PubMed:16199563, ECO:0000269|PubMed:16765569}. |
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| b3622 | b3622 | O-antigen ligase | Cell_inner_membrane | R_ECA4OALpp_enzyme R_O16A4Lpp_enzyme |
R_ECA4OALpp R_O16A4Lpp |
419 | Secretion: 419.0, Translation: 419.0, Folding: 41.9 | 46,878 | UniprotID: P27243 | FUNCTION: Adds the O-antigen on the glucose group of LPS. | |
| b3623 | b3623 | Lipopolysaccharide 1,2-N-acetylglucosaminetransferase (EC 2.4.1.56) | Cell_inner_membrane | R_HEPT4_enzyme | R_HEPT4 | 357 | Secretion: 357.0, Translation: 357.0, Folding: 35.7 | 41,729 | UniprotID: P27242 ECnumber: EC 2.4.1.56 |
FUNCTION: Adds the terminal N-acetyl-D-glucosamine group on the glucose(II) group of LPS. | |
| b3620 | b3620 | ADP-heptose--LPS heptosyltransferase 2 (EC 2.-.-.-) (ADP-heptose--LPS heptosyltransferase II) | Cytoplasm | R_HEPT2_enzyme | R_HEPT2 | 348 | Translation: 348.0, Folding: 34.8 | 39,042 | UniprotID: P37692 ECnumber: EC 2.-.-.- |
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| b3621 | b3621 | Lipopolysaccharide heptosyltransferase 1 (EC 2.-.-.-) | Cytoplasm | R_HEPT1_enzyme | R_HEPT1 | 319 | Translation: 319.0, Folding: 31.9 | 35,544 | UniprotID: P24173 ECnumber: EC 2.-.-.- |
FUNCTION: Heptose transfer to the lipopolysaccharide core. It transfers the innermost heptose to [4-P](3-deoxy-D-manno-octulosonic acid)2-IVA. | |
| b0766 | b0766 | Pyridoxal phosphate phosphatase YbhA (PLP phosphatase) (EC 3.1.3.74) | Cytoplasm | R_PDXPP_enzyme R_PYDXPP_duplicate_3_enzyme |
R_PDXPP R_PYDXPP_duplicate_3 |
272 | Translation: 272.0, Folding: 27.2 | 30,201 | UniprotID: P21829 ECnumber: EC 3.1.3.74 |
FUNCTION: Catalyzes the dephosphorylation of pyridoxal-phosphate (PLP). Can also hydrolyze erythrose-4-phosphate (Ery4P) and fructose-1,6-bis-phosphate (Fru1,6bisP). {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:16990279}. | |
| b0767 | b0767 | 6-phosphogluconolactonase (6-P-gluconolactonase) (Pgl) (EC 3.1.1.31) | Cytoplasm | R_PGL_enzyme | R_PGL | 331 | Translation: 331.0, Folding: 33.1 | 36,308 | UniprotID: P52697 ECnumber: EC 3.1.1.31 |
FUNCTION: Catalyzes the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate. {ECO:0000269|PubMed:15576773}. | |
| b3449 | b3449 | Glycerophosphodiester phosphodiesterase, cytoplasmic (Glycerophosphoryl diester phosphodiesterase, cytoplasmic) (EC 3.1.4.46) | Cytoplasm | R_GPDDA1_enzyme R_GPDDA2_enzyme R_GPDDA3_enzyme R_GPDDA4_enzyme R_GPDDA5_enzyme |
R_GPDDA1 R_GPDDA2 R_GPDDA3 R_GPDDA4 R_GPDDA5 |
247 | Translation: 247.0, Folding: 24.7 | 27,410 | UniprotID: P10908 ECnumber: EC 3.1.4.46 |
FUNCTION: Glycerophosphoryl diester phosphodiesterase hydrolyzes deacylated phospholipids to G3P and the corresponding alcohols. | |
| b2919 | b2919 | Methylmalonyl-CoA decarboxylase (MMCD) (EC 4.1.1.41) (Transcarboxylase) | Cytoplasm | R_MMCD_enzyme | R_MMCD | 261 | Translation: 261.0, Folding: 26.1 | 29,173 | UniprotID: P52045 ECnumber: EC 4.1.1.41 |
FUNCTION: Catalyzes the decarboxylation of methylmalonyl-CoA to propionyl-CoA. Could be part of a pathway that converts succinate to propionate. {ECO:0000269|PubMed:10769117}. | |
| b2917 | b2917 | Methylmalonyl-CoA mutase (MCM) (EC 5.4.99.2) | Cytoplasm | R_MMM_enzyme | R_MMM | 714 | Translation: 714.0, Folding: 71.4 | 77,871 | UniprotID: P27253 ECnumber: EC 5.4.99.2 |
FUNCTION: Catalyzes the interconversion of succinyl-CoA and methylmalonyl-CoA. Could be part of a pathway that converts succinate to propionate. {ECO:0000269|PubMed:10769117, ECO:0000269|PubMed:11955068}. | |
| b2914 | b2914 | Ribose-5-phosphate isomerase A (EC 5.3.1.6) (Phosphoriboisomerase A) (PRI) | Cytoplasm | R_RPI_enzyme | R_RPI | 219 | Translation: 219.0, Folding: 21.9 | 22,860 | UniprotID: P0A7Z0 ECnumber: EC 5.3.1.6 |
FUNCTION: Involved in the first step of the non-oxidative branch of the pentose phosphate pathway. It catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate. Can also act on D-ribose-5-diphosphate and D-ribose-5-triphosphate as substrate. {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:12517338, ECO:0000269|PubMed:4909663}. | |
| b2661 | b2661 | Succinate-semialdehyde dehydrogenase [NADP(+)] GabD (SSDH) (EC 1.2.1.79) | Cytoplasm | R_SSALy_enzyme | R_SSALy | 482 | Translation: 482.0, Folding: 48.2 | 51,720 | UniprotID: P25526 ECnumber: EC 1.2.1.79 |
FUNCTION: Catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. It appears to be important for nitrogen metabolism under N limitation conditions. {ECO:0000269|PubMed:20174634, ECO:0000269|PubMed:7011797}. | |
| b2912 | b2912 | 5-formyltetrahydrofolate cyclo-ligase (5-FCL) (EC 6.3.3.2) (5,10-methenyltetrahydrofolate synthetase) (MTHFS) | Cytoplasm | R_FOMETRi_enzyme | R_FOMETRi | 182 | Translation: 182.0, Folding: 18.2 | 21,105 | UniprotID: P0AC28 ECnumber: EC 6.3.3.2 |
FUNCTION: Involved in the removal of 5-formyltetrahydrofolate. In vitro, it is a potent inhibitor of various folate-dependent enzymes in the C1 metabolism network and in vivo it might function as a folate storage. 5-formyltetrahydrofolate is also used as an antifolate rescue agent in cancer chemotherapy. Catalyzes the irreversible ATP-dependent transformation of 5-formyltetrahydrofolate (5-CHO-THF) to form 5,10-methenyltetrahydrofolate (5,10-CH=THF). The reverse reaction is catalyzed by the serine hydroxymethyltransferase GlyA (SHMT). {ECO:0000269|PubMed:18519731, ECO:0000269|PubMed:20952389}. |
|
| b2663 | b2663 | GABA permease (4-amino butyrate transport carrier) (Gamma-aminobutyrate permease) | Cell_inner_membrane | R_ABUTt2pp_enzyme | R_ABUTt2pp | 466 | Secretion: 466.0, Translation: 466.0, Folding: 46.6 | 51,080 | UniprotID: P25527 | FUNCTION: Transporter for GABA. | |
| b2662 | b2662 | 4-aminobutyrate aminotransferase GabT (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (Glutamate:succinic semialdehyde transaminase) (L-AIBAT) | Cytoplasm | R_ABTA_enzyme | R_ABTA | 426 | Translation: 426.0, Folding: 42.6 | 45,775 | UniprotID: P22256 ECnumber: EC 2.6.1.19; 2.6.1.22 |
FUNCTION: Catalyzes the transfer of the amino group from gamma-aminobutyrate (GABA) to alpha-ketoglutarate (KG) to yield succinic semialdehyde (SSA). {ECO:0000269|PubMed:20639325}. | |
| b2261 | b2261 | o-succinylbenzoate synthase (OSB synthase) (OSBS) (EC 4.2.1.113) (4-(2-carboxyphenyl)-4-oxybutyric acid synthase) (o-succinylbenzoic acid synthase) | Cytoplasm | R_SUCBZS_enzyme | R_SUCBZS | 320 | Translation: 320.0, Folding: 32.0 | 35,477 | UniprotID: P29208 ECnumber: EC 4.2.1.113 |
FUNCTION: Converts 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 2-succinylbenzoate (OSB). {ECO:0000255|HAMAP-Rule:MF_00470, ECO:0000269|PubMed:10194342, ECO:0000269|PubMed:8335646}. | |
| b2260 | b2260 | 2-succinylbenzoate--CoA ligase (EC 6.2.1.26) (o-succinylbenzoyl-CoA synthetase) (OSB-CoA synthetase) | Cytoplasm | R_SUCBZL_enzyme | R_SUCBZL | 451 | Translation: 451.0, Folding: 45.1 | 50,185 | UniprotID: P37353 ECnumber: EC 6.2.1.26 |
FUNCTION: Converts 2-succinylbenzoate (OSB) to 2-succinylbenzoyl-CoA (OSB-CoA). {ECO:0000255|HAMAP-Rule:MF_00731, ECO:0000269|PubMed:8626063}. | |
| b2263 | b2263 | 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase (SHCHC synthase) (EC 4.2.99.20) | Cytoplasm | R_SHCHCS3_enzyme | R_SHCHCS3 | 252 | Translation: 252.0, Folding: 25.2 | 27,682 | UniprotID: P37355 ECnumber: EC 4.2.99.20 |
FUNCTION: Catalyzes a proton abstraction reaction that results in 2,5-elimination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC) and the formation of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC). Is also able to catalyze the hydrolysis of the thioester bond in palmitoyl-CoA in vitro. {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:18284213}. |
|
| b2262 | b2262 | 1,4-dihydroxy-2-naphthoyl-CoA synthase (DHNA-CoA synthase) (EC 4.1.3.36) | Cytoplasm | R_DHNCOAS_enzyme | R_DHNCOAS | 285 | Translation: 285.0, Folding: 28.5 | 31,633 | UniprotID: P0ABU0 ECnumber: EC 4.1.3.36 |
FUNCTION: Converts o-succinylbenzoyl-CoA (OSB-CoA) to 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA). {ECO:0000255|HAMAP-Rule:MF_01934, ECO:0000269|PubMed:1091286, ECO:0000269|PubMed:20643650, ECO:0000269|PubMed:21830810, ECO:0000269|PubMed:23658663}. | |
| b2265 | b2265 | Isochorismate synthase MenF (EC 5.4.4.2) (Isochorismate hydroxymutase) (Isochorismate mutase) | Cytoplasm | R_ICHORS_copy1_enzyme | R_ICHORS_copy1 | 431 | Translation: 431.0, Folding: 43.1 | 48,765 | UniprotID: P38051 ECnumber: EC 5.4.4.2 |
FUNCTION: Catalyzes the conversion of chorismate to isochorismate. Can also catalyze the reverse reaction, but with a lower efficiency. {ECO:0000269|PubMed:17240978, ECO:0000269|PubMed:8764478, ECO:0000269|PubMed:9150206, ECO:0000269|PubMed:9795253}. | |
| b2264 | b2264 | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (SEPHCHC synthase) (EC 2.2.1.9) (Menaquinone biosynthesis protein MenD) | Cytoplasm | R_SEPHCHCS_enzyme | R_SEPHCHCS | 556 | Translation: 556.0, Folding: 55.6 | 61,367 | UniprotID: P17109 ECnumber: EC 2.2.1.9 |
FUNCTION: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). {ECO:0000255|HAMAP-Rule:MF_01659, ECO:0000269|PubMed:17760421}. | |
| b3846 | b3846 | Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) | Cytoplasm | 729 | Translation: 729.0, Folding: 72.9 | 79,594 | UniprotID: P21177 ECnumber: EC 4.2.1.17; 5.1.2.3; 5.3.3.8; 1.1.1.35 |
FUNCTION: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate. {ECO:0000255|HAMAP-Rule:MF_01621, ECO:0000269|PubMed:12535077, ECO:0000269|PubMed:1748662, ECO:0000269|PubMed:368024, ECO:0000269|PubMed:8454629, ECO:0000269|PubMed:8755745}. |
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| b3844 | b3844 | NAD(P)H-flavin reductase (EC 1.16.1.3) (EC 1.5.1.41) (Aquacobalamin reductase) (FMN reductase) (Ferrisiderophore reductase C) (NAD(P)H:flavin oxidoreductase) (Riboflavin reductase [NAD(P)H]) | Cytoplasm | R_FADRx R_FE3Ri R_FLVR R_FLVRx R_FMNRx_duplicate_2 R_FMNRx2_duplicate_2 |
233 | Translation: 233.0, Folding: 23.3 | 26,242 | UniprotID: P0AEN1 ECnumber: EC 1.16.1.3; 1.5.1.41 |
FUNCTION: Catalyzes the reduction of soluble flavins by reduced pyridine nucleotides. Seems to reduce the complexed Fe(3+) iron of siderophores to Fe(2+), thus releasing it from the chelator. | ||
| b3845 | b3845 | 3-ketoacyl-CoA thiolase FadA (EC 2.3.1.16) (Acetyl-CoA acyltransferase) (Beta-ketothiolase) (Fatty acid oxidation complex subunit beta) | Cytoplasm | 387 | Translation: 387.0, Folding: 38.7 | 40,876 | UniprotID: P21151 ECnumber: EC 2.3.1.16 |
FUNCTION: Catalyzes the final step of fatty acid oxidation in which acetyl-CoA is released and the CoA ester of a fatty acid two carbons shorter is formed. Involved in the aerobic and anaerobic degradation of long-chain fatty acids. {ECO:0000269|PubMed:12535077, ECO:0000269|PubMed:368024}. | |||
| b3843 | b3843 | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase (EC 4.1.1.98) (Polyprenyl p-hydroxybenzoate decarboxylase) | Cell_inner_membrane | R_OPHBDC_enzyme | R_OPHBDC | 497 | Secretion: 497.0, Translation: 497.0, Folding: 49.7 | 55,604 | UniprotID: P0AAB4 ECnumber: EC 4.1.1.98 |
FUNCTION: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01636, ECO:0000269|PubMed:782527}. | |
| b3428 | b3428 | Glycogen phosphorylase (EC 2.4.1.1) | Cytoplasm | R_GLCP_enzyme R_GLCP2_duplicate_2_enzyme |
R_GLCP R_GLCP2_duplicate_2 |
815 | Translation: 815.0, Folding: 81.5 | 93,173 | UniprotID: P0AC86 ECnumber: EC 2.4.1.1 |
FUNCTION: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties. | |
| b2867 | b2867 | Putative xanthine dehydrogenase FAD-binding subunit XdhB (EC 1.17.1.4) | Cytoplasm | R_HXAND_enzyme R_XAND_enzyme |
R_HXAND R_XAND |
292 | Translation: 292.0, Folding: 29.2 | 31,557 | UniprotID: Q46800 ECnumber: EC 1.17.1.4 |
FUNCTION: Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism). | |
| b2866 | b2866 | Putative xanthine dehydrogenase molybdenum-binding subunit XdhA (EC 1.17.1.4) | Cytoplasm | R_HXAND_enzyme R_XAND_enzyme |
R_HXAND R_XAND |
752 | Translation: 752.0, Folding: 75.2 | 81,321 | UniprotID: Q46799 ECnumber: EC 1.17.1.4 |
FUNCTION: Presumed to be a dehydrogenase, but possibly an oxidase. Participates in limited purine salvage (requires aspartate) but does not support aerobic growth on purines as the sole carbon source (purine catabolism). Deletion results in increased adenine sensitivity, suggesting that this protein contributes to the conversion of adenine to guanine nucleotides during purine salvage. {ECO:0000269|PubMed:10986234}. |
|
| b3429 | b3429 | Glycogen synthase (EC 2.4.1.21) (Starch [bacterial glycogen] synthase) | Cytoplasm | R_GLCS1_enzyme | R_GLCS1 | 477 | Translation: 477.0, Folding: 47.7 | 52,822 | UniprotID: P0A6U8 ECnumber: EC 2.4.1.21 |
FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. | |
| b3831 | b3831 | Uridine phosphorylase (UPase) (UrdPase) (EC 2.4.2.3) | Cytoplasm | R_PYNP2r_enzyme | R_PYNP2r | 253 | Translation: 253.0, Folding: 25.3 | 27,159 | UniprotID: P12758 ECnumber: EC 2.4.2.3 |
FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-phosphate. The produced molecules are then utilized as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis. | |
| b3994 | b3994 | Phosphomethylpyrimidine synthase (EC 4.1.99.17) (Hydroxymethylpyrimidine phosphate synthase) (HMP-P synthase) (HMP-phosphate synthase) (HMPP synthase) (Thiamine biosynthesis protein ThiC) | Cytoplasm | R_AMPMS2_enzyme | R_AMPMS2 | 631 | Translation: 631.0, Folding: 63.1 | 70,850 | UniprotID: P30136 ECnumber: EC 4.1.99.17 |
FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. {ECO:0000305|PubMed:15292217, ECO:0000305|PubMed:15326535}. | |
| b3996 | b3996 | NADH pyrophosphatase (EC 3.6.1.22) | Cytoplasm | R_NADDP_enzyme | R_NADDP | 257 | Translation: 257.0, Folding: 25.7 | 29,689 | UniprotID: P32664 ECnumber: EC 3.6.1.22 |
FUNCTION: Catalyzes the hydrolysis of a broad range of dinucleotide pyrophosphates, but uniquely prefers the reduced form of NADH. {ECO:0000269|PubMed:7829480}. | |
| b3997 | b3997 | Uroporphyrinogen decarboxylase (UPD) (URO-D) (EC 4.1.1.37) | Cytoplasm | R_UPPDC1_enzyme | R_UPPDC1 | 354 | Translation: 354.0, Folding: 35.4 | 39,248 | UniprotID: P29680 ECnumber: EC 4.1.1.37 |
FUNCTION: Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III. {ECO:0000255|HAMAP-Rule:MF_00218}. | |
| b3990 | b3990 | 2-iminoacetate synthase (EC 4.1.99.19) (Dehydroglycine synthase) (Tyrosine lyase) | Cytoplasm | R_THZPSN3_enzyme | R_THZPSN3 | 377 | Translation: 377.0, Folding: 37.7 | 43,320 | UniprotID: P30140 ECnumber: EC 4.1.99.19 |
FUNCTION: Catalyzes the radical-mediated cleavage of tyrosine to 2-iminoacetate and 4-cresol. {ECO:0000269|PubMed:17403671, ECO:0000269|PubMed:17969213}. | |
| b3991 | b3991 | Thiazole synthase (EC 2.8.1.10) | Cytoplasm | R_TYRL_enzyme | R_TYRL | 256 | Translation: 256.0, Folding: 25.6 | 26,896 | UniprotID: P30139 ECnumber: EC 2.8.1.10 |
FUNCTION: Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S. {ECO:0000269|PubMed:12650933}. | |
| b3992 | b3992 | Sulfur carrier protein ThiS adenylyltransferase (EC 2.7.7.73) | Cytoplasm | R_THZPSN3_enzyme | R_THZPSN3 | 251 | Translation: 251.0, Folding: 25.1 | 26,970 | UniprotID: P30138 ECnumber: EC 2.7.7.73 |
FUNCTION: Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS. | |
| b3993 | b3993 | Thiamine-phosphate synthase (TP synthase) (TPS) (EC 2.5.1.3) (Thiamine-phosphate pyrophosphorylase) (TMP pyrophosphorylase) (TMP-PPase) | Cytoplasm | R_TMPPP_enzyme | R_TMPPP | 211 | Translation: 211.0, Folding: 21.1 | 23,015 | UniprotID: P30137 ECnumber: EC 2.5.1.3 |
FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). {ECO:0000269|PubMed:15292217, ECO:0000269|Ref.5}. | |
| b2467 | b2467 | GDP-mannose pyrophosphatase NudK (EC 3.6.1.-) | Cytoplasm | R_GDPMNP_enzyme | R_GDPMNP | 191 | Translation: 191.0, Folding: 19.1 | 21,749 | UniprotID: P37128 ECnumber: EC 3.6.1.- |
FUNCTION: Catalyzes the hydrolysis of GDP-mannose. Can also use other substrates, catalyzing the hydrolysis of the pyrophosphate bond, releasing a nucleoside monophosphate and a phosphorylated moiety, depending on the substrate. {ECO:0000269|PubMed:16766526}. | |
| b2465 | b2465 | Transketolase 2 (TK 2) (EC 2.2.1.1) | Cytoplasm | R_TKT1_duplicate_2_enzyme R_TKT2_duplicate_2_enzyme |
R_TKT1_duplicate_2 R_TKT2_duplicate_2 |
667 | Translation: 667.0, Folding: 66.7 | 73,043 | UniprotID: P33570 ECnumber: EC 2.2.1.1 |
FUNCTION: Catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate. Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate (By similarity). {ECO:0000250}. | |
| b2464 | b2464 | Transaldolase A (EC 2.2.1.2) | Cytoplasm | R_TALA_enzyme | R_TALA | 316 | Translation: 316.0, Folding: 31.6 | 35,659 | UniprotID: P0A867 ECnumber: EC 2.2.1.2 |
FUNCTION: Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. | |
| b2463 | b2463 | NADP-dependent malic enzyme (NADP-ME) (EC 1.1.1.40) | Cytoplasm | R_ME2_enzyme | R_ME2 | 759 | Translation: 759.0, Folding: 75.9 | 82,417 | UniprotID: P76558 ECnumber: EC 1.1.1.40 |
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| b2715 | b2715 | PTS system arbutin- | cellobiose- | and salicin-specific EIIBC component (EIIBC-Asc) (EII-Asc) [Includes: Arbutin- | cellobiose- | and salicin-specific phosphotransferase enzyme IIB component (EC 2.7.1.-) (PTS system arbutin- | cellobiose- | and salicin-specific EIIB component); Arbutin | cellobiose | and salicin permease IIC component (PTS system arbutin- | cellobiose- |
| b2711 | b2711 | Nitric oxide reductase FlRd-NAD(+) reductase (EC 1.18.1.-) (Flavorubredoxin reductase) (FlRd-reductase) (FlavoRb reductase) | Cytoplasm | R_NHFRBO_enzyme | R_NHFRBO | 377 | Translation: 377.0, Folding: 37.7 | 41,404 | UniprotID: P37596 ECnumber: EC 1.18.1.- |
FUNCTION: One of at least two accessory proteins for anaerobic nitric oxide (NO) reductase. Reduces the rubredoxin moiety of NO reductase. | |
| b2710 | b2710 | Anaerobic nitric oxide reductase flavorubredoxin (FlRd) (FlavoRb) | Cytoplasm | R_NHFRBO_enzyme | R_NHFRBO | 479 | Translation: 479.0, Folding: 47.9 | 54,234 | UniprotID: Q46877 | FUNCTION: Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the reductase at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase. |
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| b2719 | b2719 | Formate hydrogenlyase subunit 7 (FHL subunit 7) (Hydrogenase-3 component G) | Cytoplasm | R_FHL_duplicate_2_enzyme R_HYD1pp_duplicate_3_enzyme |
R_FHL_duplicate_2 R_HYD1pp_duplicate_3 |
255 | Translation: 255.0, Folding: 25.5 | 27,999 | UniprotID: P16433 | ||
| b2523 | b2523 | Peptidase B (EC 3.4.11.23) (Aminopeptidase B) | Cytoplasm | R_AMPTASECG_duplicate_4_enzyme R_AMPTASEPG_enzyme |
R_AMPTASECG_duplicate_4 R_AMPTASEPG |
427 | Translation: 427.0, Folding: 42.7 | 46,180 | UniprotID: P37095 ECnumber: EC 3.4.11.23 |
FUNCTION: Probably plays an important role in intracellular peptide degradation (PubMed:20067529). {ECO:0000255|HAMAP-Rule:MF_00504, ECO:0000305|PubMed:20067529}. | |
| b2485 | b2485 | Hydrogenase-4 component E (EC 1.-.-.-) | Cell_inner_membrane | R_FHL_enzyme | R_FHL | 216 | Secretion: 216.0, Translation: 216.0, Folding: 21.6 | 23,361 | UniprotID: P0AEW1 ECnumber: EC 1.-.-.- |
FUNCTION: Possible component of hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b2484 | b2484 | Hydrogenase-4 component D (EC 1.-.-.-) | Cell_inner_membrane | R_FHL_enzyme | R_FHL | 479 | Secretion: 479.0, Translation: 479.0, Folding: 47.9 | 51,755 | UniprotID: P77416 ECnumber: EC 1.-.-.- |
FUNCTION: Possible component of hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b2487 | b2487 | Hydrogenase-4 component G (EC 1.-.-.-) | Cytoplasm | R_FHL_enzyme | R_FHL | 555 | Translation: 555.0, Folding: 55.5 | 63,383 | UniprotID: P77329 ECnumber: EC 1.-.-.- |
FUNCTION: Possible component of hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b2486 | b2486 | Hydrogenase-4 component F (EC 1.-.-.-) | Cell_inner_membrane | R_FHL_enzyme | R_FHL | 526 | Secretion: 526.0, Translation: 526.0, Folding: 52.6 | 56,767 | UniprotID: P77437 ECnumber: EC 1.-.-.- |
FUNCTION: Possible component of hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b2481 | b2481 | Hydrogenase-4 component A (EC 1.-.-.-) | Cytoplasm | R_FHL_enzyme | R_FHL | 205 | Translation: 205.0, Folding: 20.5 | 22,154 | UniprotID: P23481 ECnumber: EC 1.-.-.- |
FUNCTION: Probable electron transfer protein for hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b2480 | b2480 | Peroxiredoxin Bcp (EC 1.11.1.15) (Bacterioferritin comigratory protein) (Thioredoxin peroxidase) | Cytoplasm | R_THIORDXi_enzyme R_THIORDXi_duplicate_2_enzyme |
R_THIORDXi R_THIORDXi_duplicate_2 |
156 | Translation: 156.0, Folding: 15.6 | 17,634 | UniprotID: P0AE52 ECnumber: EC 1.11.1.15 |
FUNCTION: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. {ECO:0000269|PubMed:21910476}. | |
| b2483 | b2483 | Hydrogenase-4 component C (EC 1.-.-.-) | Cell_inner_membrane | R_FHL_enzyme | R_FHL | 315 | Secretion: 315.0, Translation: 315.0, Folding: 31.5 | 34,359 | UniprotID: P77858 ECnumber: EC 1.-.-.- |
FUNCTION: Possible component of hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b2482 | b2482 | Hydrogenase-4 component B (EC 1.-.-.-) | Cell_inner_membrane | R_FHL_enzyme | R_FHL | 672 | Secretion: 672.0, Translation: 672.0, Folding: 67.2 | 72,583 | UniprotID: P23482 ECnumber: EC 1.-.-.- |
FUNCTION: Possible component of hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b2489 | b2489 | Hydrogenase-4 component I (EC 1.-.-.-) | Cytoplasm | R_FHL_enzyme | R_FHL | 252 | Translation: 252.0, Folding: 25.2 | 28,101 | UniprotID: P77668 ECnumber: EC 1.-.-.- |
FUNCTION: Possible component of hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b2488 | b2488 | Hydrogenase-4 component H | Cytoplasm | R_FHL_enzyme | R_FHL | 181 | Translation: 181.0, Folding: 18.1 | 20,159 | UniprotID: P77423 | FUNCTION: Probable electron transfer protein for hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b1015 | b1015 | Sodium/proline symporter (Proline permease) (Propionate transporter) | Cell_inner_membrane | R_PPAt4pp_enzyme R_PROt4pp_enzyme |
R_PPAt4pp R_PROt4pp |
502 | Secretion: 502.0, Translation: 502.0, Folding: 50.2 | 54,344 | UniprotID: P07117 | FUNCTION: Catalyzes the sodium-dependent uptake of extracellular L-proline. This protein is also capable of using lithium as the transport cation. Also catalyzes the uptake of propionate. {ECO:0000269|PubMed:17088549}. | |
| b1014 | b1014 | Bifunctional protein PutA [Includes: Proline dehydrogenase (EC 1.5.5.2) (Proline oxidase); Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (EC 1.2.1.88) (L-glutamate gamma-semialdehyde dehydrogenase) | Cytoplasm | R_P5CD_enzyme R_PROD2_enzyme |
R_P5CD R_PROD2 |
1320 | Translation: 1320.0, Folding: 132.0 | 143,815 | UniprotID: P09546 ECnumber: EC 1.5.5.2; 1.2.1.88 |
FUNCTION: Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon. | |
| b1012 | b1012 | Pyrimidine monooxygenase RutA (EC 1.14.99.46) | Cytoplasm | R_PYROX_enzyme | R_PYROX | 382 | Translation: 382.0, Folding: 38.2 | 42,219 | UniprotID: P75898 ECnumber: EC 1.14.99.46 |
FUNCTION: Catalyzes the pyrimidine ring opening between N-3 and C-4 by an unusual flavin hydroperoxide-catalyzed mechanism to yield ureidoacrylate peracid. It cleaves pyrmidine rings directly by adding oxygen atoms, making a toxic ureidoacrylate peracid product which can be spontaneously reduced to ureidoacrylate. Requires the flavin reductase RutF to regenerate FMN in vivo. RutF can be substituted by Fre in vitro. {ECO:0000269|PubMed:16540542, ECO:0000269|PubMed:20400551}. |
|
| b1011 | b1011 | Peroxyureidoacrylate/ureidoacrylate amidohydrolase RutB (EC 3.5.1.110) (Ureidoacrylate amidohydrolase) | Cytoplasm | R_URACPAH_enzyme | R_URACPAH | 230 | Translation: 230.0, Folding: 23.0 | 25,209 | UniprotID: P75897 ECnumber: EC 3.5.1.110 |
FUNCTION: In vivo, quickly hydrolyzes the ureidoacrylate peracid to avoid toxicity, but can also hydrolyzes ureidoacrylate that is formed spontaneously from ureidoacrylate peracid. One of the products of hydrolysis, carbamate, hydrolyzes spontaneously, thereby releasing one of the pyrimidine rings nitrogen atoms as ammonia and one of its carbons as CO2. {ECO:0000269|PubMed:16540542, ECO:0000269|PubMed:20400551}. |
|
| b1010 | b1010 | Putative aminoacrylate peracid reductase RutC (EC 1.-.-.-) | Cytoplasm | R_POAACR_enzyme | R_POAACR | 128 | Translation: 128.0, Folding: 12.8 | 13,763 | UniprotID: P0AFQ5 ECnumber: EC 1.-.-.- |
FUNCTION: May reduce aminoacrylate peracid to aminoacrylate. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. {ECO:0000269|PubMed:16540542}. | |
| b4227 | b4227 | ABC transporter periplasmic-binding protein YtfQ | Periplasm | R_GALabcpp_duplicate_2_enzyme R_RIBabcpp_duplicate_2_enzyme |
R_GALabcpp_duplicate_2 R_RIBabcpp_duplicate_2 |
318 | Secretion: 318.0, Translation: 318.0, Folding: 31.8 | 34,345 | UniprotID: P39325 | ||
| b4226 | b4226 | Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) | Cytoplasm | R_PPA_enzyme | R_PPA | 176 | Translation: 176.0, Folding: 17.6 | 19,704 | UniprotID: P0A7A9 ECnumber: EC 3.6.1.1 |
FUNCTION: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. {ECO:0000255|HAMAP-Rule:MF_00209}. | |
| b0764 | b0764 | Molybdenum transport system permease protein ModB | Cell_inner_membrane | R_MOBDabcpp_duplicate_2_enzyme R_SULabcpp_enzyme R_TUNGSabcpp_enzyme |
R_MOBDabcpp_duplicate_2 R_SULabcpp R_TUNGSabcpp |
229 | Secretion: 229.0, Translation: 229.0, Folding: 22.9 | 24,939 | UniprotID: P0AF01 | FUNCTION: Part of the binding-protein-dependent transport system for molybdenum; probably responsible for the translocation of the substrate across the membrane. | |
| b0765 | b0765 | Molybdenum import ATP-binding protein ModC (EC 3.6.3.29) | Cell_inner_membrane | R_MOBDabcpp_duplicate_2_enzyme R_SULabcpp_enzyme R_TUNGSabcpp_enzyme |
R_MOBDabcpp_duplicate_2 R_SULabcpp R_TUNGSabcpp |
352 | Secretion: 352.0, Translation: 352.0, Folding: 35.2 | 39,102 | UniprotID: P09833 ECnumber: EC 3.6.3.29 |
FUNCTION: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01705}. | |
| b0763 | b0763 | Molybdate-binding periplasmic protein | Periplasm | R_MOBDabcpp_duplicate_2_enzyme R_SULabcpp_enzyme R_TUNGSabcpp_enzyme |
R_MOBDabcpp_duplicate_2 R_SULabcpp R_TUNGSabcpp |
257 | Secretion: 257.0, Translation: 257.0, Folding: 25.7 | 27,364 | UniprotID: P37329 | FUNCTION: Involved in the transport of molybdenum into the cell. Binds molybdate with high specificity and affinity. | |
| b1640 | b1640 | Anhydro-N-acetylmuramic acid kinase (EC 2.7.1.170) (AnhMurNAc kinase) | Cytoplasm | R_ANHMK_enzyme | R_ANHMK | 369 | Translation: 369.0, Folding: 36.9 | 39,496 | UniprotID: P77570 ECnumber: EC 2.7.1.170 |
FUNCTION: Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling. {ECO:0000269|PubMed:15901686, ECO:0000269|PubMed:16452451}. |
|
| b1901 | b1901 | L-arabinose-binding periplasmic protein (ABP) | Periplasm | R_ARBabcpp_enzyme | R_ARBabcpp | 329 | Secretion: 329.0, Translation: 329.0, Folding: 32.9 | 35,541 | UniprotID: P02924 | FUNCTION: Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction). | |
| b1900 | b1900 | Arabinose import ATP-binding protein AraG (EC 3.6.3.17) | Cell_inner_membrane | R_ARBabcpp_enzyme | R_ARBabcpp | 504 | Secretion: 504.0, Translation: 504.0, Folding: 50.4 | 55,018 | UniprotID: P0AAF3 ECnumber: EC 3.6.3.17 |
FUNCTION: Part of the ABC transporter complex AraFGH involved in arabinose import. Responsible for energy coupling to the transport system (Probable). {ECO:0000305|PubMed:2656640, ECO:0000305|PubMed:7028715}. | |
| b1907 | b1907 | Tyrosine-specific transport protein (Tyrosine permease) | Cell_inner_membrane | R_TYRt2rpp_duplicate_3_enzyme | R_TYRt2rpp_duplicate_3 | 403 | Secretion: 403.0, Translation: 403.0, Folding: 40.3 | 42,819 | UniprotID: P0AAD4 | FUNCTION: Involved in transporting tyrosine across the cytoplasmic membrane. | |
| b0508 | b0508 | Hydroxypyruvate isomerase (EC 5.3.1.22) (Glyoxylate-induced protein) | Cytoplasm | R_HPYRI_enzyme | R_HPYRI | 258 | Translation: 258.0, Folding: 25.8 | 29,377 | UniprotID: P30147 ECnumber: EC 5.3.1.22 |
FUNCTION: Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). Does not catalyze the isomerization of D-fructose to D-glucose or that of D-xylulose to D-xylose. Also does not catalyze racemization of serine, alanine, glycerate or lactate. {ECO:0000269|PubMed:10561547}. | |
| b0509 | b0509 | 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60) (Tartronate semialdehyde reductase) (TSAR) | Cytoplasm | R_TRSARr_enzyme | R_TRSARr | 292 | Translation: 292.0, Folding: 29.2 | 30,801 | UniprotID: P77161 ECnumber: EC 1.1.1.60 |
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| b1589 | b1589 | Probable anaerobic dimethyl sulfoxide reductase chain YnfG (DMSO reductase iron-sulfur subunit YnfG) | Cytoplasm | R_DMSOR1_enzyme R_SELR_enzyme R_TMAOR1_duplicate_2_enzyme |
R_DMSOR1 R_SELR R_TMAOR1_duplicate_2 |
205 | Translation: 205.0, Folding: 20.5 | 22,752 | UniprotID: P0AAJ1 | FUNCTION: Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. | |
| b1588 | b1588 | Probable dimethyl sulfoxide reductase chain YnfF (DMSO reductase) (EC 1.8.99.-) | Cell_inner_membrane | R_DMSOR1_enzyme R_SELR_enzyme R_TMAOR1_duplicate_2_enzyme |
R_DMSOR1 R_SELR R_TMAOR1_duplicate_2 |
807 | Secretion: 807.0, Translation: 807.0, Folding: 80.7 | 89,987 | UniprotID: P77783 ECnumber: EC 1.8.99.- |
FUNCTION: Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. {ECO:0000250}. | |
| b1584 | b1584 | Spermidine N(1)-acetyltransferase (SAT) (EC 2.3.1.57) (Spermidine/spermine N(1)-acetyltransferase) (SSAT) | Cytoplasm | R_SPMDAT1_enzyme R_SPMDAT2_enzyme |
R_SPMDAT1 R_SPMDAT2 |
186 | Translation: 186.0, Folding: 18.6 | 21,887 | UniprotID: P0A951 ECnumber: EC 2.3.1.57 |
FUNCTION: Involved in the protection against polyamine toxicity by regulating their concentration (PubMed:7642535, PubMed:10986239). Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to the primary amino groups of spermidine to yield N(1)- and N(8)-acetylspermidine (PubMed:8077207, PubMed:7052085, PubMed:6297970). It can also use polyamines such as spermine, but not putrescine (PubMed:7052085). {ECO:0000269|PubMed:10986239, ECO:0000269|PubMed:6297970, ECO:0000269|PubMed:7052085, ECO:0000269|PubMed:7642535, ECO:0000269|PubMed:8077207}. |
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| b1587 | b1587 | Putative dimethyl sulfoxide reductase chain YnfE (DMSO reductase) (EC 1.8.99.-) | Cell_inner_membrane | R_DMSOR1_enzyme R_SELR_enzyme R_TMAOR1_duplicate_2_enzyme |
R_DMSOR1 R_SELR R_TMAOR1_duplicate_2 |
808 | Secretion: 808.0, Translation: 808.0, Folding: 80.8 | 89,780 | UniprotID: P77374 ECnumber: EC 1.8.99.- |
FUNCTION: Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. {ECO:0000250}. | |
| b4087 | b4087 | D-allose import ATP-binding protein AlsA (EC 3.6.3.17) | Cell_inner_membrane | R_ALLabcpp_enzyme R_RIBabcpp_duplicate_3_enzyme |
R_ALLabcpp R_RIBabcpp_duplicate_3 |
510 | Secretion: 510.0, Translation: 510.0, Folding: 51.0 | 56,745 | UniprotID: P32721 ECnumber: EC 3.6.3.17 |
FUNCTION: Part of the ABC transporter complex AlsBAC involved in D-allose import. Probably responsible for energy coupling to the transport system. {ECO:0000269|PubMed:9401019}. | |
| b4086 | b4086 | D-allose transport system permease protein AlsC | Cell_inner_membrane | R_ALLabcpp_enzyme R_RIBabcpp_duplicate_3_enzyme |
R_ALLabcpp R_RIBabcpp_duplicate_3 |
326 | Secretion: 326.0, Translation: 326.0, Folding: 32.6 | 34,316 | UniprotID: P32720 | FUNCTION: Part of the binding-protein-dependent transport system AlsBAC for D-allose; probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:9401019}. | |
| b4085 | b4085 | D-allulose-6-phosphate 3-epimerase (EC 5.1.3.-) | Cytoplasm | R_ALLULPE_enzyme | R_ALLULPE | 231 | Translation: 231.0, Folding: 23.1 | 26,109 | UniprotID: P32719 ECnumber: EC 5.1.3.- |
FUNCTION: Catalyzes the reversible epimerization of D-allulose 6-phosphate to D-fructose 6-phosphate. Can also catalyze with lower efficiency the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate. {ECO:0000269|PubMed:18700786, ECO:0000269|PubMed:9401019}. | |
| b0505 | b0505 | Ureidoglycolate lyase (EC 4.3.2.3) (Ureidoglycolatase) (Ureidoglycolate hydrolase) | Cytoplasm | R_UGLYCH_enzyme | R_UGLYCH | 160 | Translation: 160.0, Folding: 16.0 | 18,170 | UniprotID: P77731 ECnumber: EC 4.3.2.3 |
FUNCTION: Catalyzes the catabolism of the allantoin degradation intermediate (S)-ureidoglycolate, generating urea and glyoxylate. Involved in the anaerobic utilization of allantoin as sole nitrogen source. Reinforces the induction of genes involved in the degradation of allantoin and glyoxylate by producing glyoxylate. {ECO:0000255|HAMAP-Rule:MF_00616, ECO:0000269|PubMed:10601204, ECO:0000269|PubMed:24107613}. |
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| b0698 | b0698 | Potassium-transporting ATPase potassium-binding subunit (ATP phosphohydrolase [potassium-transporting] A chain) (Potassium-binding and translocating subunit A) (Potassium-translocating ATPase A chain) | Cell_inner_membrane | R_Kabcpp_enzyme R_Kabcpp_duplicate_2_enzyme |
R_Kabcpp R_Kabcpp_duplicate_2 |
557 | Secretion: 557.0, Translation: 557.0, Folding: 55.7 | 59,189 | UniprotID: P03959 | FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:2849541, PubMed:8499455, PubMed:23930894). This subunit binds and transports the potassium across the cytoplasmic membrane (PubMed:7896809). {ECO:0000269|PubMed:23930894, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:7896809, ECO:0000269|PubMed:8499455}. |
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| b1740 | b1740 | NH(3)-dependent NAD(+) synthetase (EC 6.3.1.5) (Nicotinamide adenine dinucleotide synthetase) (NADS) (Nitrogen regulatory protein) | Cytoplasm | R_NADS1_enzyme | R_NADS1 | 275 | Translation: 275.0, Folding: 27.5 | 30,637 | UniprotID: P18843 ECnumber: EC 6.3.1.5 |
FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000269|PubMed:8195100}. | |
| b1747 | b1747 | Arginine N-succinyltransferase (AST) (EC 2.3.1.109) (AOST) | Cytoplasm | R_AST_enzyme | R_AST | 344 | Translation: 344.0, Folding: 34.4 | 38,456 | UniprotID: P0AE37 ECnumber: EC 2.3.1.109 |
FUNCTION: Catalyzes the transfer of succinyl-CoA to arginine to produce N(2)-succinylarginine. {ECO:0000269|PubMed:9696779}. | |
| b1746 | b1746 | N-succinylglutamate 5-semialdehyde dehydrogenase (EC 1.2.1.71) (Succinylglutamic semialdehyde dehydrogenase) (SGSD) | Cytoplasm | R_SGSAD_enzyme | R_SGSAD | 492 | Translation: 492.0, Folding: 49.2 | 53,026 | UniprotID: P76217 ECnumber: EC 1.2.1.71 |
FUNCTION: Catalyzes the NAD-dependent reduction of succinylglutamate semialdehyde into succinylglutamate. Also shows activity with decanal or succinic semialdehyde as the electron donor and NAD as the electron acceptor. No activity is detected with NADP as the electron acceptor. Therefore, is an aldehyde dehydrogenase with broad substrate specificity. {ECO:0000269|PubMed:15808744}. | |
| b1745 | b1745 | N-succinylarginine dihydrolase (EC 3.5.3.23) | Cytoplasm | R_SADH_enzyme | R_SADH | 447 | Translation: 447.0, Folding: 44.7 | 49,299 | UniprotID: P76216 ECnumber: EC 3.5.3.23 |
FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-succinylornithine, ammonia and CO(2). {ECO:0000269|PubMed:15703173, ECO:0000269|PubMed:9696779}. | |
| b1744 | b1744 | Succinylglutamate desuccinylase (EC 3.5.1.96) | Cytoplasm | R_SGDS_enzyme | R_SGDS | 322 | Translation: 322.0, Folding: 32.2 | 35,800 | UniprotID: P76215 ECnumber: EC 3.5.1.96 |
FUNCTION: Transforms N(2)-succinylglutamate into succinate and glutamate. {ECO:0000269|PubMed:9696779}. | |
| b0692 | b0692 | Putrescine transporter PotE (Putrescine-proton symporter / putrescine-ornithine antiporter) | Cell_inner_membrane | R_PTRCORNt7pp_enzyme R_PTRCt2pp_duplicate_2_enzyme |
R_PTRCORNt7pp R_PTRCt2pp_duplicate_2 |
439 | Secretion: 439.0, Translation: 439.0, Folding: 43.9 | 46,495 | UniprotID: P0AAF1 | FUNCTION: Catalyzes both the uptake and excretion of putrescine. The uptake of putrescine is dependent on the membrane potential and the excretion involves putrescine-ornithine antiporter activity. {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000269|PubMed:1584788, ECO:0000269|PubMed:9045651}. | |
| b0693 | b0693 | Inducible ornithine decarboxylase (EC 4.1.1.17) | Cytoplasm | R_ORNDC_duplicate_2_enzyme | R_ORNDC_duplicate_2 | 732 | Translation: 732.0, Folding: 73.2 | 82,416 | UniprotID: P24169 ECnumber: EC 4.1.1.17 |
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| b1748 | b1748 | Succinylornithine transaminase (SOAT) (EC 2.6.1.81) (Carbon starvation protein C) (Succinylornithine aminotransferase) | Cytoplasm | R_ACOTA_enzyme R_SOTA_enzyme |
R_ACOTA R_SOTA |
406 | Translation: 406.0, Folding: 40.6 | 43,665 | UniprotID: P77581 ECnumber: EC 2.6.1.81 |
FUNCTION: Catalyzes the transamination of N(2)-succinylornithine and alpha-ketoglutarate into N(2)-succinylglutamate semialdehyde and glutamate. Can also act as an acetylornithine aminotransferase. {ECO:0000269|PubMed:9696779}. | |
| b0696 | b0696 | Potassium-transporting ATPase KdpC subunit (ATP phosphohydrolase [potassium-transporting] C chain) (Potassium-binding and translocating subunit C) (Potassium-translocating ATPase C chain) | Cell_inner_membrane | R_Kabcpp_enzyme R_Kabcpp_duplicate_2_enzyme |
R_Kabcpp R_Kabcpp_duplicate_2 |
190 | Secretion: 190.0, Translation: 190.0, Folding: 19.0 | 20,267 | UniprotID: P03961 | FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:2849541, PubMed:8499455, PubMed:23930894). This subunit acts as a catalytic chaperone that increases the ATP-binding affinity of the ATP-hydrolyzing subunit KdpB by the formation of a transient KdpB/KdpC/ATP ternary complex (PubMed:21711450). {ECO:0000269|PubMed:21711450, ECO:0000269|PubMed:23930894, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:8499455}. |
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| b0697 | b0697 | Potassium-transporting ATPase ATP-binding subunit (EC 3.6.3.12) (ATP phosphohydrolase [potassium-transporting] B chain) (Potassium-binding and translocating subunit B) (Potassium-translocating ATPase B chain) | Cell_inner_membrane | R_Kabcpp_enzyme R_Kabcpp_duplicate_2_enzyme |
R_Kabcpp R_Kabcpp_duplicate_2 |
682 | Secretion: 682.0, Translation: 682.0, Folding: 68.2 | 72,199 | UniprotID: P03960 ECnumber: EC 3.6.3.12 |
FUNCTION: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm (PubMed:2849541, PubMed:8499455, PubMed:23930894). This subunit is responsible for energy coupling to the transport system (PubMed:16354672). {ECO:0000269|PubMed:16354672, ECO:0000269|PubMed:23930894, ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:8499455}. |
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| b0980 | b0980 | Periplasmic AppA protein [Includes: Phosphoanhydride phosphohydrolase (EC 3.1.3.2) (pH 2.5 acid phosphatase) (AP); 4-phytase (EC 3.1.3.26) | Periplasm | R_NTP3pp_enzyme R_PHYTSpp_enzyme |
R_NTP3pp R_PHYTSpp |
432 | Secretion: 432.0, Translation: 432.0, Folding: 43.2 | 47,057 | UniprotID: P07102 ECnumber: EC 3.1.3.2; 3.1.3.26 |
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| b0160 | b0160 | Deoxyguanosinetriphosphate triphosphohydrolase (dGTP triphosphohydrolase) (dGTPase) (EC 3.1.5.1) | Cytoplasm | R_NTPTP1_enzyme R_NTPTP2_enzyme |
R_NTPTP1 R_NTPTP2 |
505 | Translation: 505.0, Folding: 50.5 | 59,383 | UniprotID: P15723 ECnumber: EC 3.1.5.1 |
FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs. {ECO:0000255|HAMAP-Rule:MF_00030, ECO:0000269|PubMed:2826481}. | |
| b0166 | b0166 | 2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase (EC 2.3.1.117) (Tetrahydrodipicolinate N-succinyltransferase) (THDP succinyltransferase) (THP succinyltransferase) (Tetrahydropicolinate succinylase) | Cytoplasm | R_THDPS_enzyme | R_THDPS | 274 | Translation: 274.0, Folding: 27.4 | 29,892 | UniprotID: P0A9D8 ECnumber: EC 2.3.1.117 |
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| b0340 | b0340 | Cyanate hydratase (Cyanase) (EC 4.2.1.104) (Cyanate hydrolase) (Cyanate lyase) | Cytoplasm | R_CYNTAH_enzyme | R_CYNTAH | 156 | Translation: 156.0, Folding: 15.6 | 17,049 | UniprotID: P00816 ECnumber: EC 4.2.1.104 |
FUNCTION: Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide. | |
| b0341 | b0341 | Cyanate transport protein CynX | Cell_inner_membrane | R_CYNTt2pp_enzyme | R_CYNTt2pp | 384 | Secretion: 384.0, Translation: 384.0, Folding: 38.4 | 41,361 | UniprotID: P17583 | FUNCTION: This protein is part of an active transport system that transports exogenous cyanate into E.coli cells. | |
| b0343 | b0343 | Lactose permease (Lactose-proton symport) | Cell_inner_membrane | R_LCTStpp_enzyme | R_LCTStpp | 417 | Secretion: 417.0, Translation: 417.0, Folding: 41.7 | 46,503 | UniprotID: P02920 | FUNCTION: Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). | |
| b0344 | b0344 | Beta-galactosidase (Beta-gal) (EC 3.2.1.23) (Lactase) | Cytoplasm | R_LACZ_enzyme | R_LACZ | 1024 | Translation: 1024.0, Folding: 102.4 | 116,483 | UniprotID: P00722 ECnumber: EC 3.2.1.23 |
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| b0433 | b0433 | Protein AmpG | Cell_inner_membrane | R_AGM3Pt2pp_enzyme R_AGM4Pt2pp_enzyme R_AGMt2pp_enzyme |
R_AGM3Pt2pp R_AGM4Pt2pp R_AGMt2pp |
491 | Secretion: 491.0, Translation: 491.0, Folding: 49.1 | 53,245 | UniprotID: P0AE16 | FUNCTION: Probably acts as a permease in the beta-lactamase induction system and in peptidoglycan recycling. | |
| b0430 | b0430 | Cytochrome bo(3) ubiquinol oxidase subunit 3 (Cytochrome o ubiquinol oxidase subunit 3) (Cytochrome o subunit 3) (Oxidase bo(3) subunit 3) (Ubiquinol oxidase chain C) (Ubiquinol oxidase polypeptide III) (Ubiquinol oxidase subunit 3) | Cell_inner_membrane | R_CYTBO3_4pp_enzyme | R_CYTBO3_4pp | 204 | Secretion: 204.0, Translation: 204.0, Folding: 20.4 | 22,623 | UniprotID: P0ABJ3 | FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529, ECO:0000269|PubMed:6308657}. | |
| b0347 | b0347 | 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase (3-HCI hydroxylase) (3-HPP hydroxylase) (EC 1.14.13.127) | Cytoplasm | R_3HCINNMH_enzyme R_3HPPPNH_enzyme |
R_3HCINNMH R_3HPPPNH |
554 | Translation: 554.0, Folding: 55.4 | 62,186 | UniprotID: P77397 ECnumber: EC 1.14.13.127 |
FUNCTION: Catalyzes the insertion of one atom of molecular oxygen into position 2 of the phenyl ring of 3-(3-hydroxyphenyl)propionate (3-HPP) and hydroxycinnamic acid (3HCI). {ECO:0000269|PubMed:9603882}. | |
| b0348 | b0348 | 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase (EC 1.13.11.16) (3-carboxyethylcatechol 2,3-dioxygenase) | Cytoplasm | R_DHCINDO_enzyme R_HPPPNDO_enzyme |
R_DHCINDO R_HPPPNDO |
314 | Translation: 314.0, Folding: 31.4 | 34,196 | UniprotID: P0ABR9 ECnumber: EC 1.13.11.16 |
FUNCTION: Catalyzes the non-heme iron(II)-dependent oxidative cleavage of 2,3-dihydroxyphenylpropionic acid and 2,3-dihydroxicinnamic acid into 2-hydroxy-6-ketononadienedioate and 2-hydroxy-6-ketononatrienedioate, respectively. {ECO:0000269|PubMed:8399388}. | |
| b0349 | b0349 | 2-hydroxy-6-oxononadienedioate/2-hydroxy-6-oxononatrienedioate hydrolase (EC 3.7.1.14) (2-hydroxy-6-ketonona-2,4-diene-1,9-dioic acid 5,6-hydrolase) (2-hydroxy-6-oxonona-2,4,7-triene-1,9-dioic acid 5,6-hydrolase) (2-hydroxy-6-oxonona-2,4-diene-1,9-dioic acid 5,6-hydrolase) | Cytoplasm | R_HKNDDH_enzyme R_HKNTDH_enzyme |
R_HKNDDH R_HKNTDH |
288 | Translation: 288.0, Folding: 28.8 | 31,937 | UniprotID: P77044 ECnumber: EC 3.7.1.14 |
FUNCTION: Catalyzes the cleavage of the C5-C6 bond of 2-hydroxy-6-oxononadienedioate and 2-hydroxy-6-oxononatrienedioate, a dienol ring fission product of the bacterial meta-cleavage pathway for degradation of phenylpropionic acid. MhpC shows some selectivity for the carboxylate of the side chain. {ECO:0000269|PubMed:15663941, ECO:0000269|PubMed:9098055, ECO:0000269|PubMed:9315862}. | |
| b4407 | b4407 | Sulfur carrier protein ThiS (Thiamine biosynthesis protein ThiS) | Cytoplasm | R_THZPSN3_enzyme | R_THZPSN3 | 66 | Translation: 66.0, Folding: 6.6 | 7,311 | UniprotID: O32583 | FUNCTION: Is the sulfur donor in the synthesis of the thiazole phosphate moiety of thiamine phosphate. {ECO:0000269|PubMed:9632726}. | |
| b4154 | b4154 | Fumarate reductase flavoprotein subunit (EC 1.3.5.4) | Cytoplasm | R_FRD2_enzyme R_FRD3_enzyme |
R_FRD2 R_FRD3 |
602 | Translation: 602.0, Folding: 60.2 | 65,972 | UniprotID: P00363 ECnumber: EC 1.3.5.4 |
FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. {ECO:0000269|PubMed:24374335}. | |
| b4088 | b4088 | D-allose-binding periplasmic protein (ALBP) | Periplasm | R_ALLabcpp_enzyme R_RIBabcpp_duplicate_3_enzyme |
R_ALLabcpp R_RIBabcpp_duplicate_3 |
311 | Secretion: 311.0, Translation: 311.0, Folding: 31.1 | 32,910 | UniprotID: P39265 | FUNCTION: Part of the binding-protein-dependent transport system AlsBAC for D-allose. {ECO:0000269|PubMed:9401019}. | |
| b4151 | b4151 | Fumarate reductase subunit D (Fumarate reductase 13 kDa hydrophobic protein) | Cell_inner_membrane | R_FRD2_enzyme R_FRD3_enzyme |
R_FRD2 R_FRD3 |
119 | Secretion: 119.0, Translation: 119.0, Folding: 11.9 | 13,107 | UniprotID: P0A8Q3 | FUNCTION: Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. | |
| b0180 | b0180 | 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ (EC 4.2.1.59) ((3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase) ((3R)-hydroxymyristoyl-ACP dehydrase) (17 kDa actomyosin component) (Beta-hydroxyacyl-ACP dehydratase) | Cytoplasm | R_3HAD100_duplicate_2_enzyme R_3HAD120_enzyme R_3HAD121_enzyme R_3HAD140_duplicate_2_enzyme R_3HAD141_duplicate_2_enzyme R_3HAD160_duplicate_2_enzyme R_3HAD161_enzyme R_3HAD180_duplicate_2_enzyme R_3HAD181_duplicate_2_enzyme R_3HAD40_duplicate_2_enzyme R_3HAD60_duplicate_2_enzyme R_3HAD80_duplicate_2_enzyme R_OGMEACPD_enzyme R_OPMEACPD_enzyme |
151 | Translation: 151.0, Folding: 15.1 | 17,033 | UniprotID: P0A6Q6 ECnumber: EC 4.2.1.59 |
FUNCTION: Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. {ECO:0000269|PubMed:7806516, ECO:0000269|PubMed:8910376}. | ||
| b4152 | b4152 | Fumarate reductase subunit C (Fumarate reductase 15 kDa hydrophobic protein) | Cell_inner_membrane | R_FRD2_enzyme R_FRD3_enzyme |
R_FRD2 R_FRD3 |
131 | Secretion: 131.0, Translation: 131.0, Folding: 13.1 | 15,015 | UniprotID: P0A8Q0 | FUNCTION: Seems to be involved in the anchoring of the catalytic components of the fumarate reductase complex to the cytoplasmic membrane. | |
| b4129 | b4129 | Lysine--tRNA ligase, heat inducible (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS) | Cytoplasm | R_AP4AS_enzyme R_LYSTRS_enzyme |
R_AP4AS R_LYSTRS |
505 | Translation: 505.0, Folding: 50.5 | 57,827 | UniprotID: P0A8N5 ECnumber: EC 6.1.1.6 |
FUNCTION: Also can synthesize a number of adenyl dinucleotides (in particular AppppA). These dinucleotides have been proposed to act as modulators of the heat-shock response and stress response. | |
| b0507 | b0507 | Glyoxylate carboligase (EC 4.1.1.47) (Tartronate-semialdehyde synthase) | Cytoplasm | R_GLXCL_enzyme | R_GLXCL | 593 | Translation: 593.0, Folding: 59.3 | 64,732 | UniprotID: P0AEP7 ECnumber: EC 4.1.1.47 |
FUNCTION: Catalyzes the condensation of two molecules of glyoxylate to give 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde). | |
| b0238 | b0238 | Xanthine phosphoribosyltransferase (EC 2.4.2.22) (Xanthine-guanine phosphoribosyltransferase) (XGPRT) | Cell_inner_membrane | R_GUAPRT_enzyme R_HXPRT_enzyme R_XPPT_enzyme |
R_GUAPRT R_HXPRT R_XPPT |
152 | Secretion: 152.0, Translation: 152.0, Folding: 15.2 | 16,971 | UniprotID: P0A9M5 ECnumber: EC 2.4.2.22 |
FUNCTION: Acts on guanine, xanthine and to a lesser extent hypoxanthine. {ECO:0000269|PubMed:9100006}. | |
| b4084 | b4084 | D-allose kinase (Allokinase) (EC 2.7.1.55) | Cytoplasm | R_ALLK_enzyme | R_ALLK | 309 | Translation: 309.0, Folding: 30.9 | 33,821 | UniprotID: P32718 ECnumber: EC 2.7.1.55 |
FUNCTION: Catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. Has also low level glucokinase activity in vitro. {ECO:0000255|HAMAP-Rule:MF_00988, ECO:0000269|PubMed:17979299, ECO:0000269|PubMed:9401019}. | |
| b3619 | b3619 | ADP-L-glycero-D-manno-heptose-6-epimerase (EC 5.1.3.20) (ADP-L-glycero-beta-D-manno-heptose-6-epimerase) (ADP-glyceromanno-heptose 6-epimerase) (ADP-hep 6-epimerase) (AGME) | Cytoplasm | R_AGMHE_enzyme | R_AGMHE | 310 | Translation: 310.0, Folding: 31.0 | 34,893 | UniprotID: P67910 ECnumber: EC 5.1.3.20 |
FUNCTION: Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose. {ECO:0000269|PubMed:6337148, ECO:0000269|PubMed:7929099}. | |
| b3612 | b3612 | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (BPG-independent PGAM) (Phosphoglyceromutase) (iPGM) (EC 5.4.2.12) | Cytoplasm | 514 | Translation: 514.0, Folding: 51.4 | 56,194 | UniprotID: P37689 ECnumber: EC 5.4.2.12 |
FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate (2-PGA) and 3-phosphoglycerate (3-PGA). {ECO:0000269|PubMed:10437801}. | |||
| b3610 | b3610 | Glutaredoxin 3 (Grx3) | Cytoplasm | 83 | Translation: 83.0, Folding: 8.3 | 9,137 | UniprotID: P0AC62 | FUNCTION: The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase. | |||
| b3617 | b3617 | 2-amino-3-ketobutyrate coenzyme A ligase (AKB ligase) (EC 2.3.1.29) (Glycine acetyltransferase) | Cytoplasm | R_GLYAT_enzyme | R_GLYAT | 398 | Translation: 398.0, Folding: 39.8 | 43,117 | UniprotID: P0AB77 ECnumber: EC 2.3.1.29 |
FUNCTION: Catalyzes the cleavage of 2-amino-3-ketobutyrate to glycine and acetyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00985, ECO:0000269|PubMed:2104756}. | |
| b3616 | b3616 | L-threonine 3-dehydrogenase (TDH) (EC 1.1.1.103) (L-threonine dehydrogenase) | Cytoplasm | R_THRD_enzyme | R_THRD | 341 | Translation: 341.0, Folding: 34.1 | 37,239 | UniprotID: P07913 ECnumber: EC 1.1.1.103 |
FUNCTION: Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+). {ECO:0000269|PubMed:6780553}. | |
| b0721 | b0721 | Succinate dehydrogenase cytochrome b556 subunit (Cytochrome b-556) | Cell_inner_membrane | R_SUCDi_enzyme | R_SUCDi | 129 | Secretion: 129.0, Translation: 129.0, Folding: 12.9 | 14,299 | UniprotID: P69054 | FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH). | |
| b3290 | b3290 | Trk system potassium uptake protein TrkA (K(+)-uptake protein TrkA) | Cell_inner_membrane | R_Kt2pp_enzyme R_Kt2pp_duplicate_2_enzyme |
R_Kt2pp R_Kt2pp_duplicate_2 |
458 | Secretion: 458.0, Translation: 458.0, Folding: 45.8 | 50,368 | UniprotID: P0AGI8 | FUNCTION: Part of the constitutive potassium transport systems TrkG and TrkH. May regulate the transport activity of TrkG and TrkH systems. Binds to NAD(+) and NADH. {ECO:0000269|PubMed:2674131, ECO:0000269|PubMed:8412700}. | |
| b3059 | b3059 | Probable glycerol-3-phosphate acyltransferase (G3P acyltransferase) (GPAT) (EC 2.3.1.15) (EC 2.3.1.n5) (Lysophosphatidic acid synthase) (LPA synthase) | Cell_inner_membrane | 205 | Secretion: 205.0, Translation: 205.0, Folding: 20.5 | 22,193 | UniprotID: P60782 ECnumber: EC 2.3.1.15; 2.3.1.n5 |
FUNCTION: Catalyzes the transfer of an acyl group from acyl-ACP to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme can also utilize acyl-CoA as fatty acyl donor, but not acyl-PO(4) (Probable). {ECO:0000305|PubMed:17645809}. | |||
| b3058 | b3058 | Dihydroneopterin aldolase (DHNA) (EC 4.1.2.25) (7,8-dihydroneopterin 2-epimerase) (7,8-dihydroneopterin aldolase) (7,8-dihydroneopterin epimerase) (EC 5.1.99.8) (Dihydroneopterin epimerase) | Cytoplasm | R_DHNPA2r_enzyme R_DHNPTE_enzyme |
R_DHNPA2r R_DHNPTE |
122 | Translation: 122.0, Folding: 12.2 | 13,620 | UniprotID: P0AC16 ECnumber: EC 4.1.2.25; 5.1.99.8 |
FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2 of dihydroneopterin to dihydromonapterin at appreciable velocity. {ECO:0000269|PubMed:9651328}. | |
| b3057 | b3057 | Undecaprenyl-diphosphatase (EC 3.6.1.27) (Bacitracin resistance protein) (Undecaprenyl pyrophosphate phosphatase) | Cell_inner_membrane | R_UDCPDP_duplicate_3_enzyme R_UDCPDPpp_enzyme |
R_UDCPDP_duplicate_3 R_UDCPDPpp |
273 | Secretion: 273.0, Translation: 273.0, Folding: 27.3 | 29,759 | UniprotID: P60932 ECnumber: EC 3.6.1.27 |
FUNCTION: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin. {ECO:0000269|PubMed:15778224}. | |
| b3503 | b3503 | Arsenate reductase (EC 1.20.4.1) (Arsenical pump modifier) | Cytoplasm | R_ASR_enzyme | R_ASR | 141 | Translation: 141.0, Folding: 14.1 | 15,853 | UniprotID: P0AB96 ECnumber: EC 1.20.4.1 |
FUNCTION: Reduction of arsenate [As(V)] to arsenite [As(III)]. This protein expands the substrate specificity of ArsAB pump which can extrude arsenite and antimonite to allow for arsenate pumping and resistance (By similarity). {ECO:0000250}. | |
| b3502 | b3502 | Arsenical pump membrane protein (Arsenic efflux pump protein) | Cell_inner_membrane | R_ASO3t8pp_enzyme | R_ASO3t8pp | 429 | Secretion: 429.0, Translation: 429.0, Folding: 42.9 | 45,497 | UniprotID: P0AB93 | FUNCTION: Involved in arsenical resistance. Thought to form the channel of an arsenite pump (By similarity). {ECO:0000250}. | |
| b3500 | b3500 | Glutathione reductase (GR) (GRase) (EC 1.8.1.7) | Cytoplasm | R_GTHOr_enzyme | R_GTHOr | 450 | Translation: 450.0, Folding: 45.0 | 48,773 | UniprotID: P06715 ECnumber: EC 1.8.1.7 |
FUNCTION: Maintains high levels of reduced glutathione in the cytosol. | |
| b2678 | b2678 | Glycine betaine/proline betaine transport system permease protein ProW | Cell_inner_membrane | R_CRNDabcpp_enzyme R_CRNabcpp_enzyme R_CTBTabcpp_enzyme R_PROabcpp_enzyme |
R_CRNDabcpp R_CRNabcpp R_CTBTabcpp R_PROabcpp |
354 | Secretion: 354.0, Translation: 354.0, Folding: 35.4 | 37,620 | UniprotID: P14176 | FUNCTION: Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake (PubMed:3305496, PubMed:7898450, PubMed:23249124). Probably responsible for the translocation of the substrate across the membrane (Probable). {ECO:0000269|PubMed:23249124, ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450, ECO:0000305}. | |
| b2679 | b2679 | Glycine betaine/proline betaine-binding periplasmic protein (GBBP) | Periplasm | R_CRNDabcpp_enzyme R_CRNabcpp_enzyme R_CTBTabcpp_enzyme R_PROabcpp_enzyme |
R_CRNDabcpp R_CRNabcpp R_CTBTabcpp R_PROabcpp |
330 | Secretion: 330.0, Translation: 330.0, Folding: 33.0 | 36,023 | UniprotID: P0AFM2 | FUNCTION: Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake. Binds glycine betaine and proline betaine with high affinity. {ECO:0000269|PubMed:14612446, ECO:0000269|PubMed:23249124, ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450}. | |
| b2676 | b2676 | Ribonucleoside-diphosphate reductase 2 subunit beta (EC 1.17.4.1) (R2F protein) (Ribonucleotide reductase 2) | Cytoplasm | R_RNDR1b_enzyme R_RNDR1b_duplicate_2_enzyme R_RNDR1b_duplicate_3_enzyme R_RNDR1b_duplicate_4_enzyme R_RNDR2b_enzyme R_RNDR2b_duplicate_2_enzyme R_RNDR2b_duplicate_3_enzyme R_RNDR2b_duplicate_4_enzyme R_RNDR3b_enzyme R_RNDR3b_duplicate_2_enzyme R_RNDR3b_duplicate_3_enzyme R_RNDR3b_duplicate_4_enzyme R_RNDR4b_enzyme R_RNDR4b_duplicate_2_enzyme R_RNDR4b_duplicate_3_enzyme R_RNDR4b_duplicate_4_enzyme |
319 | Translation: 319.0, Folding: 31.9 | 36,443 | UniprotID: P37146 ECnumber: EC 1.17.4.1 |
FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R2F contains the tyrosyl radical required for catalysis. | ||
| b2677 | b2677 | Glycine betaine/proline betaine transport system ATP-binding protein ProV | Cell_inner_membrane | R_CRNDabcpp_enzyme R_CRNabcpp_enzyme R_CTBTabcpp_enzyme R_PROabcpp_enzyme |
R_CRNDabcpp R_CRNabcpp R_CTBTabcpp R_PROabcpp |
400 | Secretion: 400.0, Translation: 400.0, Folding: 40.0 | 44,163 | UniprotID: P14175 | FUNCTION: Part of the ProU ABC transporter complex involved in glycine betaine and proline betaine uptake (PubMed:3305496, PubMed:7898450, PubMed:23249124). Probably responsible for energy coupling to the transport system (Probable). {ECO:0000269|PubMed:23249124, ECO:0000269|PubMed:3305496, ECO:0000269|PubMed:7898450, ECO:0000305}. | |
| b2675 | b2675 | Ribonucleoside-diphosphate reductase 2 subunit alpha (EC 1.17.4.1) (R1E protein) (Ribonucleotide reductase 2) | Cytoplasm | R_RNDR1b_enzyme R_RNDR1b_duplicate_2_enzyme R_RNDR1b_duplicate_3_enzyme R_RNDR1b_duplicate_4_enzyme R_RNDR2b_enzyme R_RNDR2b_duplicate_2_enzyme R_RNDR2b_duplicate_3_enzyme R_RNDR2b_duplicate_4_enzyme R_RNDR3b_enzyme R_RNDR3b_duplicate_2_enzyme R_RNDR3b_duplicate_3_enzyme R_RNDR3b_duplicate_4_enzyme R_RNDR4b_enzyme R_RNDR4b_duplicate_2_enzyme R_RNDR4b_duplicate_3_enzyme R_RNDR4b_duplicate_4_enzyme |
714 | Translation: 714.0, Folding: 71.4 | 80,479 | UniprotID: P39452 ECnumber: EC 1.17.4.1 |
FUNCTION: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. R1E contains the binding sites for both substrates and allosteric effectors and carries out the actual reduction of the ribonucleotide. | ||
| b2904 | b2904 | Glycine cleavage system H protein | Cytoplasm | R_GLYCL_enzyme | R_GLYCL | 129 | Translation: 129.0, Folding: 12.9 | 13,811 | UniprotID: P0A6T9 | FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. {ECO:0000255|HAMAP-Rule:MF_00272, ECO:0000269|PubMed:8375392}. | |
| b2905 | b2905 | Aminomethyltransferase (EC 2.1.2.10) (Glycine cleavage system T protein) | Cytoplasm | R_GLYCL_enzyme | R_GLYCL | 364 | Translation: 364.0, Folding: 36.4 | 40,147 | UniprotID: P27248 ECnumber: EC 2.1.2.10 |
FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. {ECO:0000255|HAMAP-Rule:MF_00259, ECO:0000269|PubMed:8375392}. | |
| b2907 | b2907 | 2-octaprenyl-6-methoxyphenol hydroxylase (EC 1.14.13.-) | Cytoplasm | R_OMPHHX_enzyme | R_OMPHHX | 392 | Translation: 392.0, Folding: 39.2 | 42,288 | UniprotID: P25534 ECnumber: EC 1.14.13.- |
FUNCTION: Is likely an oxygenase that introduces the hydroxyl group at carbon four of 2-octaprenyl-6-methoxyphenol resulting in the formation of 2-octaprenyl-6-methoxy-1,4-benzoquinol. {ECO:0000269|PubMed:4572721}. | |
| b2276 | b2276 | NADH-quinone oxidoreductase subunit N (EC 1.6.5.11) (NADH dehydrogenase I subunit N) (NDH-1 subunit N) (NUO14) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
485 | Secretion: 485.0, Translation: 485.0, Folding: 48.5 | 52,044 | UniprotID: P0AFF0 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
|
| b2277 | b2277 | NADH-quinone oxidoreductase subunit M (EC 1.6.5.11) (NADH dehydrogenase I subunit M) (NDH-1 subunit M) (NUO13) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
509 | Secretion: 509.0, Translation: 509.0, Folding: 50.9 | 56,525 | UniprotID: P0AFE8 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
|
| b2278 | b2278 | NADH-quinone oxidoreductase subunit L (EC 1.6.5.11) (NADH dehydrogenase I subunit L) (NDH-1 subunit L) (NUO12) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
613 | Secretion: 613.0, Translation: 613.0, Folding: 61.3 | 66,438 | UniprotID: P33607 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
|
| b2279 | b2279 | NADH-quinone oxidoreductase subunit K (EC 1.6.5.11) (NADH dehydrogenase I subunit K) (NDH-1 subunit K) (NUO11) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
100 | Secretion: 100.0, Translation: 100.0, Folding: 10.0 | 10,845 | UniprotID: P0AFE4 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.; FUNCTION: There are 2 NADH dehydrogenases in E.coli, however only this complex is able to use dNADH (reduced nicotinamide hypoxanthine dinucleotide, deamino-NADH) and dNADH-DB (dimethoxy-5-methyl-6-decyl-1,4-benzoquinone) as substrates. |
|
| b2874 | b2874 | Carbamate kinase-like protein YqeA | Cytoplasm | R_CBMKr_duplicate_3_enzyme | R_CBMKr_duplicate_3 | 310 | Translation: 310.0, Folding: 31.0 | 33,071 | UniprotID: Q46807 | ||
| b2019 | b2019 | ATP phosphoribosyltransferase (ATP-PRT) (ATP-PRTase) (EC 2.4.2.17) | Cytoplasm | R_ATPPRT_enzyme | R_ATPPRT | 299 | Translation: 299.0, Folding: 29.9 | 33,367 | UniprotID: P60757 ECnumber: EC 2.4.2.17 |
FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N-(5-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity. {ECO:0000269|PubMed:4909873}. | |
| b2871 | b2871 | Diaminopropionate ammonia-lyase (DAPAL) (EC 4.3.1.15) (2,3-diaminopropionate ammonia-lyase) (Alpha,beta-diaminopropionate ammonia-lyase) (Diaminopropionatase) | Cytoplasm | R_DAPAL_enzyme | R_DAPAL | 398 | Translation: 398.0, Folding: 39.8 | 43,328 | UniprotID: P66899 ECnumber: EC 4.3.1.15 |
FUNCTION: Catalyzes the alpha,beta-elimination reaction of both L- and D-alpha,beta-diaminopropionate (DAP) to form pyruvate and ammonia. In vitro the D-isomer of serine is degraded to pyruvate, though very poorly; other amino acids (L-serine, D- and L-threonine, D- and L-beta-Cl-alanine) are not substrates. In vivo allows poor growth on L-DAP or a DL-DAP mixture but not on D-DAP alone, this may be due to a poor promoter. DL-DAP is toxic in the absence of this enzyme, it may inhibit enzymes involved in the synthesis of pyruvate and aspartate, as well as amino acids derived from them. {ECO:0000269|PubMed:12596860, ECO:0000269|PubMed:12821154, ECO:0000269|PubMed:22505717, ECO:0000269|PubMed:22904288}. |
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| b2010 | b2010 | D-alanyl-D-alanine carboxypeptidase DacD (DD-carboxypeptidase) (DD-peptidase) (EC 3.4.16.4) (Penicillin-binding protein 6b) (PBP-6b) | Cell_inner_membrane | R_MDDCP1pp_duplicate_4 R_MDDCP2pp_duplicate_4 R_MDDCP3pp_duplicate_4 R_MDDCP4pp_duplicate_4 R_MDDCP5pp_duplicate_4 |
388 | Secretion: 388.0, Translation: 388.0, Folding: 38.8 | 43,346 | UniprotID: P33013 ECnumber: EC 3.4.16.4 |
FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | ||
| b3870 | b3870 | Glutamine synthetase (GS) (EC 6.3.1.2) (Glutamate--ammonia ligase) (Glutamine synthetase I beta) (GSI beta) | Cytoplasm | R_GLNS_enzyme | R_GLNS | 469 | Translation: 469.0, Folding: 46.9 | 51,904 | UniprotID: P0A9C5 ECnumber: EC 6.3.1.2 |
FUNCTION: Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. {ECO:0000250|UniProtKB:P0A1P6}. | |
| b3875 | b3875 | Porin OmpL | Cell_outer_membrane | R_H2Otex_duplicate_3_enzyme | R_H2Otex_duplicate_3 | 230 | Secretion: 230.0, Translation: 230.0, Folding: 23.0 | 27,200 | UniprotID: P76773 | FUNCTION: Outer membrane channel protein that allows an efficient diffusion of low-molecular-weight solutes such as small sugars and tetraglycine. However, the specific substrate recognized by the OmpL channel is unknown. {ECO:0000269|PubMed:12660153}. | |
| b3477 | b3477 | Nickel transport system permease protein NikB | Cell_inner_membrane | R_NI2uabcpp_enzyme | R_NI2uabcpp | 314 | Secretion: 314.0, Translation: 314.0, Folding: 31.4 | 35,248 | UniprotID: P33591 | FUNCTION: Involved in a nickel transport system, probably translocates nickel through the bacterial inner membrane. | |
| b3476 | b3476 | Nickel-binding periplasmic protein | Periplasm | R_NI2uabcpp_enzyme | R_NI2uabcpp | 524 | Secretion: 524.0, Translation: 524.0, Folding: 52.4 | 58,719 | UniprotID: P33590 | FUNCTION: Involved in a nickel transport system, probably represents the nickel binder. | |
| b3475 | b3475 | 4-phosphopantetheinyl transferase AcpT (EC 2.7.8.7) | Cytoplasm | R_ACPS1_enzyme | R_ACPS1 | 195 | Translation: 195.0, Folding: 19.5 | 21,768 | UniprotID: P37623 ECnumber: EC 2.7.8.7 |
FUNCTION: May be involved in an alternative pathway for phosphopantetheinyl transfer and holo-ACP synthesis in E.coli. The native apo-protein substrate is unknown. Is able to functionally replace AcpS in vivo but only when expressed at high levels. {ECO:0000269|PubMed:10625633, ECO:0000269|PubMed:8939709}. | |
| b2470 | b2470 | Probable aminoglycoside efflux pump (Acriflavine resistance protein D) | Cell_inner_membrane | 1037 | Secretion: 1037.0, Translation: 1037.0, Folding: 103.7 | 113,047 | UniprotID: P24177 | FUNCTION: Participates in the efflux of aminoglycosides. Confers resistance to a variety of these substances. {ECO:0000269|PubMed:10692383}. | |||
| b2472 | b2472 | Succinyl-diaminopimelate desuccinylase (SDAP desuccinylase) (EC 3.5.1.18) (N-succinyl-LL-2,6-diaminoheptanedioate amidohydrolase) | Cytoplasm | R_SDPDS_enzyme | R_SDPDS | 375 | Translation: 375.0, Folding: 37.5 | 41,269 | UniprotID: P0AED7 ECnumber: EC 3.5.1.18 |
FUNCTION: Catalyzes the hydrolysis of N-succinyl-L,L-diaminopimelic acid (SDAP), forming succinate and LL-2,6-diaminoheptanedioate (DAP), an intermediate involved in the bacterial biosynthesis of lysine and meso-diaminopimelic acid, an essential component of bacterial cell walls. {ECO:0000269|PubMed:3276674}. | |
| b2476 | b2476 | Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase) | Cytoplasm | R_PRASCSi_enzyme | R_PRASCSi | 237 | Translation: 237.0, Folding: 23.7 | 26,995 | UniprotID: P0A7D7 ECnumber: EC 6.3.2.6 |
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| b3478 | b3478 | Nickel transport system permease protein NikC | Cell_inner_membrane | R_NI2uabcpp_enzyme | R_NI2uabcpp | 277 | Secretion: 277.0, Translation: 277.0, Folding: 27.7 | 30,362 | UniprotID: P0AFA9 | FUNCTION: Involved in a nickel transport system, probably translocates nickel through the bacterial inner membrane. | |
| b2704 | b2704 | PTS system glucitol/sorbitol-specific EIIA component (EC 2.7.1.198) (EIIA-Gut) (EIII-Gut) (Glucitol/sorbitol-specific phosphotransferase enzyme IIA component) | Cytoplasm | R_SBTptspp_enzyme | R_SBTptspp | 123 | Translation: 123.0, Folding: 12.3 | 13,304 | UniprotID: P05706 ECnumber: EC 2.7.1.198 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport. It can also use D-mannitol. {ECO:0000269|PubMed:1100608}. |
|
| b2705 | b2705 | Sorbitol-6-phosphate 2-dehydrogenase (EC 1.1.1.140) (Glucitol-6-phosphate dehydrogenase) (Ketosephosphate reductase) | Cytoplasm | R_SBTPD_enzyme | R_SBTPD | 259 | Translation: 259.0, Folding: 25.9 | 27,858 | UniprotID: P05707 ECnumber: EC 1.1.1.140 |
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| b2702 | b2702 | PTS system glucitol/sorbitol-specific EIIC component (EIIC-Gut) (Glucitol/sorbitol permease IIC component) | Cell_inner_membrane | R_SBTptspp_enzyme | R_SBTptspp | 187 | Secretion: 187.0, Translation: 187.0, Folding: 18.7 | 20,580 | UniprotID: P56579 | FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport. It can also use D-mannitol. {ECO:0000269|PubMed:1100608}. |
|
| b2703 | b2703 | PTS system glucitol/sorbitol-specific EIIB component (EC 2.7.1.198) (EII-Gut) (Enzyme II-Gut) (Glucitol/sorbitol-specific phosphotransferase enzyme IIB component) | Cell_inner_membrane | R_SBTptspp_enzyme | R_SBTptspp | 319 | Secretion: 319.0, Translation: 319.0, Folding: 31.9 | 33,332 | UniprotID: P56580 ECnumber: EC 2.7.1.198 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport. It can also use D-mannitol. {ECO:0000269|PubMed:1100608}. |
|
| b2701 | b2701 | Membrane-bound lytic murein transglycosylase B (EC 4.2.2.n1) (35 kDa soluble lytic transglycosylase) (Murein hydrolase B) (Slt35) | Cell_outer_membrane | R_MLTGY1pp_enzyme R_MLTGY2pp_duplicate_6_enzyme R_MLTGY3pp_duplicate_6_enzyme R_MLTGY4pp_duplicate_3_enzyme |
R_MLTGY1pp R_MLTGY2pp_duplicate_6 R_MLTGY3pp_duplicate_6 R_MLTGY4pp_duplicate_3 |
361 | Secretion: 361.0, Translation: 361.0, Folding: 36.1 | 40,256 | UniprotID: P41052 ECnumber: EC 4.2.2.n1 |
FUNCTION: Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division. | |
| b2708 | b2708 | Arabinose 5-phosphate isomerase GutQ (API) (G-API) (EC 5.3.1.13) (Phosphosugar aldol-ketol isomerase) | Cytoplasm | R_A5PISO_duplicate_2_enzyme | R_A5PISO_duplicate_2 | 321 | Translation: 321.0, Folding: 32.1 | 34,031 | UniprotID: P17115 ECnumber: EC 5.3.1.13 |
FUNCTION: Catalyzes the reversible aldol-ketol isomerization between D-ribulose 5-phosphate (Ru5P) and D-arabinose 5-phosphate (A5P). It appears that the physiological function of G-API may be to synthesize the regulatory molecule A5P, which in turn participates in the induction of the gut operon through an unknown mechanism. It is also able of sustaining the biosynthetic pathway of 3-deoxy-D-manno-octulosonate (KDO), a unique 8-carbon sugar component of lipopolysaccharides (LPSs). {ECO:0000269|PubMed:16199563}. |
|
| b2497 | b2497 | Uracil permease (Uracil transporter) | Cell_inner_membrane | R_URAt2pp_copy1_enzyme | R_URAt2pp_copy1 | 429 | Secretion: 429.0, Translation: 429.0, Folding: 42.9 | 45,060 | UniprotID: P0AGM7 | FUNCTION: Transport of uracil in the cell. {ECO:0000269|PubMed:21423164, ECO:0000269|PubMed:7721693}. | |
| b2492 | b2492 | Probable formate transporter 2 (Formate channel 2) | Cell_inner_membrane | R_FORt2pp_duplicate_2_enzyme R_FORtppi_duplicate_2_enzyme |
R_FORt2pp_duplicate_2 R_FORtppi_duplicate_2 |
282 | Secretion: 282.0, Translation: 282.0, Folding: 28.2 | 30,565 | UniprotID: P77733 | FUNCTION: Involved in the bidirectional transport of formate. {ECO:0000250}. | |
| b2490 | b2490 | Hydrogenase-4 component J (EC 1.-.-.-) | Cytoplasm | R_FHL_enzyme | R_FHL | 137 | Translation: 137.0, Folding: 13.7 | 15,577 | UniprotID: P77453 ECnumber: EC 1.-.-.- |
FUNCTION: Possible component of hydrogenase 4. {ECO:0000305|PubMed:9387241}. | |
| b0432 | b0432 | Cytochrome bo(3) ubiquinol oxidase subunit 2 (Cytochrome b562-o complex subunit II) (Cytochrome o ubiquinol oxidase subunit 2) (Cytochrome o subunit 2) (Oxidase bo(3) subunit 2) (Ubiquinol oxidase chain B) (Ubiquinol oxidase polypeptide II) (Ubiquinol oxidase subunit 2) | Cell_inner_membrane | R_CYTBO3_4pp_enzyme | R_CYTBO3_4pp | 315 | Secretion: 315.0, Translation: 315.0, Folding: 31.5 | 34,911 | UniprotID: P0ABJ1 | FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529, ECO:0000269|PubMed:6308657}. | |
| b2498 | b2498 | Uracil phosphoribosyltransferase (EC 2.4.2.9) (UMP pyrophosphorylase) (UPRTase) | Cytoplasm | R_UPPRT_enzyme | R_UPPRT | 208 | Translation: 208.0, Folding: 20.8 | 22,533 | UniprotID: P0A8F0 ECnumber: EC 2.4.2.9 |
FUNCTION: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate. | |
| b2499 | b2499 | Phosphoribosylformylglycinamidine cyclo-ligase (EC 6.3.3.1) (AIR synthase) (AIRS) (Phosphoribosyl-aminoimidazole synthetase) | Cytoplasm | R_PRAIS_enzyme | R_PRAIS | 345 | Translation: 345.0, Folding: 34.5 | 36,854 | UniprotID: P08178 ECnumber: EC 6.3.3.1 |
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| b0431 | b0431 | Cytochrome bo(3) ubiquinol oxidase subunit 1 (EC 1.10.3.10) (Cytochrome b562-o complex subunit I) (Cytochrome o ubiquinol oxidase subunit 1) (Cytochrome o subunit 1) (Oxidase bo(3) subunit 1) (Ubiquinol oxidase chain A) (Ubiquinol oxidase polypeptide I) (Ubiquinol oxidase subunit 1) | Cell_inner_membrane | R_CYTBO3_4pp_enzyme | R_CYTBO3_4pp | 663 | Secretion: 663.0, Translation: 663.0, Folding: 66.3 | 74,368 | UniprotID: P0ABI8 ECnumber: EC 1.10.3.10 |
FUNCTION: Cytochrome bo(3) ubiquinol terminal oxidase is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at high aeration. Has proton pump activity across the membrane in addition to electron transfer, pumping 2 protons/electron. Protons are probably pumped via D- and K- channels found in this subunit (PubMed:11017202). {ECO:0000269|PubMed:11017202, ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:22843529, ECO:0000269|PubMed:6308657}. |
|
| b1008 | b1008 | Probable malonic semialdehyde reductase RutE (EC 1.1.1.298) | Cytoplasm | R_MSAR_enzyme | R_MSAR | 196 | Translation: 196.0, Folding: 19.6 | 21,570 | UniprotID: P75894 ECnumber: EC 1.1.1.298 |
FUNCTION: May reduce toxic product malonic semialdehyde to 3-hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation. {ECO:0000269|PubMed:16540542}. | |
| b1009 | b1009 | Putative aminoacrylate hydrolase RutD (EC 3.5.1.-) (Aminohydrolase) | Cytoplasm | R_3AMACHYD_enzyme | R_3AMACHYD | 266 | Translation: 266.0, Folding: 26.6 | 28,898 | UniprotID: P75895 ECnumber: EC 3.5.1.- |
FUNCTION: May increase the rate of spontaneous hydrolysis of aminoacrylate to malonic semialdehyde. Required to remove a toxic intermediate produce in vivo, but not in vitro in the pyrimidine nitrogen degradation. {ECO:0000269|PubMed:16540542}. | |
| b1002 | b1002 | Glucose-1-phosphatase (G1Pase) (EC 3.1.3.10) | Periplasm | R_G1PPpp_enzyme R_GAL1PPpp_enzyme |
R_G1PPpp R_GAL1PPpp |
413 | Secretion: 413.0, Translation: 413.0, Folding: 41.3 | 45,683 | UniprotID: P19926 ECnumber: EC 3.1.3.10 |
FUNCTION: Absolutely required for the growth of E.coli in a high-phosphate medium containing G-1-P as the sole carbon source. | |
| b1006 | b1006 | Putative pyrimidine permease RutG | Cell_inner_membrane | R_URAt2pp_copy2_enzyme | R_URAt2pp_copy2 | 442 | Secretion: 442.0, Translation: 442.0, Folding: 44.2 | 45,557 | UniprotID: P75892 | FUNCTION: May function as a proton-driven pyrimidine uptake system. {ECO:0000269|PubMed:16540542}. | |
| b1007 | b1007 | FMN reductase (NADH) RutF (EC 1.5.1.42) (FMN reductase) (NADH-flavin reductase RutF) (NADH:flavin oxidoreductase) | Cytoplasm | R_PYROX_enzyme | R_PYROX | 164 | Translation: 164.0, Folding: 16.4 | 17,749 | UniprotID: P75893 ECnumber: EC 1.5.1.42 |
FUNCTION: Catalyzes the reduction of FMN to FMNH2 which is used to reduce pyrimidine by RutA via the Rut pathway. In vitro, the flavin reductase Fre can substitute for the function of RutF, however, RutF is required for uracil utilization in vivo. {ECO:0000269|PubMed:16540542, ECO:0000269|PubMed:20400551}. | |
| b4238 | b4238 | Anaerobic ribonucleoside-triphosphate reductase (EC 1.1.98.6) (Class III ribonucleoside-triphosphate reductase) | Cytoplasm | R_RNTR1c2_enzyme R_RNTR1c2_duplicate_2_enzyme R_RNTR1c2_duplicate_3_enzyme R_RNTR1c2_duplicate_4_enzyme R_RNTR2c2_enzyme R_RNTR2c2_duplicate_2_enzyme R_RNTR2c2_duplicate_3_enzyme R_RNTR2c2_duplicate_4_enzyme R_RNTR3c2_enzyme R_RNTR3c2_duplicate_2_enzyme R_RNTR3c2_duplicate_3_enzyme R_RNTR3c2_duplicate_4_enzyme R_RNTR4c2_enzyme R_RNTR4c2_duplicate_2_enzyme R_RNTR4c2_duplicate_3_enzyme R_RNTR4c2_duplicate_4_enzyme |
712 | Translation: 712.0, Folding: 71.2 | 80,023 | UniprotID: P28903 ECnumber: EC 1.1.98.6 |
FUNCTION: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair. {ECO:0000269|PubMed:1460049, ECO:0000269|PubMed:24827372, ECO:0000269|PubMed:7568012, ECO:0000269|PubMed:8381402, ECO:0000269|PubMed:9305874}. | ||
| b4239 | b4239 | Trehalose-6-phosphate hydrolase (EC 3.2.1.93) (Alpha,alpha-phosphotrehalase) | Cytoplasm | R_TRE6PH_enzyme | R_TRE6PH | 551 | Translation: 551.0, Folding: 55.1 | 63,838 | UniprotID: P28904 ECnumber: EC 3.2.1.93 |
FUNCTION: Hydrolyzes trehalose-6-phosphate to glucose and glucose 6-phosphate. Can also very effectively hydrolyzes p-nitrophenyl-alpha-D-glucopyranoside, but it does not recognize trehalose, sucrose, maltose, isomaltose, or maltodextrins. {ECO:0000269|PubMed:8083158}. | |
| b0759 | b0759 | UDP-glucose 4-epimerase (EC 5.1.3.2) (Galactowaldenase) (UDP-galactose 4-epimerase) | Cytoplasm | R_UDPG4E_enzyme | R_UDPG4E | 338 | Translation: 338.0, Folding: 33.8 | 37,265 | UniprotID: P09147 ECnumber: EC 5.1.3.2 |
FUNCTION: Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. It is only active on UDP-galactose and UDP-glucose. {ECO:0000269|PubMed:14235524}. | |
| b0758 | b0758 | Galactose-1-phosphate uridylyltransferase (Gal-1-P uridylyltransferase) (EC 2.7.7.12) (UDP-glucose--hexose-1-phosphate uridylyltransferase) | Cytoplasm | R_UGLT_enzyme | R_UGLT | 348 | Translation: 348.0, Folding: 34.8 | 39,646 | UniprotID: P09148 ECnumber: EC 2.7.7.12 |
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| b4230 | b4230 | Inner membrane ABC transporter permease protein YtfT | Cell_inner_membrane | R_GALabcpp_duplicate_2_enzyme R_RIBabcpp_duplicate_2_enzyme |
R_GALabcpp_duplicate_2 R_RIBabcpp_duplicate_2 |
341 | Secretion: 341.0, Translation: 341.0, Folding: 34.1 | 35,659 | UniprotID: P39328 | FUNCTION: Probably part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane. | |
| b0752 | b0752 | Zinc transporter ZitB | Cell_inner_membrane | R_CD2t3pp_duplicate_2 R_COBALT2t3pp R_MN2t3pp_duplicate_2 R_NI2t3pp_duplicate_2 R_ZN2t3pp_duplicate_2 |
313 | Secretion: 313.0, Translation: 313.0, Folding: 31.3 | 34,678 | UniprotID: P75757 | FUNCTION: Involved in zinc efflux across the cytoplasmic membrane, thus reducing zinc accumulation in the cytoplasm and rendering bacteria more resistant to zinc. It may contribute to zinc homeostasis at low concentrations of zinc, whereas ZntA is required for growth at more toxic concentrations. | ||
| b4232 | b4232 | Fructose-1,6-bisphosphatase class 1 (FBPase class 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1) | Cytoplasm | R_FBP_enzyme | R_FBP | 332 | Translation: 332.0, Folding: 33.2 | 36,834 | UniprotID: P0A993 ECnumber: EC 3.1.3.11 |
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| b4233 | b4233 | UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase (EC 6.3.2.45) (Murein peptide ligase) (UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-meso-diaminopimelate ligase) | Secreted | R_UM3PL_enzyme R_UM4PL_enzyme |
R_UM3PL R_UM4PL |
457 | Translation: 457.0, Folding: 45.7 | 49,874 | UniprotID: P37773 ECnumber: EC 6.3.2.45 |
FUNCTION: Reutilizes the intact tripeptide L-alanyl-gamma-D-glutamyl-meso-diaminopimelate by linking it to UDP-N-acetylmuramate. The enzyme can also use the tetrapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioyl-D-alanyl-D-alanine in vivo and in vitro. {ECO:0000269|PubMed:17384195, ECO:0000269|PubMed:8808921}. |
|
| b0757 | b0757 | Galactokinase (EC 2.7.1.6) (Galactose kinase) | Cytoplasm | R_GALKr_duplicate_2_enzyme | R_GALKr_duplicate_2 | 382 | Translation: 382.0, Folding: 38.2 | 41,442 | UniprotID: P0A6T3 ECnumber: EC 2.7.1.6 |
FUNCTION: Catalyzes the transfer of the gamma-phosphate of ATP to D-galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D-galactosamine. Is not able to use D-galacturonic acid, D-talose, L-altrose, and L-glucose as substrates. {ECO:0000255|HAMAP-Rule:MF_00246, ECO:0000269|PubMed:12816414, ECO:0000269|PubMed:14612558, ECO:0000269|PubMed:200486}. |
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| b0756 | b0756 | Aldose 1-epimerase (EC 5.1.3.3) (Galactose mutarotase) (Type-1 mutarotase) | Cytoplasm | R_GALM2pp_enzyme | R_GALM2pp | 346 | Translation: 346.0, Folding: 34.6 | 38,190 | UniprotID: P0A9C3 ECnumber: EC 5.1.3.3 |
FUNCTION: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose. | |
| b0755 | b0755 | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase (BPG-dependent PGAM) (PGAM) (Phosphoglyceromutase) (dPGM) (EC 5.4.2.11) | Cytoplasm | 250 | Translation: 250.0, Folding: 25.0 | 28,556 | UniprotID: P62707 ECnumber: EC 5.4.2.11 |
FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01039, ECO:0000269|PubMed:10437801}. | |||
| b0754 | b0754 | Phospho-2-dehydro-3-deoxyheptonate aldolase, Phe-sensitive (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase) (DAHP synthase) (Phospho-2-keto-3-deoxyheptonate aldolase) | Cytoplasm | R_DDPA_enzyme | R_DDPA | 350 | Translation: 350.0, Folding: 35.0 | 38,010 | UniprotID: P0AB91 ECnumber: EC 2.5.1.54 |
FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). | |
| b0186 | b0186 | Constitutive lysine decarboxylase (LDC) (EC 4.1.1.18) | Cytoplasm | R_LYSDC_enzyme | R_LYSDC | 713 | Translation: 713.0, Folding: 71.3 | 80,590 | UniprotID: P52095 ECnumber: EC 4.1.1.18 |
FUNCTION: LDC is constitutively but weakly expressed under various conditions. | |
| b2683 | b2683 | Uncharacterized protein YgaH | Cytoplasm | R_VALt2rpp_duplicate_2_enzyme | R_VALt2rpp_duplicate_2 | 111 | Translation: 111.0, Folding: 11.1 | 12,024 | UniprotID: P43667 | ||
| b1919 | b1919 | D-cysteine desulfhydrase (EC 4.4.1.15) | Cytoplasm | R_CYSDDS_enzyme | R_CYSDDS | 328 | Translation: 328.0, Folding: 32.8 | 35,153 | UniprotID: P76316 ECnumber: EC 4.4.1.15 |
FUNCTION: Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D-alanine. {ECO:0000255|HAMAP-Rule:MF_01045, ECO:0000269|PubMed:3908101}. | |
| b1912 | b1912 | CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase (EC 2.7.8.5) (Phosphatidylglycerophosphate synthase) (PGP synthase) | Cell_inner_membrane | R_PGSA120 R_PGSA140 R_PGSA141 R_PGSA160 R_PGSA161 R_PGSA180 R_PGSA181 |
182 | Secretion: 182.0, Translation: 182.0, Folding: 18.2 | 20,701 | UniprotID: P0ABF8 ECnumber: EC 2.7.8.5 |
FUNCTION: This protein catalyzes the committed step to the synthesis of the acidic phospholipids. | ||
| b0182 | b0182 | Lipid-A-disaccharide synthase (EC 2.4.1.182) | Cytoplasm | R_LPADSS_enzyme | R_LPADSS | 382 | Translation: 382.0, Folding: 38.2 | 42,382 | UniprotID: P10441 ECnumber: EC 2.4.1.182 |
FUNCTION: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | |
| b4153 | b4153 | Fumarate reductase iron-sulfur subunit (EC 1.3.5.1) | Cytoplasm | R_FRD2_enzyme R_FRD3_enzyme |
R_FRD2 R_FRD3 |
244 | Translation: 244.0, Folding: 24.4 | 27,123 | UniprotID: P0AC47 ECnumber: EC 1.3.5.1 |
FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. | |
| b1599 | b1599 | Spermidine export protein MdtI | Cell_inner_membrane | R_SPMDt3pp_enzyme | R_SPMDt3pp | 109 | Secretion: 109.0, Translation: 109.0, Folding: 10.9 | 11,720 | UniprotID: P69210 | FUNCTION: Catalyzes the excretion of spermidine. Can also confer resistance to deoxycholate and SDS. {ECO:0000269|PubMed:11566977, ECO:0000269|PubMed:18039771}. | |
| b0181 | b0181 | Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase (UDP-N-acetylglucosamine acyltransferase) (EC 2.3.1.129) | Cytoplasm | R_UAGAAT_enzyme | R_UAGAAT | 262 | Translation: 262.0, Folding: 26.2 | 28,080 | UniprotID: P0A722 ECnumber: EC 2.3.1.129 |
FUNCTION: Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. | |
| b1592 | b1592 | Voltage-gated ClC-type chloride channel ClcB | Cell_inner_membrane | R_CLt3_2pp_duplicate_2_enzyme | R_CLt3_2pp_duplicate_2 | 418 | Secretion: 418.0, Translation: 418.0, Folding: 41.8 | 44,153 | UniprotID: P76175 | FUNCTION: Probably acts as an electrical shunt for an outwardly-directed proton pump that is linked to amino acid decarboxylation, as part of the extreme acid resistance (XAR) response. {ECO:0000269|PubMed:12384697}. | |
| b1590 | b1590 | Anaerobic dimethyl sulfoxide reductase chain YnfH (DMSO reductase anchor subunit YnfH) | Cell_inner_membrane | R_DMSOR1_enzyme R_SELR_enzyme R_TMAOR1_duplicate_2_enzyme |
R_DMSOR1 R_SELR R_TMAOR1_duplicate_2 |
284 | Secretion: 284.0, Translation: 284.0, Folding: 28.4 | 30,524 | UniprotID: P76173 | FUNCTION: Terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. The C subunit anchors the other two subunits to the membrane and stabilize the catalytic subunits (By similarity). {ECO:0000250}. | |
| b2893 | b2893 | Thiol:disulfide interchange protein DsbC | Periplasm | R_DSBCGT_enzyme R_TDSR1_enzyme |
R_DSBCGT R_TDSR1 |
236 | Secretion: 236.0, Translation: 236.0, Folding: 23.6 | 25,622 | UniprotID: P0AEG6 | FUNCTION: Acts as a disulfide isomerase, interacting with incorrectly folded proteins to correct non-native disulfide bonds. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbC is reoxidized by DsbD. {ECO:0000269|PubMed:19965429}. |
|
| b1759 | b1759 | CTP pyrophosphohydrolase (EC 3.6.1.65) | Cytoplasm | R_NTPP3_duplicate_3_enzyme R_NTPP4_enzyme |
R_NTPP3_duplicate_3 R_NTPP4 |
135 | Translation: 135.0, Folding: 13.5 | 15,046 | UniprotID: P77788 ECnumber: EC 3.6.1.65 |
FUNCTION: Hydrolase with a preference for pyrimidine substrates. Has high activity with 5-methyl-dCTP, and much lower activity with CTP, dCTP, 5-hydroxy-dCTP, 2-hydroxy-dATP and 8-hydroxy-dGTP. {ECO:0000269|PubMed:11053429, ECO:0000269|PubMed:12509230, ECO:0000269|PubMed:15823026}. | |
| b2131 | b2131 | Glycine betaine-binding protein YehZ | Periplasm | R_CHLabcpp_enzyme R_GLYBabcpp_enzyme |
R_CHLabcpp R_GLYBabcpp |
305 | Secretion: 305.0, Translation: 305.0, Folding: 30.5 | 32,609 | UniprotID: P33362 | FUNCTION: Part of an ABC transporter complex involved in low-affinity glycine betaine uptake. Binds glycine betaine with low affinity. {ECO:0000269|PubMed:26325238}. | |
| b4013 | b4013 | Homoserine O-succinyltransferase (HST) (EC 2.3.1.46) (Homoserine transsuccinylase) (HTS) | Cytoplasm | R_HSST_enzyme | R_HSST | 309 | Translation: 309.0, Folding: 30.9 | 35,727 | UniprotID: P07623 ECnumber: EC 2.3.1.46 |
FUNCTION: Transfers a succinyl group from succinyl-CoA to L-homoserine, forming succinyl-L-homoserine (PubMed:10572016, PubMed:17442255, PubMed:17302437, PubMed:28581482). Utilizes a ping-pong kinetic mechanism in which the succinyl group of succinyl-CoA is initially transferred to the enzyme to form a succinyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-succinylhomoserine (PubMed:10572016, PubMed:17442255, PubMed:17302437). Cannot use acetyl-CoA (PubMed:10572016). {ECO:0000269|PubMed:10572016, ECO:0000269|PubMed:17302437, ECO:0000269|PubMed:17442255, ECO:0000269|PubMed:28581482}. |
|
| b0403 | b0403 | Maltodextrin glucosidase (EC 3.2.1.20) (Alpha-glucosidase) | Cytoplasm | R_MLTG1_enzyme R_MLTG2_enzyme R_MLTG3_enzyme R_MLTG4_enzyme R_MLTG5_enzyme |
R_MLTG1 R_MLTG2 R_MLTG3 R_MLTG4 R_MLTG5 |
604 | Translation: 604.0, Folding: 60.4 | 69,041 | UniprotID: P21517 ECnumber: EC 3.2.1.20 |
FUNCTION: May play a role in regulating the intracellular level of maltotriose. Cleaves glucose from the reducing end of maltotriose and longer maltodextrins with a chain length of up to 7 glucose units. | |
| b0401 | b0401 | Branched-chain amino acid transport system 2 carrier protein (LIV-II) | Cell_inner_membrane | R_ILEt2rpp_enzyme R_LEUt2rpp_enzyme R_VALt2rpp_enzyme |
R_ILEt2rpp R_LEUt2rpp R_VALt2rpp |
439 | Secretion: 439.0, Translation: 439.0, Folding: 43.9 | 46,209 | UniprotID: P0AD99 | FUNCTION: Component of the LIV-II transport system for branched-chain amino acids. This LIV-II transport system may be H(+)-coupled. | |
| b0404 | b0404 | Acyl carrier protein phosphodiesterase (ACP phosphodiesterase) (EC 3.1.4.14) | Cytoplasm | R_FA100ACPHi R_FA120ACPHi R_FA140ACPHi R_FA141ACPHi R_FA160ACPHi R_FA161ACPHi R_FA80ACPHi |
193 | Translation: 193.0, Folding: 19.3 | 22,961 | UniprotID: P21515 ECnumber: EC 3.1.4.14 |
FUNCTION: Converts holo-ACP to apo-ACP by hydrolytic cleavage of the phosphopantetheine prosthetic group from ACP. {ECO:0000255|HAMAP-Rule:MF_01950, ECO:0000269|PubMed:16107329}. | ||
| b4094 | b4094 | Ribose 1,5-bisphosphate phosphokinase PhnN (EC 2.7.4.23) (Ribose 1,5-bisphosphokinase) | Cytoplasm | R_R15BPK_enzyme | R_R15BPK | 185 | Translation: 185.0, Folding: 18.5 | 20,730 | UniprotID: P16690 ECnumber: EC 2.7.4.23 |
FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). Accepts ATP but not GTP as a phosphoryl donor, and uses ribose 1,5-bisphosphate but not ribose, ribose 1-phosphate, or ribose 5-phosphate as a phosphoryl acceptor. {ECO:0000269|PubMed:12700258, ECO:0000269|PubMed:19733071}. | |
| b4090 | b4090 | Ribose-5-phosphate isomerase B (EC 5.3.1.6) (Phosphoriboisomerase B) | Cytoplasm | R_ALLPI_enzyme R_RPI_duplicate_2_enzyme |
R_ALLPI R_RPI_duplicate_2 |
149 | Translation: 149.0, Folding: 14.9 | 16,073 | UniprotID: P37351 ECnumber: EC 5.3.1.6 |
FUNCTION: Catalyzes the interconversion of ribulose-5-P and ribose-5-P. It probably also has activity on D-allose 6-phosphate. {ECO:0000269|PubMed:1104357, ECO:0000269|PubMed:18640127, ECO:0000269|PubMed:4909663, ECO:0000269|PubMed:8576032}. | |
| b0241 | b0241 | Outer membrane pore protein E | Cell_outer_membrane | R_pqqtex_enzyme R_12PPDRtex_duplicate_2_enzyme R_12PPDStex_duplicate_2_enzyme R_23CAMPtex_duplicate_2_enzyme R_23CCMPtex_duplicate_2_enzyme R_23CGMPtex_duplicate_2_enzyme R_23CUMPtex_duplicate_2_enzyme R_23DAPPAtex_duplicate_2_enzyme R_26DAHtex_duplicate_2_enzyme R_34dhpactex_duplicate_2_enzyme R_3AMPtex_duplicate_2_enzyme R_3CMPtex_duplicate_2_enzyme R_3GMPtex_duplicate_4_enzyme R_3HPPtex_duplicate_4_enzyme R_3PEPTtex_duplicate_2_enzyme R_3UMPtex_duplicate_2_enzyme R_4HOXPACDtex_duplicate_2_enzyme R_4PEPTtex_duplicate_2_enzyme R_5DGLCNtex_duplicate_2_enzyme R_5MTRtex_duplicate_4_enzyme R_ABUTtex_duplicate_2_enzyme R_ACACtex_duplicate_2_enzyme R_ACALDtex_duplicate_2_enzyme R_ACGAL1Ptex_duplicate_2_enzyme R_ACGALtex_duplicate_2_enzyme R_ACGAM1Ptex_duplicate_2_enzyme R_ACGAtex_duplicate_2_enzyme R_ACMANAtex_duplicate_2_enzyme R_ACMUMtex_duplicate_2_enzyme R_ACSERtex_enzyme R_ACtex_duplicate_2_enzyme R_ADEtex_duplicate_2_enzyme R_AGMtex_duplicate_2_enzyme R_AKGtex_duplicate_2_enzyme R_ALAALAtex_duplicate_2_enzyme R_ALAtex_duplicate_2_enzyme R_ALLTNtex_duplicate_2_enzyme R_ALLtex_duplicate_2_enzyme R_AMPtex_duplicate_4_enzyme R_ANHGMtex_duplicate_2_enzyme R_ARBTtex_enzyme R_ARBtex_duplicate_2_enzyme R_ARGtex_duplicate_2_enzyme R_ASCBtex_duplicate_2_enzyme R_ASNtex_duplicate_2_enzyme R_ASO3tex_duplicate_2_enzyme R_ASPtex_duplicate_2_enzyme R_BALAtex_duplicate_2_enzyme R_BTNtex_enzyme R_BUTSO3tex_duplicate_2_enzyme R_BUTtex_duplicate_2_enzyme R_CA2tex_duplicate_2_enzyme R_CD2tex_duplicate_2_enzyme R_CGLYtex_duplicate_2_enzyme R_CHLtex_duplicate_2_enzyme R_CHTBStex_duplicate_4_enzyme R_CITtex_duplicate_2_enzyme R_CLtex_duplicate_2_enzyme R_CMPtex_duplicate_2_enzyme R_CMtex_duplicate_4_enzyme R_CO2tex_duplicate_2_enzyme R_COBALT2tex_duplicate_2_enzyme R_CRNDtex_duplicate_4_enzyme R_CRNtex_duplicate_2_enzyme R_CSNtex_duplicate_2_enzyme R_CU2tex_duplicate_3_enzyme R_CUtex_duplicate_2_enzyme R_CYANtex_duplicate_2_enzyme R_CYNTtex_duplicate_2_enzyme R_CYSDtex_duplicate_2_enzyme R_CYStex_duplicate_2_enzyme R_CYTDtex_duplicate_2_enzyme R_D_LACtex_duplicate_2_enzyme R_DALAtex_duplicate_2_enzyme R_DAMPtex_duplicate_2_enzyme R_DAPtex_duplicate_2_enzyme R_DCAtex_duplicate_2_enzyme R_DCMPtex_duplicate_2_enzyme R_DDGLCNtex_duplicate_4_enzyme R_DGMPtex_duplicate_2_enzyme R_DGSNtex_duplicate_2_enzyme R_DHAtex_duplicate_2_enzyme R_DIMPtex_duplicate_2_enzyme R_DINStex_duplicate_2_enzyme R_DMSOtex_duplicate_2_enzyme R_DMStex_duplicate_2_enzyme R_DOPAtex_duplicate_2_enzyme R_DOXRBCNtex_duplicate_4_enzyme R_DSERtex_duplicate_2_enzyme R_DTMPtex_duplicate_2_enzyme R_DUMPtex_duplicate_2_enzyme R_ETHAtex_duplicate_2_enzyme R_ETHSO3tex_duplicate_2_enzyme R_ETOHtex_duplicate_2_enzyme R_F6Ptex_duplicate_2_enzyme R_FALDtex_duplicate_2_enzyme R_FE2tex_duplicate_2_enzyme R_FE3tex_duplicate_2_enzyme R_FORtex_duplicate_2_enzyme R_FRULYStex_duplicate_2_enzyme R_FRUURtex_duplicate_2_enzyme R_FRUtex_duplicate_2_enzyme R_FUCtex_duplicate_2_enzyme R_FUMtex_duplicate_2_enzyme R_FUSAtex_duplicate_4_enzyme R_G1Ptex_duplicate_2_enzyme R_G3PCtex_duplicate_2_enzyme R_G3PEtex_duplicate_4_enzyme R_G3PGtex_duplicate_2_enzyme R_G3PItex_duplicate_2_enzyme R_G3PStex_duplicate_2_enzyme R_G6Ptex_duplicate_2_enzyme R_GAL1Ptex_duplicate_2_enzyme R_GALBDtex_duplicate_2_enzyme R_GALCTNLtex_duplicate_4_enzyme R_GALCTNtex_duplicate_2_enzyme R_GALCTtex_duplicate_2_enzyme R_GALTtex_duplicate_2_enzyme R_GALURtex_duplicate_2_enzyme R_GALtex_duplicate_2_enzyme R_GAMAN6Ptex_duplicate_2_enzyme R_GAMtex_duplicate_2_enzyme R_GBBTNtex_duplicate_2_enzyme R_GDPtex_duplicate_4_enzyme R_GLCNtex_duplicate_2_enzyme R_GLCRtex_duplicate_2_enzyme R_GLCUR1Ptex_duplicate_2_enzyme R_GLCURtex_duplicate_2_enzyme R_GLCtex_copy1_enzyme R_GLNtex_duplicate_2_enzyme R_GLUtex_duplicate_2_enzyme R_GLYALDtex_duplicate_2_enzyme R_GLYBtex_duplicate_2_enzyme R_GLYC2Ptex_duplicate_3_enzyme R_GLYC3Ptex_duplicate_2_enzyme R_GLYCAtex_duplicate_2_enzyme R_GLYCLTtex_duplicate_2_enzyme R_GLYCtex_duplicate_2_enzyme R_GLYtex_duplicate_2_enzyme R_GMPtex_enzyme R_GSNtex_duplicate_2_enzyme R_GTHOXtex_duplicate_2_enzyme R_GTHRDtex_duplicate_2_enzyme R_GTPtex_duplicate_2_enzyme R_H2O2tex_duplicate_2_enzyme R_H2Otex_duplicate_2_enzyme R_H2Stex_duplicate_2_enzyme R_H2tex_duplicate_2_enzyme R_HCINNMtex_duplicate_2_enzyme R_HG2tex_duplicate_2_enzyme R_HIStex_duplicate_2_enzyme R_HOMtex_duplicate_2_enzyme R_HPPPNtex_duplicate_4_enzyme R_HXAtex_duplicate_3_enzyme R_HYXNtex_duplicate_2_enzyme R_Htex_duplicate_4_enzyme R_IDONtex_duplicate_2_enzyme R_ILEtex_duplicate_2_enzyme R_IMPtex_duplicate_2_enzyme R_INDOLEtex_duplicate_2_enzyme R_INSTtex_duplicate_2_enzyme R_ISETACtex_duplicate_2_enzyme R_Ktex_duplicate_2_enzyme R_L_LACtex_duplicate_4_enzyme R_LALADGLUtex_enzyme R_LALALGLUtex_enzyme R_LCTStex_duplicate_2_enzyme R_LEUtex_duplicate_2_enzyme R_LIPOtex_duplicate_4_enzyme R_LYStex_duplicate_2_enzyme R_LYXtex_duplicate_2_enzyme R_MALDtex_enzyme R_MALtex_duplicate_2_enzyme R_MAN6Ptex_duplicate_2_enzyme R_MANGLYCtex_duplicate_2_enzyme R_MANtex_duplicate_2_enzyme R_MELIBtex_duplicate_2_enzyme R_MEOHtex_duplicate_4_enzyme R_METDtex_duplicate_2_enzyme R_METSOX1tex_duplicate_2_enzyme R_METSOX2tex_duplicate_2_enzyme R_METtex_duplicate_2_enzyme R_MG2tex_duplicate_2_enzyme R_MINCYCtex_duplicate_4_enzyme R_MMETtex_duplicate_2_enzyme R_MNLtex_duplicate_2_enzyme R_MNtex_duplicate_2_enzyme R_MOBDtex_duplicate_2_enzyme R_MSO3tex_duplicate_2_enzyme R_N2Otex_duplicate_2_enzyme R_NACtex_duplicate_2_enzyme R_NAtex_duplicate_2_enzyme R_NH4tex_duplicate_2_enzyme R_NI2tex_duplicate_2_enzyme R_NMNtex_duplicate_2_enzyme R_NO2tex_duplicate_2_enzyme R_NO3tex_duplicate_3_enzyme R_NOtex_duplicate_2_enzyme R_O2Stex_enzyme R_O2tex_duplicate_2_enzyme R_OCTAtex_duplicate_2_enzyme R_ORNtex_duplicate_2_enzyme R_OROTtex_duplicate_4_enzyme R_PACALDtex_duplicate_2_enzyme R_PEAMNtex_duplicate_2_enzyme R_PHEtex_duplicate_2_enzyme R_PItex_duplicate_2_enzyme R_PNTOtex_duplicate_2_enzyme R_PPALtex_duplicate_2_enzyme R_PPAtex_duplicate_4_enzyme R_PPPNtex_duplicate_2_enzyme R_PPTtex_duplicate_2_enzyme R_PROGLYtex_duplicate_2_enzyme R_PROtex_enzyme R_PSCLYStex_enzyme R_PSERtex_duplicate_2_enzyme R_PTRCtex_duplicate_2_enzyme R_PYDAMtex_duplicate_4_enzyme R_PYDXNtex_duplicate_4_enzyme R_PYDXtex_duplicate_4_enzyme R_PYRtex_duplicate_2_enzyme R_QUIN2tex_enzyme R_R5Ptex_duplicate_2_enzyme R_RIBtex_duplicate_2_enzyme R_RMNtex_duplicate_3_enzyme R_SBTtex_duplicate_2_enzyme R_SELtex_duplicate_4_enzyme R_SERtex_duplicate_2_enzyme R_SKMtex_duplicate_2_enzyme R_SLNTtex_duplicate_4_enzyme R_SO2tex_duplicate_2_enzyme R_SO3tex_duplicate_2_enzyme R_SO4tex_duplicate_2_enzyme R_SPMDtex_duplicate_2_enzyme R_SUCCtex_duplicate_2_enzyme R_SUCRtex_duplicate_2_enzyme R_SULFACtex_enzyme R_TARTRDtex_enzyme R_TARTRtex_duplicate_2_enzyme R_TAURtex_duplicate_2_enzyme R_TCYNTtex_duplicate_2_enzyme R_THMDtex_duplicate_2_enzyme R_THMtex_duplicate_2_enzyme R_THRPtex_duplicate_2_enzyme R_THRtex_duplicate_2_enzyme R_THYMtex_duplicate_4_enzyme R_TMAOtex_duplicate_2_enzyme R_TMAtex_duplicate_2_enzyme R_TREtex_duplicate_2_enzyme R_TRPtex_duplicate_2_enzyme R_TSULtex_duplicate_2_enzyme R_TTRCYCtex_duplicate_4_enzyme R_TUNGStex_enzyme R_TYMtex_duplicate_2_enzyme R_TYRPtex_duplicate_3_enzyme R_TYRtex_duplicate_2_enzyme R_UACGAMtex_duplicate_2_enzyme R_UDPACGALtex_duplicate_2_enzyme R_UDPGALtex_duplicate_2_enzyme R_UDPGLCURtex_duplicate_2_enzyme R_UDPGtex_duplicate_2_enzyme R_UMPtex_duplicate_4_enzyme R_URAtex_duplicate_2_enzyme R_UREAtex_duplicate_2_enzyme R_VALtex_duplicate_2_enzyme R_XANtex_duplicate_2_enzyme R_XMPtex_duplicate_2_enzyme R_XTSNtex_duplicate_2_enzyme R_XYLUtex_duplicate_2_enzyme R_XYLtex_duplicate_2_enzyme R_Zn2tex_duplicate_2_enzyme |
R_pqqtex R_12PPDRtex_duplicate_2 R_12PPDStex_duplicate_2 R_23CAMPtex_duplicate_2 R_23CCMPtex_duplicate_2 R_23CGMPtex_duplicate_2 R_23CUMPtex_duplicate_2 R_23DAPPAtex_duplicate_2 R_26DAHtex_duplicate_2 R_34dhpactex_duplicate_2 R_3AMPtex_duplicate_2 R_3CMPtex_duplicate_2 R_3GMPtex_duplicate_4 R_3HPPtex_duplicate_4 R_3PEPTtex_duplicate_2 R_3UMPtex_duplicate_2 R_4HOXPACDtex_duplicate_2 R_4PEPTtex_duplicate_2 R_5DGLCNtex_duplicate_2 R_5MTRtex_duplicate_4 R_ABUTtex_duplicate_2 R_ACACtex_duplicate_2 R_ACALDtex_duplicate_2 R_ACGAL1Ptex_duplicate_2 R_ACGALtex_duplicate_2 R_ACGAM1Ptex_duplicate_2 R_ACGAtex_duplicate_2 R_ACMANAtex_duplicate_2 R_ACMUMtex_duplicate_2 R_ACSERtex R_ACtex_duplicate_2 R_ADEtex_duplicate_2 R_AGMtex_duplicate_2 R_AKGtex_duplicate_2 R_ALAALAtex_duplicate_2 R_ALAtex_duplicate_2 R_ALLTNtex_duplicate_2 R_ALLtex_duplicate_2 R_AMPtex_duplicate_4 R_ANHGMtex_duplicate_2 R_ARBTtex R_ARBtex_duplicate_2 R_ARGtex_duplicate_2 R_ASCBtex_duplicate_2 R_ASNtex_duplicate_2 R_ASO3tex_duplicate_2 R_ASPtex_duplicate_2 R_BALAtex_duplicate_2 R_BTNtex R_BUTSO3tex_duplicate_2 R_BUTtex_duplicate_2 R_CA2tex_duplicate_2 R_CD2tex_duplicate_2 R_CGLYtex_duplicate_2 R_CHLtex_duplicate_2 R_CHTBStex_duplicate_4 R_CITtex_duplicate_2 R_CLtex_duplicate_2 R_CMPtex_duplicate_2 R_CMtex_duplicate_4 R_CO2tex_duplicate_2 R_COBALT2tex_duplicate_2 R_CRNDtex_duplicate_4 R_CRNtex_duplicate_2 R_CSNtex_duplicate_2 R_CU2tex_duplicate_3 R_CUtex_duplicate_2 R_CYANtex_duplicate_2 R_CYNTtex_duplicate_2 R_CYSDtex_duplicate_2 R_CYStex_duplicate_2 R_CYTDtex_duplicate_2 R_D_LACtex_duplicate_2 R_DALAtex_duplicate_2 R_DAMPtex_duplicate_2 R_DAPtex_duplicate_2 R_DCAtex_duplicate_2 R_DCMPtex_duplicate_2 R_DDGLCNtex_duplicate_4 R_DGMPtex_duplicate_2 R_DGSNtex_duplicate_2 R_DHAtex_duplicate_2 R_DIMPtex_duplicate_2 R_DINStex_duplicate_2 R_DMSOtex_duplicate_2 R_DMStex_duplicate_2 R_DOPAtex_duplicate_2 R_DOXRBCNtex_duplicate_4 R_DSERtex_duplicate_2 R_DTMPtex_duplicate_2 R_DUMPtex_duplicate_2 R_ETHAtex_duplicate_2 R_ETHSO3tex_duplicate_2 R_ETOHtex_duplicate_2 R_F6Ptex_duplicate_2 R_FALDtex_duplicate_2 R_FE2tex_duplicate_2 R_FE3tex_duplicate_2 R_FORtex_duplicate_2 R_FRULYStex_duplicate_2 R_FRUURtex_duplicate_2 R_FRUtex_duplicate_2 R_FUCtex_duplicate_2 R_FUMtex_duplicate_2 R_FUSAtex_duplicate_4 R_G1Ptex_duplicate_2 R_G3PCtex_duplicate_2 R_G3PEtex_duplicate_4 R_G3PGtex_duplicate_2 R_G3PItex_duplicate_2 R_G3PStex_duplicate_2 R_G6Ptex_duplicate_2 R_GAL1Ptex_duplicate_2 R_GALBDtex_duplicate_2 R_GALCTNLtex_duplicate_4 R_GALCTNtex_duplicate_2 R_GALCTtex_duplicate_2 R_GALTtex_duplicate_2 R_GALURtex_duplicate_2 R_GALtex_duplicate_2 R_GAMAN6Ptex_duplicate_2 R_GAMtex_duplicate_2 R_GBBTNtex_duplicate_2 R_GDPtex_duplicate_4 R_GLCNtex_duplicate_2 R_GLCRtex_duplicate_2 R_GLCUR1Ptex_duplicate_2 R_GLCURtex_duplicate_2 R_GLCtex_copy1 R_GLNtex_duplicate_2 R_GLUtex_duplicate_2 R_GLYALDtex_duplicate_2 R_GLYBtex_duplicate_2 R_GLYC2Ptex_duplicate_3 R_GLYC3Ptex_duplicate_2 R_GLYCAtex_duplicate_2 R_GLYCLTtex_duplicate_2 R_GLYCtex_duplicate_2 R_GLYtex_duplicate_2 R_GMPtex R_GSNtex_duplicate_2 R_GTHOXtex_duplicate_2 R_GTHRDtex_duplicate_2 R_GTPtex_duplicate_2 R_H2O2tex_duplicate_2 R_H2Otex_duplicate_2 R_H2Stex_duplicate_2 R_H2tex_duplicate_2 R_HCINNMtex_duplicate_2 R_HG2tex_duplicate_2 R_HIStex_duplicate_2 R_HOMtex_duplicate_2 R_HPPPNtex_duplicate_4 R_HXAtex_duplicate_3 R_HYXNtex_duplicate_2 R_Htex_duplicate_4 R_IDONtex_duplicate_2 R_ILEtex_duplicate_2 R_IMPtex_duplicate_2 R_INDOLEtex_duplicate_2 R_INSTtex_duplicate_2 R_ISETACtex_duplicate_2 R_Ktex_duplicate_2 R_L_LACtex_duplicate_4 R_LALADGLUtex R_LALALGLUtex R_LCTStex_duplicate_2 R_LEUtex_duplicate_2 R_LIPOtex_duplicate_4 R_LYStex_duplicate_2 R_LYXtex_duplicate_2 R_MALDtex R_MALtex_duplicate_2 R_MAN6Ptex_duplicate_2 R_MANGLYCtex_duplicate_2 R_MANtex_duplicate_2 R_MELIBtex_duplicate_2 R_MEOHtex_duplicate_4 R_METDtex_duplicate_2 R_METSOX1tex_duplicate_2 R_METSOX2tex_duplicate_2 R_METtex_duplicate_2 R_MG2tex_duplicate_2 R_MINCYCtex_duplicate_4 R_MMETtex_duplicate_2 R_MNLtex_duplicate_2 R_MNtex_duplicate_2 R_MOBDtex_duplicate_2 R_MSO3tex_duplicate_2 R_N2Otex_duplicate_2 R_NACtex_duplicate_2 R_NAtex_duplicate_2 R_NH4tex_duplicate_2 R_NI2tex_duplicate_2 R_NMNtex_duplicate_2 R_NO2tex_duplicate_2 R_NO3tex_duplicate_3 R_NOtex_duplicate_2 R_O2Stex R_O2tex_duplicate_2 R_OCTAtex_duplicate_2 R_ORNtex_duplicate_2 R_OROTtex_duplicate_4 R_PACALDtex_duplicate_2 R_PEAMNtex_duplicate_2 R_PHEtex_duplicate_2 R_PItex_duplicate_2 R_PNTOtex_duplicate_2 R_PPALtex_duplicate_2 R_PPAtex_duplicate_4 R_PPPNtex_duplicate_2 R_PPTtex_duplicate_2 R_PROGLYtex_duplicate_2 R_PROtex R_PSCLYStex R_PSERtex_duplicate_2 R_PTRCtex_duplicate_2 R_PYDAMtex_duplicate_4 R_PYDXNtex_duplicate_4 R_PYDXtex_duplicate_4 R_PYRtex_duplicate_2 R_QUIN2tex R_R5Ptex_duplicate_2 R_RIBtex_duplicate_2 R_RMNtex_duplicate_3 R_SBTtex_duplicate_2 R_SELtex_duplicate_4 R_SERtex_duplicate_2 R_SKMtex_duplicate_2 R_SLNTtex_duplicate_4 R_SO2tex_duplicate_2 R_SO3tex_duplicate_2 R_SO4tex_duplicate_2 R_SPMDtex_duplicate_2 R_SUCCtex_duplicate_2 R_SUCRtex_duplicate_2 R_SULFACtex R_TARTRDtex R_TARTRtex_duplicate_2 R_TAURtex_duplicate_2 R_TCYNTtex_duplicate_2 R_THMDtex_duplicate_2 R_THMtex_duplicate_2 R_THRPtex_duplicate_2 R_THRtex_duplicate_2 R_THYMtex_duplicate_4 R_TMAOtex_duplicate_2 R_TMAtex_duplicate_2 R_TREtex_duplicate_2 R_TRPtex_duplicate_2 R_TSULtex_duplicate_2 R_TTRCYCtex_duplicate_4 R_TUNGStex R_TYMtex_duplicate_2 R_TYRPtex_duplicate_3 R_TYRtex_duplicate_2 R_UACGAMtex_duplicate_2 R_UDPACGALtex_duplicate_2 R_UDPGALtex_duplicate_2 R_UDPGLCURtex_duplicate_2 R_UDPGtex_duplicate_2 R_UMPtex_duplicate_4 R_URAtex_duplicate_2 R_UREAtex_duplicate_2 R_VALtex_duplicate_2 R_XANtex_duplicate_2 R_XMPtex_duplicate_2 R_XTSNtex_duplicate_2 R_XYLUtex_duplicate_2 R_XYLtex_duplicate_2 R_Zn2tex_duplicate_2 |
351 | Secretion: 351.0, Translation: 351.0, Folding: 35.1 | 38,922 | UniprotID: P02932 | FUNCTION: Uptake of inorganic phosphate, phosphorylated compounds, and some other negatively charged solutes. | |
| b0243 | b0243 | Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase) (GSA dehydrogenase) | Cytoplasm | R_G5SD_enzyme | R_G5SD | 417 | Translation: 417.0, Folding: 41.7 | 44,630 | UniprotID: P07004 ECnumber: EC 1.2.1.41 |
FUNCTION: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate. {ECO:0000255|HAMAP-Rule:MF_00412, ECO:0000269|PubMed:7034716, ECO:0000269|PubMed:7035170}. | |
| b0242 | b0242 | Glutamate 5-kinase (EC 2.7.2.11) (Gamma-glutamyl kinase) (GK) | Cytoplasm | R_GLU5K_enzyme | R_GLU5K | 367 | Translation: 367.0, Folding: 36.7 | 39,057 | UniprotID: P0A7B5 ECnumber: EC 2.7.2.11 |
FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00456, ECO:0000269|PubMed:6319365}. | |
| b3256 | b3256 | Biotin carboxylase (EC 6.3.4.14) (Acetyl-CoA carboxylase subunit A) (ACC) (EC 6.4.1.2) | Cytoplasm | R_ACCOAC_enzyme | R_ACCOAC | 449 | Translation: 449.0, Folding: 44.9 | 49,321 | UniprotID: P24182 ECnumber: EC 6.3.4.14; 6.4.1.2 |
FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | |
| b0789 | b0789 | Cardiolipin synthase B (CL synthase) (EC 2.7.8.-) | Cell_inner_membrane | 413 | Secretion: 413.0, Translation: 413.0, Folding: 41.3 | 47,634 | UniprotID: P0AA84 ECnumber: EC 2.7.8.- |
FUNCTION: Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. Can also catalyze phosphatidyl group transfer to water to form phosphatidate. {ECO:0000255|HAMAP-Rule:MF_01917, ECO:0000269|PubMed:10634942, ECO:0000269|PubMed:22988102}. | |||
| b3447 | b3447 | Glutathione hydrolase proenzyme (EC 3.4.19.13) (Gamma-glutamyltranspeptidase proenzyme) (GGT) (EC 2.3.2.2) [Cleaved into: Glutathione hydrolase large chain; Glutathione hydrolase small chain | Periplasm | R_GTHRDHpp_enzyme | R_GTHRDHpp | 580 | Secretion: 580.0, Translation: 580.0, Folding: 58.0 | 61,768 | UniprotID: P18956 ECnumber: EC 3.4.19.13; 2.3.2.2 |
FUNCTION: Cleaves the gamma-glutamyl bond of periplasmic glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases; it may function in amino acid uptake/salvage, or possibly in peptidoglycan linkage. Catalyzes the hydrolysis and transpeptidation of many gamma-glutamyl compounds (including some D-gamma-glutamyl substrates), with a preference for basic and aromatic amino acids as acceptors (PubMed:2877974). The KM values for gamma-glutamyl acceptors are so high that it has been proposed transpeptidation is not the physiological role in E.coli (PubMed:2877974, PubMed:8104180). {ECO:0000269|PubMed:2877974, ECO:0000305|PubMed:8104180}. |
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| b3288 | b3288 | Methionyl-tRNA formyltransferase (EC 2.1.2.9) (Met-tRNA(fMet) formyltransferase) | Cytoplasm | R_FMETTRS_enzyme | R_FMETTRS | 315 | Translation: 315.0, Folding: 31.5 | 34,168 | UniprotID: P23882 ECnumber: EC 2.1.2.9 |
FUNCTION: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus. {ECO:0000255|HAMAP-Rule:MF_00182, ECO:0000269|PubMed:6989606, ECO:0000269|PubMed:8331078, ECO:0000269|PubMed:9843487}. |
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| b3281 | b3281 | Shikimate dehydrogenase (NADP(+)) (SD) (SDH) (EC 1.1.1.25) | Cytoplasm | R_SHK3Dr_duplicate_2_enzyme | R_SHK3Dr_duplicate_2 | 272 | Translation: 272.0, Folding: 27.2 | 29,414 | UniprotID: P15770 ECnumber: EC 1.1.1.25 |
FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It displays no activity in the presence of NAD. {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:12637497, ECO:0000269|PubMed:3883995}. | |
| b3519 | b3519 | Cytoplasmic trehalase (EC 3.2.1.28) (Alpha,alpha-trehalase) (Alpha,alpha-trehalose glucohydrolase) | Cytoplasm | R_TREH_enzyme | R_TREH | 549 | Translation: 549.0, Folding: 54.9 | 63,697 | UniprotID: P62601 ECnumber: EC 3.2.1.28 |
FUNCTION: Hydrolyzes trehalose to glucose. Could be involved, in cells returning to low osmolarity conditions, in the utilization of the accumulated cytoplasmic trehalose, which was synthesized in response to high osmolarity. | |
| b3040 | b3040 | Zinc transporter ZupT | Cell_inner_membrane | R_CD2tpp_enzyme R_COBALT2tpp_enzyme R_CU2tpp_enzyme R_FE2tpp_enzyme R_MN2tpp_enzyme R_ZN2tpp_enzyme |
R_CD2tpp R_COBALT2tpp R_CU2tpp R_FE2tpp R_MN2tpp R_ZN2tpp |
257 | Secretion: 257.0, Translation: 257.0, Folding: 25.7 | 26,485 | UniprotID: P0A8H3 | FUNCTION: Mediates zinc uptake. May also transport other divalent cations such as copper and cadmium ions. {ECO:0000269|PubMed:11790762}. | |
| b3041 | b3041 | 3,4-dihydroxy-2-butanone 4-phosphate synthase (DHBP synthase) (EC 4.1.99.12) | Cell_inner_membrane | R_DB4PS_enzyme | R_DB4PS | 217 | Secretion: 217.0, Translation: 217.0, Folding: 21.7 | 23,353 | UniprotID: P0A7J0 ECnumber: EC 4.1.99.12 |
FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate. | |
| b3266 | b3266 | Multidrug export protein AcrF (Acriflavine resistance protein F) (Protein EnvD) | Cell_inner_membrane | R_INDOLEt2pp_enzyme | R_INDOLEt2pp | 1034 | Secretion: 1034.0, Translation: 1034.0, Folding: 103.4 | 111,454 | UniprotID: P24181 | FUNCTION: Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. {ECO:0000269|PubMed:10518736, ECO:0000269|PubMed:11274125}. | |
| b3265 | b3265 | Multidrug export protein AcrE (Acriflavine resistance protein E) (Protein EnvC) | Cell_inner_membrane | R_INDOLEt2pp_enzyme | R_INDOLEt2pp | 385 | Secretion: 385.0, Translation: 385.0, Folding: 38.5 | 41,318 | UniprotID: P24180 | FUNCTION: Part of the tripartite efflux system AcrEF-TolC. Involved in the efflux of indole and organic solvents. {ECO:0000269|PubMed:10518736, ECO:0000269|PubMed:11274125}. | |
| b2393 | b2393 | Nucleoside permease NupC (Nucleoside-transport system protein NupC) | Cell_inner_membrane | 400 | Secretion: 400.0, Translation: 400.0, Folding: 40.0 | 43,476 | UniprotID: P0AFF2 | FUNCTION: Transports nucleosides with a high affinity except guanosine and deoxyguanosine. Driven by a proton motive force. Transports cytidine, uridine, thymidine, adenosine and inosine. Can also transport xanthosine, but with a very low affinity. {ECO:0000269|PubMed:11466294, ECO:0000269|PubMed:15678184, ECO:0000269|PubMed:374403}. | |||
| b2392 | b2392 | Divalent metal cation transporter MntH | Cell_inner_membrane | R_FE2t2pp_enzyme R_MNt2pp_enzyme |
R_FE2t2pp R_MNt2pp |
412 | Secretion: 412.0, Translation: 412.0, Folding: 41.2 | 44,194 | UniprotID: P0A769 | FUNCTION: H(+)-stimulated, divalent metal cation uptake system. Involved in manganese and iron uptake. Can also transport cadmium, cobalt, zinc and to a lesser extent nickel and copper. Involved in response to reactive oxygen. {ECO:0000255|HAMAP-Rule:MF_00221, ECO:0000269|PubMed:10712688, ECO:0000269|PubMed:10844693}. | |
| b2243 | b2243 | Anaerobic glycerol-3-phosphate dehydrogenase subunit C (G-3-P dehydrogenase) | Cell_inner_membrane | R_G3PD5_enzyme R_G3PD6_enzyme R_G3PD7_enzyme |
R_G3PD5 R_G3PD6 R_G3PD7 |
396 | Secretion: 396.0, Translation: 396.0, Folding: 39.6 | 44,108 | UniprotID: P0A996 | FUNCTION: Electron transfer protein; may also function as the membrane anchor for the GlpAB dimer. | |
| b2242 | b2242 | Anaerobic glycerol-3-phosphate dehydrogenase subunit B (Anaerobic G-3-P dehydrogenase subunit B) (Anaerobic G3Pdhase B) (EC 1.1.5.3) | Cell_inner_membrane | R_G3PD5_enzyme R_G3PD6_enzyme R_G3PD7_enzyme |
R_G3PD5 R_G3PD6 R_G3PD7 |
419 | Secretion: 419.0, Translation: 419.0, Folding: 41.9 | 45,357 | UniprotID: P13033 ECnumber: EC 1.1.5.3 |
FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. | |
| b2241 | b2241 | Anaerobic glycerol-3-phosphate dehydrogenase subunit A (G-3-P dehydrogenase) (EC 1.1.5.3) | Cell_inner_membrane | R_G3PD5_enzyme R_G3PD6_enzyme R_G3PD7_enzyme |
R_G3PD5 R_G3PD6 R_G3PD7 |
542 | Secretion: 542.0, Translation: 542.0, Folding: 54.2 | 58,958 | UniprotID: P0A9C0 ECnumber: EC 1.1.5.3 |
FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses fumarate or nitrate as electron acceptor. | |
| b2240 | b2240 | Glycerol-3-phosphate transporter (G-3-P transporter) (G-3-P permease) | Cell_inner_membrane | R_GLYC3Pt6pp_enzyme | R_GLYC3Pt6pp | 452 | Secretion: 452.0, Translation: 452.0, Folding: 45.2 | 50,310 | UniprotID: P08194 | FUNCTION: Responsible for glycerol-3-phosphate uptake. | |
| b3605 | b3605 | L-lactate dehydrogenase (EC 1.1.-.-) | Cell_inner_membrane | R_L_LACD2_enzyme R_L_LACD3_enzyme |
R_L_LACD2 R_L_LACD3 |
396 | Secretion: 396.0, Translation: 396.0, Folding: 39.6 | 42,728 | UniprotID: P33232 ECnumber: EC 1.1.-.- |
FUNCTION: Catalyzes the conversion of L-lactate to pyruvate. Seems to be a primary dehydrogenase in the respiratory chain. To a lesser extent, can also oxidize DL-alpha-hydroxybutyrate, but not D-lactate. {ECO:0000269|PubMed:18473, ECO:0000269|PubMed:8407843}. | |
| b3607 | b3607 | Serine acetyltransferase (SAT) (EC 2.3.1.30) | Cytoplasm | R_SERAT_enzyme | R_SERAT | 273 | Translation: 273.0, Folding: 27.3 | 29,317 | UniprotID: P0A9D4 ECnumber: EC 2.3.1.30 |
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| b3600 | b3600 | Mannitol-1-phosphate 5-dehydrogenase (EC 1.1.1.17) | Cytoplasm | R_M1PD_enzyme | R_M1PD | 382 | Translation: 382.0, Folding: 38.2 | 41,139 | UniprotID: P09424 ECnumber: EC 1.1.1.17 |
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| b3603 | b3603 | L-lactate permease | Cell_inner_membrane | R_D_LACt2pp_enzyme R_GLYCLTt2rpp_enzyme R_L_LACt2rpp_enzyme |
R_D_LACt2pp R_GLYCLTt2rpp R_L_LACt2rpp |
551 | Secretion: 551.0, Translation: 551.0, Folding: 55.1 | 59,168 | UniprotID: P33231 | FUNCTION: Transports L-lactate across the membrane. Can also transport D-lactate and glycolate. Seems to be driven by a proton motive force. | |
| b3608 | b3608 | Glycerol-3-phosphate dehydrogenase [NAD(P)+] (EC 1.1.1.94) (NAD(P)H-dependent glycerol-3-phosphate dehydrogenase) | Cytoplasm | R_G3PD2_enzyme | R_G3PD2 | 339 | Translation: 339.0, Folding: 33.9 | 36,362 | UniprotID: P0A6S7 ECnumber: EC 1.1.1.94 |
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| b2801 | b2801 | L-fucose-proton symporter (6-deoxy-L-galactose permease) (L-fucose permease) | Cell_inner_membrane | R_FUCtpp_enzyme | R_FUCtpp | 438 | Secretion: 438.0, Translation: 438.0, Folding: 43.8 | 47,545 | UniprotID: P11551 | FUNCTION: Mediates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Can also transport L-galactose and D-arabinose, but at reduced rates compared with L-fucose. Is not able to transport L-rhamnose and L-arabinose. {ECO:0000269|PubMed:2829831}. | |
| b1710 | b1710 | Thioredoxin/glutathione peroxidase BtuE (EC 1.11.1.15) (EC 1.11.1.9) | Periplasm | R_GTHPi_enzyme R_THIORDXi_duplicate_3_enzyme |
R_GTHPi R_THIORDXi_duplicate_3 |
183 | Secretion: 183.0, Translation: 183.0, Folding: 18.3 | 20,470 | UniprotID: P06610 ECnumber: EC 1.11.1.15; 1.11.1.9 |
FUNCTION: Non-specific peroxidase that can use thioredoxin or glutathione as a reducing agent. In vitro, utilizes preferentially thioredoxin A to decompose hydrogen peroxide as well as cumene-, tert-butyl-, and linoleic acid hydroperoxides, suggesting that it may have one or more organic hydroperoxide as its physiological substrate. {ECO:0000269|PubMed:20621065}. | |
| b2803 | b2803 | L-fuculokinase (EC 2.7.1.51) (L-fuculose kinase) | Cytoplasm | R_FCLK_enzyme | R_FCLK | 472 | Translation: 472.0, Folding: 47.2 | 52,259 | UniprotID: P11553 ECnumber: EC 2.7.1.51 |
FUNCTION: Catalyzes the phosphorylation of L-fuculose. Can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. {ECO:0000255|HAMAP-Rule:MF_00986, ECO:0000269|PubMed:13905785}. | |
| b2802 | b2802 | L-fucose isomerase (FucIase) (EC 5.3.1.25) (6-deoxy-L-galactose isomerase) (D-arabinose isomerase) (EC 5.3.1.3) | Cytoplasm | R_FCI_enzyme | R_FCI | 591 | Translation: 591.0, Folding: 59.1 | 64,977 | UniprotID: P69922 ECnumber: EC 5.3.1.25; 5.3.1.3 |
FUNCTION: Converts the aldose L-fucose into the corresponding ketose L-fuculose. Is also able to convert D-arabinose into D-ribulose, but this isomerase has a higher affinity for fucose and fuculose than for arabinose and ribulose, respectively. | |
| b1711 | b1711 | Vitamin B12 import system permease protein BtuC | Cell_inner_membrane | R_ADOCBLabcpp_enzyme R_CBIuabcpp_enzyme R_CBL1abcpp_enzyme |
R_ADOCBLabcpp R_CBIuabcpp R_CBL1abcpp |
326 | Secretion: 326.0, Translation: 326.0, Folding: 32.6 | 34,949 | UniprotID: P06609 | FUNCTION: Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane. | |
| b1245 | b1245 | Oligopeptide transport system permease protein OppC | Cell_inner_membrane | R_3PEPTabcpp_enzyme R_4PEPTabcpp_enzyme |
R_3PEPTabcpp R_4PEPTabcpp |
302 | Secretion: 302.0, Translation: 302.0, Folding: 30.2 | 33,022 | UniprotID: P0AFH6 | FUNCTION: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane. | |
| b3867 | b3867 | Oxygen-independent coproporphyrinogen III oxidase (CPO) (EC 1.3.98.3) (Coproporphyrinogen III dehydrogenase) (CPDH) | Cytoplasm | R_CPPPGO2_enzyme | R_CPPPGO2 | 457 | Translation: 457.0, Folding: 45.7 | 52,729 | UniprotID: P32131 ECnumber: EC 1.3.98.3 |
FUNCTION: Involved in the heme biosynthesis. Catalyzes the anaerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen III to yield the vinyl groups in protoporphyrinogen IX. It can use NAD or NADP, but NAD is preferred. {ECO:0000269|PubMed:12114526, ECO:0000269|PubMed:7768836}. | |
| b3860 | b3860 | Thiol:disulfide interchange protein DsbA | Periplasm | R_DSBAO1_enzyme R_DSBAO2_enzyme |
R_DSBAO1 R_DSBAO2 |
208 | Secretion: 208.0, Translation: 208.0, Folding: 20.8 | 23,105 | UniprotID: P0AEG4 | FUNCTION: Required for disulfide bond formation in some periplasmic proteins such as PhoA or OmpA. Acts by transferring its disulfide bond to other proteins and is reduced in the process. DsbA is reoxidized by DsbB. Required for pilus biogenesis. PhoP-regulated transcription is redox-sensitive, being activated when the periplasm becomes more reducing (deletion of dsbA/dsbB, treatment with dithiothreitol). MgrB acts between DsbA/DsbB and PhoP/PhoQ in this pathway. {ECO:0000269|PubMed:1429594, ECO:0000269|PubMed:22267510}. |
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| b0237 | b0237 | Cytosol non-specific dipeptidase (EC 3.4.13.18) (Aminoacyl-histidine dipeptidase) (Beta-alanyl-histidine dipeptidase) (Carnosinase) (Cysteinylglycinase) (Peptidase D) (Xaa-His dipeptidase) (X-His dipeptidase) | Cytoplasm | R_AMPTASECG_duplicate_2_enzyme R_AMPTASEPG_duplicate_3_enzyme R_LALGP_enzyme |
R_AMPTASECG_duplicate_2 R_AMPTASEPG_duplicate_3 R_LALGP |
485 | Translation: 485.0, Folding: 48.5 | 52,915 | UniprotID: P15288 ECnumber: EC 3.4.13.18 |
FUNCTION: Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also shows cysteinylglycinase activity, which is sufficient for E.coli to utilize cysteinylglycine as a cysteine source. {ECO:0000269|PubMed:11157967, ECO:0000269|PubMed:20067529, ECO:0000269|PubMed:355237, ECO:0000269|PubMed:7988883}. |
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| b3460 | b3460 | Leu/Ile/Val-binding protein (LIV-BP) | Periplasm | R_ALAabcpp_enzyme R_ILEabcpp_enzyme R_LEUabcpp_enzyme R_THRabcpp_enzyme R_VALabcpp_enzyme |
R_ALAabcpp R_ILEabcpp R_LEUabcpp R_THRabcpp R_VALabcpp |
367 | Secretion: 367.0, Translation: 367.0, Folding: 36.7 | 39,076 | UniprotID: P0AD96 | FUNCTION: This protein is a component of the leucine, isoleucine, valine, (threonine) transport system, which is one of the two periplasmic binding protein-dependent transport systems of the high-affinity transport of the branched-chain amino acids. | |
| b1493 | b1493 | Glutamate decarboxylase beta (GAD-beta) (EC 4.1.1.15) | Cytoplasm | R_GLUDC_duplicate_2_enzyme | R_GLUDC_duplicate_2 | 466 | Translation: 466.0, Folding: 46.6 | 52,668 | UniprotID: P69910 ECnumber: EC 4.1.1.15 |
FUNCTION: Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria. |
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| b0662 | b0662 | 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase (EC 1.14.13.-) | Cytoplasm | R_OMMBLHX_enzyme | R_OMMBLHX | 391 | Translation: 391.0, Folding: 39.1 | 42,953 | UniprotID: P75728 ECnumber: EC 1.14.13.- |
FUNCTION: Oxygenase that introduces the hydroxyl group at carbon five of 2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol resulting in the formation of 2-octaprenyl-3-methyl-5-hydroxy-6-methoxy-1,4-benzoquinol. | |
| b3469 | b3469 | Zinc/cadmium/lead-transporting P-type ATPase (EC 3.6.3.-) (EC 3.6.3.3) (EC 3.6.3.5) (Pb(II)/Cd(II)/Zn(II)-translocating ATPase) (Zn(2+)/Cd(2+)/Pb(2+) export ATPase) | Cell_inner_membrane | R_CD2abcpp R_COBALT2abcpp R_CU2abcpp R_HG2abcpp R_NI2abcpp R_ZN2abcpp |
732 | Secretion: 732.0, Translation: 732.0, Folding: 73.2 | 76,840 | UniprotID: P37617 ECnumber: EC 3.6.3.-; 3.6.3.3; 3.6.3.5 |
FUNCTION: Confers resistance to zinc, cadmium and lead (PubMed:9405611, PubMed:9364914, PubMed:9830000, PubMed:10660539, PubMed:17326661). Couples the hydrolysis of ATP with the export of zinc, cadmium or lead, with highest activity when the metals are present as metal-thiolate complexes (PubMed:9405611, PubMed:10660539, PubMed:17326661). Can also bind nickel, copper, cobalt and mercury (PubMed:10660539, PubMed:17326661). {ECO:0000269|PubMed:10660539, ECO:0000269|PubMed:17326661, ECO:0000269|PubMed:9364914, ECO:0000269|PubMed:9405611, ECO:0000269|PubMed:9830000}. |
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| b2738 | b2738 | 3-oxo-tetronate 4-phosphate decarboxylase (EC 4.1.1.104) | Cytoplasm | R_FCLPA_enzyme | R_FCLPA | 212 | Translation: 212.0, Folding: 21.2 | 23,222 | UniprotID: Q46890 ECnumber: EC 4.1.1.104 |
FUNCTION: Catalyzes the decarboxylation of 3-oxo-tetronate 4-phosphate to dihydroxyacetone phosphate (DHAP) and CO(2). {ECO:0000250|UniProtKB:A0A0H2VA12}. | |
| b2027 | b2027 | Chain length determinant protein (Polysaccharide antigen chain regulator) | Cell_inner_membrane | R_O16AP1pp_enzyme R_O16AP2pp_enzyme R_O16AP3pp_enzyme |
R_O16AP1pp R_O16AP2pp R_O16AP3pp |
326 | Secretion: 326.0, Translation: 326.0, Folding: 32.6 | 36,455 | UniprotID: P76372 | FUNCTION: Confers a modal distribution of chain length on the O-antigen component of lipopolysaccharide (LPS). Gives rise to a reduced number of short chain molecules and increases in numbers of longer molecules. | |
| b2026 | b2026 | Histidine biosynthesis bifunctional protein HisIE [Includes: Phosphoribosyl-AMP cyclohydrolase (PRA-CH) (EC 3.5.4.19); Phosphoribosyl-ATP pyrophosphatase (PRA-PH) (EC 3.6.1.31) | Cytoplasm | R_PRAMPC_enzyme R_PRATPP_enzyme |
R_PRAMPC R_PRATPP |
203 | Translation: 203.0, Folding: 20.3 | 22,756 | UniprotID: P06989 ECnumber: EC 3.5.4.19; 3.6.1.31 |
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| b2025 | b2025 | Imidazole glycerol phosphate synthase subunit HisF (EC 4.1.3.-) (IGP synthase cyclase subunit) (IGP synthase subunit HisF) (ImGP synthase subunit HisF) (IGPS subunit HisF) | Cytoplasm | R_IG3PS_enzyme | R_IG3PS | 258 | Translation: 258.0, Folding: 25.8 | 28,454 | UniprotID: P60664 ECnumber: EC 4.1.3.- |
FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisF subunit catalyzes the cyclization activity that produces IGP and AICAR from PRFAR using the ammonia provided by the HisH subunit. | |
| b2024 | b2024 | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase (EC 5.3.1.16) (Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase) | Cytoplasm | R_PRMICI_enzyme | R_PRMICI | 245 | Translation: 245.0, Folding: 24.5 | 26,033 | UniprotID: P10371 ECnumber: EC 5.3.1.16 |
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| b2023 | b2023 | Imidazole glycerol phosphate synthase subunit HisH (EC 2.4.2.-) (IGP synthase glutamine amidotransferase subunit) (IGP synthase subunit HisH) (ImGP synthase subunit HisH) (IGPS subunit HisH) | Cytoplasm | R_IG3PS_enzyme | R_IG3PS | 196 | Translation: 196.0, Folding: 19.6 | 21,653 | UniprotID: P60595 ECnumber: EC 2.4.2.- |
FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to IGP, AICAR and glutamate. The HisH subunit provides the glutamine amidotransferase activity that produces the ammonia necessary to HisF for the synthesis of IGP and AICAR. | |
| b2022 | b2022 | Histidine biosynthesis bifunctional protein HisB [Includes: Histidinol-phosphatase (EC 3.1.3.15); Imidazoleglycerol-phosphate dehydratase (IGPD) (EC 4.2.1.19) | Cytoplasm | R_HISTP_enzyme R_IGPDH_enzyme |
R_HISTP R_IGPDH |
355 | Translation: 355.0, Folding: 35.5 | 40,278 | UniprotID: P06987 ECnumber: EC 3.1.3.15; 4.2.1.19 |
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| b2021 | b2021 | Histidinol-phosphate aminotransferase (EC 2.6.1.9) (Imidazole acetol-phosphate transaminase) (HPAT) (HspAT) | Cytoplasm | R_HSTPT_enzyme | R_HSTPT | 356 | Translation: 356.0, Folding: 35.6 | 39,360 | UniprotID: P06986 ECnumber: EC 2.6.1.9 |
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| b2020 | b2020 | Histidinol dehydrogenase (HDH) (EC 1.1.1.23) | Cytoplasm | R_HISTD_enzyme | R_HISTD | 434 | Translation: 434.0, Folding: 43.4 | 46,110 | UniprotID: P06988 ECnumber: EC 1.1.1.23 |
FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine. {ECO:0000255|HAMAP-Rule:MF_01024}. | |
| b2029 | b2029 | 6-phosphogluconate dehydrogenase, decarboxylating (EC 1.1.1.44) | Cytoplasm | R_GND_enzyme | R_GND | 468 | Translation: 468.0, Folding: 46.8 | 51,481 | UniprotID: P00350 ECnumber: EC 1.1.1.44 |
FUNCTION: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. {ECO:0000269|PubMed:19686854}. | |
| b2028 | b2028 | UDP-glucose 6-dehydrogenase (UDP-Glc dehydrogenase) (UDP-GlcDH) (UDPGDH) (EC 1.1.1.22) | Cytoplasm | R_UDPGD_enzyme | R_UDPGD | 388 | Translation: 388.0, Folding: 38.8 | 43,657 | UniprotID: P76373 ECnumber: EC 1.1.1.22 |
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| b1611 | b1611 | Fumarate hydratase class II (Fumarase C) (EC 4.2.1.2) (Aerobic fumarase) (Iron-independent fumarase) | Cytoplasm | R_FUM_duplicate_3_enzyme | R_FUM_duplicate_3 | 467 | Translation: 467.0, Folding: 46.7 | 50,489 | UniprotID: P05042 ECnumber: EC 4.2.1.2 |
FUNCTION: Involved in the TCA cycle. FumC seems to be a backup enzyme for FumA under conditions of iron limitation and oxidative stress (PubMed:7592392). Catalyzes the stereospecific interconversion of fumarate to L-malate (PubMed:1917897, PubMed:3282546). {ECO:0000269|PubMed:1917897, ECO:0000269|PubMed:3282546, ECO:0000269|PubMed:7592392, ECO:0000305|PubMed:8496960}. | |
| b3952 | b3952 | Pyruvate formate-lyase 2-activating enzyme (EC 1.97.1.4) (Formate-C-acetyltransferase-activating enzyme 2) (PFL-activating enzyme 2) | Cytoplasm | R_PFL_enzyme | R_PFL | 292 | Translation: 292.0, Folding: 29.2 | 32,430 | UniprotID: P32675 ECnumber: EC 1.97.1.4 |
FUNCTION: Activation of pyruvate formate-lyase 2 under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5-deoxy-adenosine. {ECO:0000250}. | |
| b1613 | b1613 | Mannose-6-phosphate isomerase (EC 5.3.1.8) (Phosphohexomutase) (Phosphomannose isomerase) (PMI) | Cytoplasm | R_MAN6PI_enzyme | R_MAN6PI | 391 | Translation: 391.0, Folding: 39.1 | 42,850 | UniprotID: P00946 ECnumber: EC 5.3.1.8 |
FUNCTION: Involved in the conversion of glucose to GDP-L-fucose, which can be converted to L-fucose, a capsular polysaccharide. | |
| b1612 | b1612 | Fumarate hydratase class I, aerobic (EC 4.2.1.2) (Fumarase A) (Oxaloacetate keto--enol-isomerase) (OAAKE isomerase) (Oxaloacetate tautomerase) (EC 5.3.2.2) | Cytoplasm | R_FUM_duplicate_2_enzyme | R_FUM_duplicate_2 | 548 | Translation: 548.0, Folding: 54.8 | 60,299 | UniprotID: P0AC33 ECnumber: EC 4.2.1.2; 5.3.2.2 |
FUNCTION: Catalyzes the reversible hydration of fumarate to (S)-malate. Functions as an aerobic enzyme in the direction of malate formation as part of the citric acid cycle. Accounts for about 80% of the fumarase activity when the bacteria grow aerobically. To a lesser extent, also displays D-tartrate dehydratase activity in vitro, but is not able to convert (R)-malate, L-tartrate or meso-tartrate. Can also catalyze the isomerization of enol- to keto-oxaloacetate. {ECO:0000269|PubMed:1329945, ECO:0000269|PubMed:23405168, ECO:0000269|PubMed:3282546, ECO:0000269|PubMed:8422384, ECO:0000269|Ref.7}. |
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| b4367 | b4367 | Ferric iron reductase protein FhuF | Cytoplasm | R_FEOXAMR1_enzyme R_FEOXAMR2_enzyme R_FEOXAMR3_enzyme |
R_FEOXAMR1 R_FEOXAMR2 R_FEOXAMR3 |
262 | Translation: 262.0, Folding: 26.2 | 30,113 | UniprotID: P39405 | FUNCTION: Involved in the reduction of ferric iron in cytoplasmic ferrioxamine B. | |
| b1291 | b1291 | Putrescine export system ATP-binding protein SapD | Cell_inner_membrane | R_Kt2pp_enzyme R_Kt2pp_duplicate_2_enzyme |
R_Kt2pp R_Kt2pp_duplicate_2 |
330 | Secretion: 330.0, Translation: 330.0, Folding: 33.0 | 37,661 | UniprotID: P0AAH4 | FUNCTION: Part of a putrescine export transport system, does not play a role in resistance to antimicrobial peptides (PubMed:27803167). Stimulates K(+)-uptake proteins TrkG and TrkH to import K(+), may act via ATP-binding rather than ATP hydrolysis (PubMed:11700350). {ECO:0000269|PubMed:11700350, ECO:0000269|PubMed:27803167}. | |
| b1297 | b1297 | Gamma-glutamylputrescine synthetase PuuA (Gamma-Glu-Put synthetase) (EC 6.3.1.11) (Glutamate--putrescine ligase) | Cytoplasm | R_GGPTRCS_enzyme R_GLNS_duplicate_2_enzyme |
R_GGPTRCS R_GLNS_duplicate_2 |
472 | Translation: 472.0, Folding: 47.2 | 53,177 | UniprotID: P78061 ECnumber: EC 6.3.1.11 |
FUNCTION: Involved in the breakdown of putrescine via the biosynthesis of gamma-L-glutamylputrescine. It is able to use several diamines, spermidine and spermine. Absolutely essential to utilize putrescine as both nitrogen and carbon sources and to decrease the toxicity of putrescine, which can lead to inhibition of cell growth and protein synthesis. {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:18495664}. |
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| b1296 | b1296 | Putrescine importer PuuP | Cell_inner_membrane | R_PTRCt2pp_enzyme | R_PTRCt2pp | 461 | Secretion: 461.0, Translation: 461.0, Folding: 46.1 | 50,853 | UniprotID: P76037 | FUNCTION: Involved in the uptake of putrescine. {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:19181795, ECO:0000269|PubMed:27803167}. | |
| b1298 | b1298 | Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (Gamma-Glu-GABA hydrolase) (EC 3.5.1.94) | Cytoplasm | R_GGGABAH_enzyme | R_GGGABAH | 254 | Translation: 254.0, Folding: 25.4 | 28,013 | UniprotID: P76038 ECnumber: EC 3.5.1.94 |
FUNCTION: Involved in the breakdown of putrescine via hydrolysis of the gamma-glutamyl linkage of gamma-glutamyl-gamma-aminobutyrate. {ECO:0000269|PubMed:15590624, ECO:0000269|PubMed:16499623}. | |
| b1101 | b1101 | PTS system glucose-specific EIICB component (EIICB-Glc) (EII-Glc) [Includes: Glucose permease IIC component (PTS system glucose-specific EIIC component); Glucose-specific phosphotransferase enzyme IIB component (EC 2.7.1.199) (PTS system glucose-specific EIIB component) | Cell_inner_membrane | R_ACGAptspp_enzyme R_GLCptspp_enzyme |
R_ACGAptspp R_GLCptspp |
477 | Secretion: 477.0, Translation: 477.0, Folding: 47.7 | 50,677 | UniprotID: P69786 ECnumber: EC 2.7.1.199 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport (PubMed:3129430, PubMed:10562420). Also functions as a chemoreceptor monitoring the environment for changes in sugar concentration and an effector modulating the activity of the transcriptional repressor Mlc (PubMed:18319344). {ECO:0000269|PubMed:10562420, ECO:0000269|PubMed:18319344, ECO:0000269|PubMed:3129430}. |
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| b2423 | b2423 | Sulfate transport system permease protein CysW | Cell_inner_membrane | 291 | Secretion: 291.0, Translation: 291.0, Folding: 29.1 | 32,538 | UniprotID: P0AEB0 | FUNCTION: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane. | |||
| b1102 | b1102 | FhuE receptor (Outer-membrane receptor for Fe(III)-coprogen, Fe(III)-ferrioxamine B and Fe(III)-rhodotrulic acid) | Cell_outer_membrane | R_CPGNtonex_enzyme | R_CPGNtonex | 729 | Secretion: 729.0, Translation: 729.0, Folding: 72.9 | 81,233 | UniprotID: P16869 | FUNCTION: Required for the uptake of Fe(3+) via coprogen, ferrioxamine B, and rhodotorulic acid. | |
| b1107 | b1107 | Beta-hexosaminidase (EC 3.2.1.52) (Beta-N-acetylhexosaminidase) (N-acetyl-beta-glucosaminidase) | Cytoplasm | R_AGM3PH_enzyme R_AGM4PH_enzyme R_AGMH_enzyme |
R_AGM3PH R_AGM4PH R_AGMH |
341 | Translation: 341.0, Folding: 34.1 | 37,595 | UniprotID: P75949 ECnumber: EC 3.2.1.52 |
FUNCTION: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides. Cleaves GlcNAc linked beta-1,4 to MurNAc tripeptides. | |
| b2422 | b2422 | Sulfate/thiosulfate import ATP-binding protein CysA (EC 3.6.3.25) (Sulfate-transporting ATPase) | Cell_inner_membrane | 365 | Secretion: 365.0, Translation: 365.0, Folding: 36.5 | 41,059 | UniprotID: P16676 ECnumber: EC 3.6.3.25 |
FUNCTION: Part of the ABC transporter complex CysAWTP involved in sulfate/thiosulfate import. Responsible for energy coupling to the transport system. | |||
| b1109 | b1109 | NADH dehydrogenase (EC 1.6.99.3) | Cell_inner_membrane | R_NADH10_enzyme R_NADH5_enzyme R_NADH9_enzyme |
R_NADH10 R_NADH5 R_NADH9 |
434 | Secretion: 434.0, Translation: 434.0, Folding: 43.4 | 47,359 | UniprotID: P00393 ECnumber: EC 1.6.99.3 |
FUNCTION: Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Does not couple the redox reaction to proton translocation. | |
| b2421 | b2421 | Cysteine synthase B (CSase B) (EC 2.5.1.47) (O-acetylserine (thiol)-lyase B) (OAS-TL B) (O-acetylserine sulfhydrylase B) | Cytoplasm | R_CYSS_duplicate_2_enzyme | R_CYSS_duplicate_2 | 303 | Translation: 303.0, Folding: 30.3 | 32,664 | UniprotID: P16703 ECnumber: EC 2.5.1.47 |
FUNCTION: Two cysteine synthase enzymes are found. Both catalyze the same reaction. Cysteine synthase B can also use thiosulfate in place of sulfide to give cysteine thiosulfonate as a product. | |
| b4395 | b4395 | Probable phosphoglycerate mutase GpmB (EC 5.4.2.-) (PGAM) (Phosphoglyceromutase) | Cytoplasm | 215 | Translation: 215.0, Folding: 21.5 | 24,065 | UniprotID: P0A7A2 ECnumber: EC 5.4.2.- |
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| b4394 | b4394 | Non-canonical purine NTP phosphatase (EC 3.6.1.-) (Inosine triphosphatase) (ITPase) (Non-standard purine NTP phosphatase) (Nucleoside-triphosphate phosphatase) (NTPase) (Xanthosine triphosphatase) (XTPase) | Cytoplasm | R_NTP10_duplicate_2_enzyme R_NTP11_enzyme R_NTP12_enzyme |
R_NTP10_duplicate_2 R_NTP11 R_NTP12 |
170 | Translation: 170.0, Folding: 17.0 | 18,213 | UniprotID: P39411 ECnumber: EC 3.6.1.- |
FUNCTION: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA precursor pool, thus preventing their incorporation into DNA and avoiding chromosomal lesions. ITP is the best substrate, followed by XTP, GDP or dITP. Also implicated in the resistance against the thiamine metabolism inhibitors bacimethrin and CF3-HMP. {ECO:0000269|PubMed:16216582}. |
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| b4392 | b4392 | Soluble lytic murein transglycosylase (EC 4.2.2.n1) (Exomuramidase) (Peptidoglycan lytic exotransglycosylase) (Slt70) | Periplasm | R_MLTGY1pp_duplicate_2_enzyme R_MLTGY2pp_duplicate_5_enzyme R_MLTGY3pp_duplicate_5_enzyme R_MLTGY4pp_enzyme |
R_MLTGY1pp_duplicate_2 R_MLTGY2pp_duplicate_5 R_MLTGY3pp_duplicate_5 R_MLTGY4pp |
645 | Secretion: 645.0, Translation: 645.0, Folding: 64.5 | 73,353 | UniprotID: P0AGC3 ECnumber: EC 4.2.2.n1 |
FUNCTION: Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division. | |
| b4390 | b4390 | Trifunctional NAD biosynthesis/regulator protein NadR [Includes: Transcriptional regulator NadR; Nicotinamide mononucleotide adenylyltransferase (NMN adenylyltransferase) (NMN-AT) (NMNAT) (EC 2.7.7.1) (Nicotinamide ribonucleotide adenylyltransferase) (Nicotinamide-nucleotide adenylyltransferase); Ribosylnicotinamide kinase (RNK) (EC 2.7.1.22) (Nicotinamide riboside kinase) (NRK) (NmR-K) | Cell_inner_membrane | R_NMNAT_enzyme | R_NMNAT | 410 | Secretion: 410.0, Translation: 410.0, Folding: 41.0 | 47,346 | UniprotID: P27278 ECnumber: EC 2.7.7.1; 2.7.1.22 |
FUNCTION: This enzyme has three activities: DNA binding, nicotinamide mononucleotide (NMN) adenylyltransferase and ribosylnicotinamide (RN) kinase. The DNA-binding domain binds to the nadB operator sequence in an NAD- and ATP-dependent manner. As NAD levels increase within the cell, the affinity of NadR for the nadB operator regions of nadA, nadB, and pncB increases, repressing the transcription of these genes. The RN kinase activity catalyzes the phosphorylation of RN to form nicotinamide ribonucleotide. The NMN adenylyltransferase activity catalyzes the transfer of the AMP moiety of ATP to nicotinamide ribonucleotide to form NAD(+). The NMN adenylyltransferase domain also functions as the NAD and ATP sensor. {ECO:0000269|PubMed:10464228}. |
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| b1723 | b1723 | ATP-dependent 6-phosphofructokinase isozyme 2 (ATP-PFK 2) (Phosphofructokinase 2) (EC 2.7.1.11) (6-phosphofructokinase isozyme II) (Phosphohexokinase 2) | Cytoplasm | 309 | Translation: 309.0, Folding: 30.9 | 32,456 | UniprotID: P06999 ECnumber: EC 2.7.1.11 |
FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000269|PubMed:16866375}. | |||
| b2424 | b2424 | Sulfate transport system permease protein CysT | Cell_inner_membrane | 277 | Secretion: 277.0, Translation: 277.0, Folding: 27.7 | 30,292 | UniprotID: P16701 | FUNCTION: Part of the ABC transporter complex CysAWTP (TC 3.A.1.6.1) involved in sulfate/thiosulfate import. Probably responsible for the translocation of the substrate across the membrane. | |||
| b0418 | b0418 | Phosphatidylglycerophosphatase A (EC 3.1.3.27) (Phosphatidylglycerolphosphate phosphatase A) (PGP phosphatase A) | Cell_inner_membrane | 172 | Secretion: 172.0, Translation: 172.0, Folding: 17.2 | 19,418 | UniprotID: P18200 ECnumber: EC 3.1.3.27 |
FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). {ECO:0000269|PubMed:20485265, ECO:0000269|PubMed:21148555, ECO:0000269|PubMed:2846510, ECO:0000269|PubMed:6296050}. | |||
| b0414 | b0414 | Riboflavin biosynthesis protein RibD [Includes: Diaminohydroxyphosphoribosylaminopyrimidine deaminase (DRAP deaminase) (EC 3.5.4.26) (Riboflavin-specific deaminase); 5-amino-6-(5-phosphoribosylamino)uracil reductase (EC 1.1.1.193) (HTP reductase) | Cytoplasm | R_APRAUR_enzyme R_DHPPDA2_enzyme |
R_APRAUR R_DHPPDA2 |
367 | Translation: 367.0, Folding: 36.7 | 40,338 | UniprotID: P25539 ECnumber: EC 3.5.4.26; 1.1.1.193 |
FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5-phosphate. | |
| b0415 | b0415 | 6,7-dimethyl-8-ribityllumazine synthase (DMRL synthase) (LS) (Lumazine synthase) (EC 2.5.1.78) | Cytoplasm | R_RBFSb_enzyme | R_RBFSb | 156 | Translation: 156.0, Folding: 15.6 | 16,157 | UniprotID: P61714 ECnumber: EC 2.5.1.78 |
FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin. {ECO:0000269|PubMed:8969176}. | |
| b0417 | b0417 | Thiamine-monophosphate kinase (TMP kinase) (Thiamine-phosphate kinase) (EC 2.7.4.16) | Cytoplasm | R_TMPK_enzyme | R_TMPK | 325 | Translation: 325.0, Folding: 32.5 | 35,071 | UniprotID: P0AGG0 ECnumber: EC 2.7.4.16 |
FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. Cannot use thiamine as substrate. Is highly specific for ATP as phosphate donor. {ECO:0000269|PubMed:4567662, ECO:0000269|PubMed:6284709}. | |
| b0411 | b0411 | Nucleoside-specific channel-forming protein Tsx | Cell_outer_membrane | R_ADNtex R_DADNtex R_DCYTtex R_DURItex R_GUAtex R_INStex R_URItex |
294 | Secretion: 294.0, Translation: 294.0, Folding: 29.4 | 33,589 | UniprotID: P0A927 | FUNCTION: Functions as substrate-specific channel for nucleosides and deoxynucleosides (PubMed:791677, PubMed:3276691, PubMed:2458926). Has a greater affinity for deoxynucleosides than for nucleosides, and does not transport free bases (PubMed:2458926). In addition, constitutes the receptor for colicin K and phage T6 (PubMed:791677, PubMed:3276691). {ECO:0000269|PubMed:2458926, ECO:0000269|PubMed:3276691, ECO:0000269|PubMed:791677}. |
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| b4177 | b4177 | Adenylosuccinate synthetase (AMPSase) (AdSS) (EC 6.3.4.4) (IMP--aspartate ligase) | Cytoplasm | R_ADSS_enzyme | R_ADSS | 432 | Translation: 432.0, Folding: 43.2 | 47,345 | UniprotID: P0A7D4 ECnumber: EC 6.3.4.4 |
FUNCTION: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. | |
| b0521 | b0521 | Carbamate kinase (EC 2.7.2.2) | Cytoplasm | R_CBMKr_duplicate_2_enzyme | R_CBMKr_duplicate_2 | 297 | Translation: 297.0, Folding: 29.7 | 31,644 | UniprotID: P37306 ECnumber: EC 2.7.2.2 |
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| b0522 | b0522 | N5-carboxyaminoimidazole ribonucleotide synthase (N5-CAIR synthase) (EC 6.3.4.18) (5-(carboxyamino)imidazole ribonucleotide synthetase) | Cytoplasm | R_AIRC2_enzyme | R_AIRC2 | 355 | Translation: 355.0, Folding: 35.5 | 39,461 | UniprotID: P09029 ECnumber: EC 6.3.4.18 |
FUNCTION: Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR). {ECO:0000255|HAMAP-Rule:MF_01928, ECO:0000269|PubMed:8117684}. | |
| b0523 | b0523 | N5-carboxyaminoimidazole ribonucleotide mutase (N5-CAIR mutase) (EC 5.4.99.18) (5-(carboxyamino)imidazole ribonucleotide mutase) | Cytoplasm | R_AIRC3_enzyme | R_AIRC3 | 169 | Translation: 169.0, Folding: 16.9 | 17,780 | UniprotID: P0AG18 ECnumber: EC 5.4.99.18 |
FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929, ECO:0000269|PubMed:8117684}. | |
| b0524 | b0524 | UDP-2,3-diacylglucosamine hydrolase (EC 3.6.1.54) (UDP-2,3-diacylglucosamine diphosphatase) (UDP-2,3-diacylglucosamine pyrophosphatase) | Cell_inner_membrane | R_USHD_enzyme | R_USHD | 240 | Secretion: 240.0, Translation: 240.0, Folding: 24.0 | 26,894 | UniprotID: P43341 ECnumber: EC 3.6.1.54 |
FUNCTION: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom (PubMed:12000770). Involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell (PubMed:12000770, PubMed:12000771). Is essential for E.coli growth (PubMed:12000771). Does not cleave the unacylated UDP-GlcNAc, the mono-acylated UDP-3-O-(R)-3-hydroxymyristoyl-GlcNAc, and CDP-diacylglycerol (PubMed:12000770). {ECO:0000269|PubMed:12000770, ECO:0000269|PubMed:12000771}. |
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| b0526 | b0526 | Cysteine--tRNA ligase (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS) | Cytoplasm | R_CYSTRS_enzyme | R_CYSTRS | 461 | Translation: 461.0, Folding: 46.1 | 52,202 | UniprotID: P21888 ECnumber: EC 6.1.1.16 |
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| b0529 | b0529 | Bifunctional protein FolD [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9) | Cytoplasm | R_MTHFC_enzyme R_MTHFD_enzyme |
R_MTHFC R_MTHFD |
288 | Translation: 288.0, Folding: 28.8 | 31,044 | UniprotID: P24186 ECnumber: EC 1.5.1.5; 3.5.4.9 |
FUNCTION: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate. This enzyme is specific for NADP. {ECO:0000255|HAMAP-Rule:MF_01576, ECO:0000269|PubMed:1748668}. | |
| b2223 | b2223 | Putative short-chain fatty acid transporter | Cell_inner_membrane | R_ACACt2pp_enzyme R_BUTt2rpp_enzyme R_HEXt2rpp_enzyme |
R_ACACt2pp R_BUTt2rpp R_HEXt2rpp |
440 | Secretion: 440.0, Translation: 440.0, Folding: 44.0 | 47,528 | UniprotID: P76460 | FUNCTION: May be responsible for the uptake of short-chain fatty acids. | |
| b3073 | b3073 | Putrescine aminotransferase (EC 2.6.1.82) (Putrescine--2-oxoglutaric acid transaminase) (PAT) (PATase) | Cytoplasm | R_PTRCTA_enzyme | R_PTRCTA | 459 | Translation: 459.0, Folding: 45.9 | 49,661 | UniprotID: P42588 ECnumber: EC 2.6.1.82 |
FUNCTION: Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. Is also able to transaminate cadaverine and, in lower extent, spermidine, but not ornithine. Alpha-ketobutyrate and pyruvate can also act as amino acceptors, although much less efficiently. {ECO:0000269|PubMed:12617754}. |
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| b2388 | b2388 | Glucokinase (EC 2.7.1.2) (Glucose kinase) | Cytoplasm | R_HEX1_enzyme | R_HEX1 | 321 | Translation: 321.0, Folding: 32.1 | 34,723 | UniprotID: P0A6V8 ECnumber: EC 2.7.1.2 |
FUNCTION: Not highly important in E.coli as glucose is transported into the cell by the PTS system already as glucose 6-phosphate. | |
| b3709 | b3709 | Low affinity tryptophan permease | Cell_inner_membrane | R_TRPt2rpp_duplicate_3_enzyme | R_TRPt2rpp_duplicate_3 | 415 | Secretion: 415.0, Translation: 415.0, Folding: 41.5 | 45,211 | UniprotID: P23173 | FUNCTION: Involved in tryptophan transport across the cytoplasmic membrane. Plays a role in transporting tryptophan which is to be used catabolically. | |
| b3708 | b3708 | Tryptophanase (EC 4.1.99.1) (L-tryptophan indole-lyase) (TNase) | Cytoplasm | R_CYSDS_enzyme R_SERD_L_duplicate_4_enzyme R_TRPAS2_enzyme |
R_CYSDS R_SERD_L_duplicate_4 R_TRPAS2 |
471 | Translation: 471.0, Folding: 47.1 | 52,773 | UniprotID: P0A853 ECnumber: EC 4.1.99.1 |
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| b3255 | b3255 | Biotin carboxyl carrier protein of acetyl-CoA carboxylase (BCCP) | Cytoplasm | R_ACCOAC_enzyme | R_ACCOAC | 156 | Translation: 156.0, Folding: 15.6 | 16,687 | UniprotID: P0ABD8 | FUNCTION: This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. {ECO:0000269|PubMed:4934522}. | |
| b3258 | b3258 | Sodium/pantothenate symporter (Pantothenate permease) | Cell_inner_membrane | R_PNTOt4pp_enzyme | R_PNTOt4pp | 483 | Secretion: 483.0, Translation: 483.0, Folding: 48.3 | 51,717 | UniprotID: P16256 | FUNCTION: Catalyzes the sodium-dependent uptake of extracellular pantothenate. | |
| b2258 | b2258 | Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF (L-Ara4N-phosphoundecaprenol flippase subunit ArnF) (Undecaprenyl phosphate-aminoarabinose flippase subunit ArnF) | Cell_inner_membrane | R_ULA4Ntppi_enzyme | R_ULA4Ntppi | 128 | Secretion: 128.0, Translation: 128.0, Folding: 12.8 | 14,085 | UniprotID: P76474 | FUNCTION: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane. {ECO:0000269|PubMed:17928292}. | |
| b3380 | b3380 | Uncharacterized protein YhfW | Cytoplasm | R_PPM_enzyme | R_PPM | 408 | Translation: 408.0, Folding: 40.8 | 44,560 | UniprotID: P45549 | ||
| b3385 | b3385 | Phosphoglycolate phosphatase (PGP) (PGPase) (EC 3.1.3.18) | Cytoplasm | R_PGLYCP_enzyme | R_PGLYCP | 252 | Translation: 252.0, Folding: 25.2 | 27,389 | UniprotID: P32662 ECnumber: EC 3.1.3.18 |
FUNCTION: Specifically catalyzes the dephosphorylation of 2-phosphoglycolate (2P-Gly). Is involved in the dissimilation of the intracellular 2-phosphoglycolate formed during the DNA repair of 3-phosphoglycolate ends, a major class of DNA lesions induced by oxidative stress. {ECO:0000269|PubMed:16990279}. | |
| b3384 | b3384 | Tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (TrpRS) | Cytoplasm | R_TRPTRS_enzyme | R_TRPTRS | 334 | Translation: 334.0, Folding: 33.4 | 37,438 | UniprotID: P00954 ECnumber: EC 6.1.1.2 |
FUNCTION: Amino acylates tRNA(Trp) with both L- and D-tryptophan, although D-tryptophan is a poor substrate (PubMed:10918062). {ECO:0000269|PubMed:10918062}. | |
| b3386 | b3386 | Ribulose-phosphate 3-epimerase (EC 5.1.3.1) (Pentose-5-phosphate 3-epimerase) (PPE) (R5P3E) | Cytoplasm | R_RPE_duplicate_2_enzyme | R_RPE_duplicate_2 | 225 | Translation: 225.0, Folding: 22.5 | 24,554 | UniprotID: P0AG07 ECnumber: EC 5.1.3.1 |
FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5-phosphate to D-xylulose 5-phosphate. {ECO:0000269|PubMed:21402925}. | |
| b3389 | b3389 | 3-dehydroquinate synthase (DHQS) (EC 4.2.3.4) | Cytoplasm | R_DHQS_enzyme | R_DHQS | 362 | Translation: 362.0, Folding: 36.2 | 38,881 | UniprotID: P07639 ECnumber: EC 4.2.3.4 |
FUNCTION: Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ). {ECO:0000255|HAMAP-Rule:MF_00110, ECO:0000269|PubMed:2514789}. | |
| b2251 | b2251 | Nucleoside triphosphatase NudI (EC 3.6.1.9) (Nucleotide diphosphatase NudI) (Pyrimidine deoxynucleoside triphosphate diphosphatase) (dCTP diphosphatase) (EC 3.6.1.12) (dTTP diphosphatase) (EC 3.6.1.-) (dUTP diphosphatase) (EC 3.6.1.23) | Cytoplasm | R_DUTPDP_duplicate_2_enzyme R_NTPP3_enzyme R_NTPP7_duplicate_2_enzyme |
R_DUTPDP_duplicate_2 R_NTPP3 R_NTPP7_duplicate_2 |
141 | Translation: 141.0, Folding: 14.1 | 16,371 | UniprotID: P52006 ECnumber: EC 3.6.1.9; 3.6.1.12; 3.6.1.-; 3.6.1.23 |
FUNCTION: Catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP). {ECO:0000269|PubMed:16766526}. | |
| b2253 | b2253 | UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase (EC 2.6.1.87) (Polymyxin resistance protein PmrH) (UDP-(beta-L-threo-pentapyranosyl-4-ulose diphosphate) aminotransferase) (UDP-Ara4O aminotransferase) (UDP-4-amino-4-deoxy-L-arabinose aminotransferase) | Cytoplasm | R_UDPKAAT_enzyme | R_UDPKAAT | 385 | Translation: 385.0, Folding: 38.5 | 42,238 | UniprotID: P77690 ECnumber: EC 2.6.1.87 |
FUNCTION: Catalyzes the conversion of UDP-4-keto-arabinose (UDP-Ara4O) to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. {ECO:0000269|PubMed:12704196}. | |
| b2254 | b2254 | Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase (EC 2.4.2.53) (Polymyxin resistance protein PmrF) (Undecaprenyl-phosphate Ara4FN transferase) (Ara4FN transferase) | Cell_inner_membrane | R_UPLA4FNT_enzyme | R_UPLA4FNT | 322 | Secretion: 322.0, Translation: 322.0, Folding: 32.2 | 36,339 | UniprotID: P77757 ECnumber: EC 2.4.2.53 |
FUNCTION: Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. {ECO:0000269|PubMed:11706007}. | |
| b2255 | b2255 | Bifunctional polymyxin resistance protein ArnA (Polymyxin resistance protein PmrI) [Includes: UDP-4-amino-4-deoxy-L-arabinose formyltransferase (EC 2.1.2.13) (ArnAFT) (UDP-L-Ara4N formyltransferase); UDP-glucuronic acid oxidase UDP-4-keto-hexauronic acid decarboxylating (EC 1.1.1.305) (ArnADH) (UDP-GlcUA decarboxylase) (UDP-glucuronic acid dehydrogenase) | Cytoplasm | R_UDPGDC_enzyme R_ULA4NFT_enzyme |
R_UDPGDC R_ULA4NFT |
660 | Translation: 660.0, Folding: 66.0 | 74,289 | UniprotID: P77398 ECnumber: EC 2.1.2.13; 1.1.1.305 |
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| b2256 | b2256 | Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD (EC 3.5.1.n3) | Cytoplasm | R_UPLA4FNF_enzyme | R_UPLA4FNF | 296 | Translation: 296.0, Folding: 29.6 | 33,112 | UniprotID: P76472 ECnumber: EC 3.5.1.n3 |
FUNCTION: Catalyzes the deformylation of 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol to 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides (Probable). {ECO:0000305|PubMed:15695810}. | |
| b2257 | b2257 | Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase (EC 2.4.2.43) (4-amino-4-deoxy-L-arabinose lipid A transferase) (Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase) (Polymyxin resistance protein PmrK) (Undecaprenyl phosphate-alpha-L-Ara4N transferase) | Cell_inner_membrane | R_LA4NTpp_enzyme | R_LA4NTpp | 550 | Secretion: 550.0, Translation: 550.0, Folding: 55.0 | 62,543 | UniprotID: P76473 ECnumber: EC 2.4.2.43 |
FUNCTION: Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. {ECO:0000269|PubMed:11535604}. | |
| b3671 | b3671 | Acetolactate synthase isozyme 1 large subunit (AHAS-I) (EC 2.2.1.6) (Acetohydroxy-acid synthase I large subunit) (ALS-I) | Cytoplasm | R_ACHBS_enzyme R_ACLS_enzyme |
R_ACHBS R_ACLS |
562 | Translation: 562.0, Folding: 56.2 | 60,441 | UniprotID: P08142 ECnumber: EC 2.2.1.6 |
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| b3670 | b3670 | Acetolactate synthase isozyme 1 small subunit (EC 2.2.1.6) (Acetohydroxy-acid synthase I small subunit) (AHAS-I) (ALS-I) | Cytoplasm | R_ACHBS_enzyme R_ACLS_enzyme |
R_ACHBS R_ACLS |
96 | Translation: 96.0, Folding: 9.6 | 11,106 | UniprotID: P0ADF8 ECnumber: EC 2.2.1.6 |
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| b3679 | b3679 | Uncharacterized symporter YidK | Cell_inner_membrane | R_INOSTt4pp_enzyme | R_INOSTt4pp | 571 | Secretion: 571.0, Translation: 571.0, Folding: 57.1 | 62,085 | UniprotID: P31448 | ||
| b2813 | b2813 | Membrane-bound lytic murein transglycosylase A (EC 4.2.2.n1) (Mlt38) (Murein hydrolase A) | Cell_outer_membrane | R_MLTGY1pp_duplicate_5_enzyme R_MLTGY2pp_enzyme R_MLTGY3pp_enzyme R_MLTGY4pp_duplicate_6_enzyme |
R_MLTGY1pp_duplicate_5 R_MLTGY2pp R_MLTGY3pp R_MLTGY4pp_duplicate_6 |
365 | Secretion: 365.0, Translation: 365.0, Folding: 36.5 | 40,411 | UniprotID: P0A935 ECnumber: EC 4.2.2.n1 |
FUNCTION: Murein-degrading enzyme. May play a role in recycling of muropeptides during cell elongation and/or cell division. Degrades murein glycan strands and insoluble, high-molecular weight murein sacculi. | |
| b2810 | b2810 | Cysteine desulfurase CsdA (EC 2.8.1.7) (Cysteine sulfinate desulfinase) (CSD) (EC 4.4.1.-) (Selenocysteine lyase) (EC 4.4.1.16) | Cytoplasm | R_CYSSADS_enzyme | R_CYSSADS | 401 | Translation: 401.0, Folding: 40.1 | 43,234 | UniprotID: Q46925 ECnumber: EC 2.8.1.7; 4.4.1.-; 4.4.1.16 |
FUNCTION: Catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine, and transiently retains the released sulfur atom on a cysteine residue, in the form of a persulfide. Can also desulfinate L-cysteine sulfinate, which is the best substrate of the enzyme. Functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Seems to participate in Fe/S biogenesis by recruiting the SufBCD-SufE proteins. Transfers sulfur to CsdE that increases the cysteine desulfurase activity of CsdA. Can also transfer sulfur directly to TcdA/CsdL in vitro. Appears to support the function of TcdA in the generation of cyclic threonylcarbamoyladenosine at position 37 (ct(6)A37) in tRNAs that read codons beginning with adenine. {ECO:0000269|PubMed:10829016, ECO:0000269|PubMed:15901727, ECO:0000269|PubMed:20054882, ECO:0000269|PubMed:23242255, ECO:0000269|PubMed:9278392}. |
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| b2817 | b2817 | N-acetylmuramoyl-L-alanine amidase AmiC (EC 3.5.1.28) | Periplasm | R_AGM3PApp_enzyme R_AGM4PApp_enzyme |
R_AGM3PApp R_AGM4PApp |
417 | Secretion: 417.0, Translation: 417.0, Folding: 41.7 | 45,634 | UniprotID: P63883 ECnumber: EC 3.5.1.28 |
FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors. {ECO:0000269|PubMed:11454209, ECO:0000269|PubMed:18390656}. | |
| b2818 | b2818 | Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGS) (NAGS) | Cytoplasm | R_ACGS_enzyme | R_ACGS | 443 | Translation: 443.0, Folding: 44.3 | 49,195 | UniprotID: P0A6C5 ECnumber: EC 2.3.1.1 |
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| b3816 | b3816 | Magnesium transport protein CorA | Cell_inner_membrane | R_COBALT2tpp_duplicate_2_enzyme R_MG2tpp_enzyme R_NI2tpp_enzyme |
R_COBALT2tpp_duplicate_2 R_MG2tpp R_NI2tpp |
316 | Secretion: 316.0, Translation: 316.0, Folding: 31.6 | 36,590 | UniprotID: P0ABI4 | FUNCTION: Mediates influx of magnesium ions. Can also mediate cobalt and manganese uptake (PubMed:780341). Alternates between open and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+) levels are high (By similarity). {ECO:0000250|UniProtKB:Q9WZ31, ECO:0000269|PubMed:780341}. | |
| b3496 | b3496 | Dipeptide and tripeptide permease B | Cell_inner_membrane | R_LALADGLUtpp_duplicate_3_enzyme R_LALALGLUtpp_duplicate_3_enzyme |
R_LALADGLUtpp_duplicate_3 R_LALALGLUtpp_duplicate_3 |
489 | Secretion: 489.0, Translation: 489.0, Folding: 48.9 | 53,575 | UniprotID: P36837 | FUNCTION: Proton-dependent permease that transports di- and tripeptides. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate. {ECO:0000269|PubMed:18485005}. | |
| b3493 | b3493 | Low-affinity inorganic phosphate transporter 1 | Cell_inner_membrane | R_PIt2rpp_duplicate_2_enzyme | R_PIt2rpp_duplicate_2 | 499 | Secretion: 499.0, Translation: 499.0, Folding: 49.9 | 53,389 | UniprotID: P0AFJ7 | FUNCTION: Low-affinity inorganic phosphate transport. Can also transport arsenate. | |
| b2724 | b2724 | Formate hydrogenlyase subunit 2 (FHL subunit 2) (Hydrogenase-3 component B) | Cytoplasm | R_FHL_duplicate_2_enzyme R_HYD1pp_duplicate_3_enzyme |
R_FHL_duplicate_2 R_HYD1pp_duplicate_3 |
203 | Translation: 203.0, Folding: 20.3 | 21,873 | UniprotID: P0AAK1 | FUNCTION: Probable electron transfer protein for hydrogenase 3. | |
| b2720 | b2720 | Formate hydrogenlyase subunit 6 (FHL subunit 6) (Hydrogenase-3 component F) | Cytoplasm | R_FHL_duplicate_2_enzyme R_HYD1pp_duplicate_3_enzyme |
R_FHL_duplicate_2 R_HYD1pp_duplicate_3 |
180 | Translation: 180.0, Folding: 18.0 | 20,309 | UniprotID: P16432 | FUNCTION: Probable electron transfer protein for hydrogenase 3. | |
| b2721 | b2721 | Formate hydrogenlyase subunit 5 (FHL subunit 5) (Hydrogenase-3 component E) | Cytoplasm | R_FHL_duplicate_2_enzyme R_HYD1pp_duplicate_3_enzyme |
R_FHL_duplicate_2 R_HYD1pp_duplicate_3 |
569 | Translation: 569.0, Folding: 56.9 | 64,980 | UniprotID: P16431 | ||
| b2722 | b2722 | Formate hydrogenlyase subunit 4 (FHL subunit 4) (Hydrogenase 3 component D) | Cell_inner_membrane | R_FHL_duplicate_2_enzyme R_HYD1pp_duplicate_3_enzyme |
R_FHL_duplicate_2 R_HYD1pp_duplicate_3 |
307 | Secretion: 307.0, Translation: 307.0, Folding: 30.7 | 33,029 | UniprotID: P16430 | ||
| b2723 | b2723 | Formate hydrogenlyase subunit 3 (FHL subunit 3) (Hydrogenase-3 component C) | Cell_inner_membrane | R_FHL_duplicate_2_enzyme R_HYD1pp_duplicate_3_enzyme |
R_FHL_duplicate_2 R_HYD1pp_duplicate_3 |
608 | Secretion: 608.0, Translation: 608.0, Folding: 60.8 | 64,077 | UniprotID: P16429 | ||
| b3925 | b3925 | Fructose-1,6-bisphosphatase 1 class 2 (FBPase 1 class 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1 class 2) | Cytoplasm | R_FBP_duplicate_2_enzyme | R_FBP_duplicate_2 | 336 | Translation: 336.0, Folding: 33.6 | 35,852 | UniprotID: P0A9C9 ECnumber: EC 3.1.3.11 |
FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Is likely to be involved in gluconeogenesis during growth on glycerol. Also displays a low activity toward glucose 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate, fructose 2,6-bisphosphate, or fructose 1-phosphate. {ECO:0000269|PubMed:10986273, ECO:0000269|PubMed:19073594}. | |
| b3924 | b3924 | Flavodoxin/ferredoxin--NADP reductase (EC 1.18.1.2) (EC 1.19.1.1) (Ferredoxin (flavodoxin):NADP(+) oxidoreductase) (Ferredoxin--NADP reductase) (FNR) (Flavodoxin--NADP reductase) (FLDR) (Methyl viologen resistance protein A) (dA1) | Cytoplasm | 248 | Translation: 248.0, Folding: 24.8 | 27,751 | UniprotID: P28861 ECnumber: EC 1.18.1.2; 1.19.1.1 |
FUNCTION: Transports electrons between flavodoxin or ferredoxin and NADPH (PubMed:8449868, PubMed:9839946, PubMed:12234497, PubMed:21306142). Reduces flavodoxin 1, flavodoxin 2 and ferredoxin, ferredoxin being the kinetically and thermodynamically preferred partner (PubMed:12234497). Required for the activation of several enzymes such as pyruvate formate-lyase, anaerobic ribonucleotide reductase and cobalamin-dependent methionine synthase (PubMed:7042345, PubMed:8267617). {ECO:0000269|PubMed:12234497, ECO:0000269|PubMed:21306142, ECO:0000269|PubMed:7042345, ECO:0000269|PubMed:8267617, ECO:0000269|PubMed:8449868, ECO:0000269|PubMed:9839946}. |
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| b3927 | b3927 | Glycerol uptake facilitator protein (Aquaglyceroporin) | Cell_inner_membrane | R_GLYALDtpp_enzyme R_GLYCtpp_enzyme R_UREAtpp_enzyme |
R_GLYALDtpp R_GLYCtpp R_UREAtpp |
281 | Secretion: 281.0, Translation: 281.0, Folding: 28.1 | 29,780 | UniprotID: P0AER0 | FUNCTION: Transporter of glycerol across the cytoplasmic membrane, with limited permeability to water and small uncharged compounds such as polyols. | |
| b3926 | b3926 | Glycerol kinase (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) (Glycerokinase) (GK) | Cytoplasm | R_GLYK_enzyme | R_GLYK | 502 | Translation: 502.0, Folding: 50.2 | 56,231 | UniprotID: P0A6F3 ECnumber: EC 2.7.1.30 |
FUNCTION: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:2826434, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908}. | |
| b2032 | b2032 | Putative glycosyltransferase WbbK | Cell_inner_membrane | R_O16GLCT1_enzyme | R_O16GLCT1 | 372 | Secretion: 372.0, Translation: 372.0, Folding: 37.2 | 43,188 | UniprotID: P37751 | FUNCTION: May be a glycosyltransferase involved in the transfer of UDP-GalF and UDP-glucose. | |
| b2033 | b2033 | Putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ (EC 2.3.1.-) | Cytoplasm | R_O16AT_enzyme | R_O16AT | 196 | Translation: 196.0, Folding: 19.6 | 21,675 | UniprotID: P37750 ECnumber: EC 2.3.1.- |
FUNCTION: Putative O-acetyltransferase that transfers an O-acetyl group to the O antigen. | |
| b2034 | b2034 | Beta-1,6-galactofuranosyltransferase WbbI (EC 2.4.1.-) (D-Galf:alpha-D-Glc beta-1,6-galactofuranosyltransferase) (GalF transferase) | Cytoplasm | R_O16GALFT_enzyme | R_O16GALFT | 330 | Translation: 330.0, Folding: 33.0 | 37,757 | UniprotID: P37749 ECnumber: EC 2.4.1.- |
FUNCTION: Involved in the transfer of galactofuranose (Galf) onto an alpha-D-gluco-configured acceptor substrate to form a beta-1,6-linkage. It uses n-octyl alpha-D-glucopyranoside as an acceptor substrate for the addition of galactofuranose from the donor substrate UDP-galactofuranose. It is not able to use beta-D-glucopyranoside isomers. {ECO:0000269|PubMed:17047874}. | |
| b2035 | b2035 | O-antigen polymerase | Cell_inner_membrane | R_O16AP1pp_enzyme R_O16AP2pp_enzyme R_O16AP3pp_enzyme |
R_O16AP1pp R_O16AP2pp R_O16AP3pp |
388 | Secretion: 388.0, Translation: 388.0, Folding: 38.8 | 44,744 | UniprotID: P37748 | FUNCTION: May link the O-antigen tetrasaccharide units into long chains, giving rise to typical smooth LPS. | |
| b2036 | b2036 | UDP-galactopyranose mutase (UGM) (EC 5.4.99.9) (UDP-GALP mutase) (Uridine 5-diphosphate galactopyranose mutase) | Cytoplasm | R_UDPGALM_enzyme | R_UDPGALM | 367 | Translation: 367.0, Folding: 36.7 | 42,966 | UniprotID: P37747 ECnumber: EC 5.4.99.9 |
FUNCTION: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF). {ECO:0000250, ECO:0000269|PubMed:11448178, ECO:0000269|PubMed:8576037}. | |
| b2037 | b2037 | Putative O-antigen transporter | Cell_inner_membrane | R_O16AUNDtpp_enzyme | R_O16AUNDtpp | 415 | Secretion: 415.0, Translation: 415.0, Folding: 41.5 | 45,383 | UniprotID: P37746 | FUNCTION: May be involved in the translocation process of the nascent O-polysaccharide molecules and/or its ligation to lipid A core units. | |
| b2038 | b2038 | dTDP-4-dehydrorhamnose 3,5-epimerase (EC 5.1.3.13) (Thymidine diphospho-4-keto-rhamnose 3,5-epimerase) (dTDP-4-keto-6-deoxyglucose 3,5-epimerase) (dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase) (dTDP-L-rhamnose synthase) | Cytoplasm | R_TDPDRE_enzyme | R_TDPDRE | 185 | Translation: 185.0, Folding: 18.5 | 21,270 | UniprotID: P37745 ECnumber: EC 5.1.3.13 |
FUNCTION: Catalyzes the epimerization of the C3 and C5positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose. {ECO:0000250}. | |
| b2039 | b2039 | Glucose-1-phosphate thymidylyltransferase 1 (G1P-TT 1) (EC 2.7.7.24) (dTDP-glucose pyrophosphorylase 1) (dTDP-glucose synthase 1) | Cytoplasm | R_G1PTT_enzyme | R_G1PTT | 293 | Translation: 293.0, Folding: 29.3 | 32,694 | UniprotID: P37744 ECnumber: EC 2.7.7.24 |
FUNCTION: Catalyzes the formation of dTDP-glucose, from dTTP and glucose 1-phosphate, as well as its pyrophosphorolysis. {ECO:0000269|PubMed:11697907}. | |
| b1606 | b1606 | Dihydromonapterin reductase (H(2)-MPt reductase) (EC 1.5.1.-) (Dihydrofolate reductase) (DHFR) (EC 1.5.1.3) | Cytoplasm | R_DHFR_enzyme R_DHMPTR_enzyme |
R_DHFR R_DHMPTR |
240 | Translation: 240.0, Folding: 24.0 | 26,348 | UniprotID: P0AFS3 ECnumber: EC 1.5.1.-; 1.5.1.3 |
FUNCTION: Catalyzes the reduction of dihydromonapterin to tetrahydromonapterin. Also has lower activity with dihydrofolate. {ECO:0000269|PubMed:19897652}. | |
| b1605 | b1605 | Putative arginine/ornithine antiporter | Cell_inner_membrane | R_ARGORNt7pp_enzyme | R_ARGORNt7pp | 460 | Secretion: 460.0, Translation: 460.0, Folding: 46.0 | 49,501 | UniprotID: P0AAE5 | FUNCTION: Catalyzes an electroneutral exchange between arginine and ornithine to allow high-efficiency energy conversion in the arginine deiminase pathway. {ECO:0000250}. | |
| b1602 | b1602 | NAD(P) transhydrogenase subunit beta (EC 1.6.1.2) (Nicotinamide nucleotide transhydrogenase subunit beta) (Pyridine nucleotide transhydrogenase subunit beta) | Cell_inner_membrane | R_NADTRHD_duplicate_2_enzyme R_THD2pp_enzyme |
R_NADTRHD_duplicate_2 R_THD2pp |
462 | Secretion: 462.0, Translation: 462.0, Folding: 46.2 | 48,723 | UniprotID: P0AB67 ECnumber: EC 1.6.1.2 |
FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. | |
| b1603 | b1603 | NAD(P) transhydrogenase subunit alpha (EC 1.6.1.2) (Nicotinamide nucleotide transhydrogenase subunit alpha) (Pyridine nucleotide transhydrogenase subunit alpha) | Cell_inner_membrane | R_NADTRHD_duplicate_2_enzyme R_THD2pp_enzyme |
R_NADTRHD_duplicate_2 R_THD2pp |
510 | Secretion: 510.0, Translation: 510.0, Folding: 51.0 | 54,623 | UniprotID: P07001 ECnumber: EC 1.6.1.2 |
FUNCTION: The transhydrogenation between NADH and NADP is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane. | |
| b1600 | b1600 | Spermidine export protein MdtJ | Cell_inner_membrane | R_SPMDt3pp_enzyme | R_SPMDt3pp | 121 | Secretion: 121.0, Translation: 121.0, Folding: 12.1 | 13,115 | UniprotID: P69212 | FUNCTION: Catalyzes the excretion of spermidine. Can also confer resistance to deoxycholate and SDS. {ECO:0000269|PubMed:11566977, ECO:0000269|PubMed:18039771}. | |
| b1281 | b1281 | Orotidine 5-phosphate decarboxylase (EC 4.1.1.23) (OMP decarboxylase) (OMPDCase) (OMPdecase) | Cytoplasm | R_OMPDC_enzyme | R_OMPDC | 245 | Translation: 245.0, Folding: 24.5 | 26,350 | UniprotID: P08244 ECnumber: EC 4.1.1.23 |
FUNCTION: Catalyzes the decarboxylation of orotidine 5-monophosphate (OMP) to uridine 5-monophosphate (UMP). | |
| b1288 | b1288 | Enoyl-[acyl-carrier-protein] reductase [NADH] FabI (ENR) (EC 1.3.1.9) (NADH-dependent enoyl-ACP reductase) | Cytoplasm | R_EAR100x_enzyme R_EAR100y_enzyme R_EAR120x_enzyme R_EAR120y_enzyme R_EAR121x_enzyme R_EAR121y_enzyme R_EAR140x_enzyme R_EAR140y_enzyme R_EAR141x_enzyme R_EAR141y_enzyme R_EAR160x_enzyme R_EAR160y_enzyme R_EAR161x_enzyme R_EAR161y_enzyme R_EAR180x_enzyme R_EAR180y_enzyme R_EAR181x_enzyme R_EAR181y_enzyme R_EAR40x_enzyme R_EAR40y_enzyme R_EAR60x_enzyme R_EAR60y_enzyme R_EAR80x_enzyme R_EAR80y_enzyme R_EGMEACPR_enzyme R_EPMEACPR_enzyme |
262 | Translation: 262.0, Folding: 26.2 | 27,864 | UniprotID: P0AEK4 ECnumber: EC 1.3.1.9 |
FUNCTION: Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis. {ECO:0000269|PubMed:20693992, ECO:0000269|PubMed:7592873, ECO:0000269|PubMed:8119879}. | ||
| b2835 | b2835 | Lysophospholipid transporter LplT | Cell_inner_membrane | R_2AGPA120tipp_enzyme R_2AGPA140tipp_enzyme R_2AGPA141tipp_enzyme R_2AGPA160tipp_enzyme R_2AGPA161tipp_enzyme R_2AGPA180tipp_enzyme R_2AGPA181tipp_enzyme R_2AGPE120tipp_enzyme R_2AGPE140tipp_enzyme R_2AGPE141tipp_enzyme R_2AGPE160tipp_enzyme R_2AGPE161tipp_enzyme R_2AGPE180tipp_enzyme R_2AGPE181tipp_enzyme R_2AGPG120tipp_enzyme R_2AGPG140tipp_enzyme R_2AGPG141tipp_enzyme R_2AGPG160tipp_enzyme R_2AGPG161tipp_enzyme R_2AGPG180tipp_enzyme R_2AGPG181tipp_enzyme |
397 | Secretion: 397.0, Translation: 397.0, Folding: 39.7 | 41,656 | UniprotID: P39196 | FUNCTION: Catalyzes the facilitated diffusion of 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) into the cell. {ECO:0000269|PubMed:15661733}. | ||
| b1119 | b1119 | N-acetyl-D-glucosamine kinase (EC 2.7.1.59) (GlcNAc kinase) | Cytoplasm | R_ACGAMK_enzyme | R_ACGAMK | 303 | Translation: 303.0, Folding: 30.3 | 33,043 | UniprotID: P75959 ECnumber: EC 2.7.1.59 |
FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. Has also low level glucokinase activity in vitro. {ECO:0000269|PubMed:15489439}. | |
| b4544 | b4544 | Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnE (L-Ara4N-phosphoundecaprenol flippase subunit ArnE) (Undecaprenyl phosphate-aminoarabinose flippase subunit ArnE) | Cell_inner_membrane | R_ULA4Ntppi_enzyme | R_ULA4Ntppi | 111 | Secretion: 111.0, Translation: 111.0, Folding: 11.1 | 12,192 | UniprotID: Q47377 | FUNCTION: Translocates 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol (alpha-L-Ara4N-phosphoundecaprenol) from the cytoplasmic to the periplasmic side of the inner membrane. {ECO:0000269|PubMed:17928292}. | |
| b0642 | b0642 | Leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) | Cytoplasm | R_LEUTRS_enzyme | R_LEUTRS | 860 | Translation: 860.0, Folding: 86.0 | 97,234 | UniprotID: P07813 ECnumber: EC 6.1.1.4 |
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| b4381 | b4381 | Deoxyribose-phosphate aldolase (DERA) (EC 4.1.2.4) (2-deoxy-D-ribose 5-phosphate aldolase) (Phosphodeoxyriboaldolase) (Deoxyriboaldolase) | Cytoplasm | R_DRPA_enzyme | R_DRPA | 259 | Translation: 259.0, Folding: 25.9 | 27,734 | UniprotID: P0A6L0 ECnumber: EC 4.1.2.4 |
FUNCTION: Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00592, ECO:0000269|PubMed:11598300, ECO:0000269|PubMed:17905878, ECO:0000269|PubMed:6749498}. | |
| b4382 | b4382 | Thymidine phosphorylase (EC 2.4.2.4) (TdRPase) | Cytoplasm | R_DURIPP_enzyme R_TMDPP_enzyme |
R_DURIPP R_TMDPP |
440 | Translation: 440.0, Folding: 44.0 | 47,207 | UniprotID: P07650 ECnumber: EC 2.4.2.4 |
FUNCTION: The enzymes which catalyze the reversible phosphorolysis of pyrimidine nucleosides are involved in the degradation of these compounds and in their utilization as carbon and energy sources, or in the rescue of pyrimidine bases for nucleotide synthesis. | |
| b4383 | b4383 | Phosphopentomutase (EC 5.4.2.7) (Phosphodeoxyribomutase) | Cytoplasm | R_PPM_duplicate_2_enzyme R_PPM2_enzyme |
R_PPM_duplicate_2 R_PPM2 |
407 | Translation: 407.0, Folding: 40.7 | 44,370 | UniprotID: P0A6K6 ECnumber: EC 5.4.2.7 |
FUNCTION: Phosphotransfer between the C1 and C5 carbon atoms of pentose. | |
| b4384 | b4384 | Purine nucleoside phosphorylase DeoD-type (PNP) (EC 2.4.2.1) (Inosine phosphorylase) | Cytoplasm | 239 | Translation: 239.0, Folding: 23.9 | 25,950 | UniprotID: P0ABP8 ECnumber: EC 2.4.2.1 |
FUNCTION: Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. {ECO:0000269|PubMed:11786017}. | |||
| b4386 | b4386 | Lipoate-protein ligase A (EC 6.3.1.20) (Lipoate--protein ligase) | Cytoplasm | R_LIPAMPL_enzyme R_LIPATPT_enzyme R_OCTNLL_enzyme |
R_LIPAMPL R_LIPATPT R_OCTNLL |
338 | Translation: 338.0, Folding: 33.8 | 37,926 | UniprotID: P32099 ECnumber: EC 6.3.1.20 |
FUNCTION: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. Is also able to catalyze very poorly the transfer of lipoyl and octanoyl moiety from their acyl carrier protein. {ECO:0000269|PubMed:7639702}. | |
| b1732 | b1732 | Catalase HPII (EC 1.11.1.6) (Hydroxyperoxidase II) | Cytoplasm | R_CAT_enzyme | R_CAT | 753 | Translation: 753.0, Folding: 75.3 | 84,163 | UniprotID: P21179 ECnumber: EC 1.11.1.6 |
FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. | |
| b1734 | b1734 | 6-phospho-beta-glucosidase (EC 3.2.1.86) (Cellobiose-6-phosphate hydrolase) (Phospho-chitobiase) | Cytoplasm | R_DC6PH_enzyme | R_DC6PH | 450 | Translation: 450.0, Folding: 45.0 | 50,513 | UniprotID: P17411 ECnumber: EC 3.2.1.86 |
FUNCTION: Hydrolyzes a wide variety of P-beta-glucosides including cellobiose-6P, salicin-6P, arbutin-6P, gentiobiose-6P, methyl-beta-glucoside-6P and p-nitrophenyl-beta-D-glucopyranoside-6P. Is also able to hydrolyze phospho-N,N-diacetylchitobiose. {ECO:0000269|PubMed:10913117}. | |
| b0887 | b0887 | ATP-binding/permease protein CydD | Cell_inner_membrane | R_CYSabc2pp_enzyme R_GTHRDabc2pp_enzyme |
R_CYSabc2pp R_GTHRDabc2pp |
588 | Secretion: 588.0, Translation: 588.0, Folding: 58.8 | 65,056 | UniprotID: P29018 | FUNCTION: Somehow involved in the cytochrome D branch of aerobic respiration. Seems to be a component of a transport system. | |
| b0886 | b0886 | ATP-binding/permease protein CydC | Cell_inner_membrane | R_CYSabc2pp_enzyme R_GTHRDabc2pp_enzyme |
R_CYSabc2pp R_GTHRDabc2pp |
573 | Secretion: 573.0, Translation: 573.0, Folding: 57.3 | 62,920 | UniprotID: P23886 | FUNCTION: Somehow involved in the cytochrome D branch of aerobic respiration. Seems to be a component of a transport system. | |
| b0733 | b0733 | Cytochrome bd-I ubiquinol oxidase subunit 1 (EC 1.10.3.14) (Cytochrome bd-I oxidase subunit I) (Cytochrome d ubiquinol oxidase subunit I) | Cell_inner_membrane | R_CYTBDpp_duplicate_2_enzyme | R_CYTBDpp_duplicate_2 | 522 | Secretion: 522.0, Translation: 522.0, Folding: 52.2 | 58,205 | UniprotID: P0ABJ9 ECnumber: EC 1.10.3.14 |
FUNCTION: A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791, ECO:0000269|PubMed:2656671, ECO:0000269|PubMed:6307994, ECO:0000269|PubMed:7577938}. |
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| b0732 | b0732 | Mannosylglycerate hydrolase (EC 3.2.1.170) (2-O-(6-phospho-mannosyl)-D-glycerate hydrolase) (Alpha-mannosidase mngB) | Cytoplasm | R_MANPGH_enzyme | R_MANPGH | 877 | Translation: 877.0, Folding: 87.7 | 100,015 | UniprotID: P54746 ECnumber: EC 3.2.1.170 |
FUNCTION: May hydrolyze mannosyl-D-glycerate to mannose-6-phosphate and glycerate. {ECO:0000269|PubMed:14645248}. | |
| b0734 | b0734 | Cytochrome bd-I ubiquinol oxidase subunit 2 (EC 1.10.3.14) (Cytochrome bd-I oxidase subunit II) (Cytochrome d ubiquinol oxidase subunit II) | Cell_inner_membrane | R_CYTBDpp_duplicate_2_enzyme | R_CYTBDpp_duplicate_2 | 379 | Secretion: 379.0, Translation: 379.0, Folding: 37.9 | 42,453 | UniprotID: P0ABK2 ECnumber: EC 1.10.3.14 |
FUNCTION: A terminal oxidase that produces a proton motive force by the vectorial transfer of protons across the inner membrane. It is the component of the aerobic respiratory chain of E.coli that predominates when cells are grown at low aeration. Generates a proton motive force using protons and electrons from opposite sides of the membrane to generate H(2)O, transferring 1 proton/electron. {ECO:0000269|PubMed:19542282, ECO:0000269|PubMed:21987791, ECO:0000269|PubMed:6307994}. |
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| b0736 | b0736 | Acyl-CoA thioester hydrolase YbgC (Acyl-CoA thioesterase) (EC 3.1.2.-) | Cell_inner_membrane | R_DHNCOAT_enzyme | R_DHNCOAT | 134 | Secretion: 134.0, Translation: 134.0, Folding: 13.4 | 15,562 | UniprotID: P0A8Z3 ECnumber: EC 3.1.2.- |
FUNCTION: Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond. {ECO:0000269|PubMed:16294310}. | |
| b0888 | b0888 | Thioredoxin reductase (TRXR) (EC 1.8.1.9) | Cytoplasm | R_TRDR_enzyme R_TRDR_duplicate_2_enzyme |
R_TRDR R_TRDR_duplicate_2 |
321 | Translation: 321.0, Folding: 32.1 | 34,623 | UniprotID: P0A9P4 ECnumber: EC 1.8.1.9 |
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| b0469 | b0469 | Adenine phosphoribosyltransferase (APRT) (EC 2.4.2.7) | Cytoplasm | R_ADPT_enzyme | R_ADPT | 183 | Translation: 183.0, Folding: 18.3 | 19,859 | UniprotID: P69503 ECnumber: EC 2.4.2.7 |
FUNCTION: Catalyzes a salvage reaction resulting in the formation of AMP, that is energically less costly than de novo synthesis. | |
| b0463 | b0463 | Multidrug efflux pump subunit AcrA (AcrAB-TolC multidrug efflux pump subunit AcrA) (Acridine resistance protein A) | Cell_inner_membrane | R_CMtpp_enzyme R_CMtpp_duplicate_2_enzyme R_DOXRBCNtpp_enzyme R_DOXRBCNtpp_duplicate_2_enzyme R_FUSAtpp_enzyme R_FUSAtpp_duplicate_2_enzyme R_MINCYCtpp_enzyme R_MINCYCtpp_duplicate_2_enzyme R_NOVBCNtpp_enzyme R_NOVBCNtpp_duplicate_2_enzyme R_RFAMPtpp_enzyme R_RFAMPtpp_duplicate_2_enzyme R_TTRCYCtpp_enzyme R_TTRCYCtpp_duplicate_2_enzyme |
397 | Secretion: 397.0, Translation: 397.0, Folding: 39.7 | 42,197 | UniprotID: P0AE06 | FUNCTION: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm. {ECO:0000269|PubMed:9878415}. | ||
| b0462 | b0462 | Multidrug efflux pump subunit AcrB (AcrAB-TolC multidrug efflux pump subunit AcrB) (Acridine resistance protein B) | Cell_inner_membrane | R_CMtpp R_DOXRBCNtpp R_FUSAtpp R_MINCYCtpp R_NOVBCNtpp R_RFAMPtpp R_TTRCYCtpp |
1049 | Secretion: 1049.0, Translation: 1049.0, Folding: 104.9 | 113,574 | UniprotID: P31224 | FUNCTION: AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. {ECO:0000269|PubMed:16915237, ECO:0000269|PubMed:16946072, ECO:0000269|PubMed:17194213, ECO:0000269|PubMed:23010927}.; FUNCTION: Involved in contact-dependent growth inhibition (CDI), acts downstream of BamA, the receptor for CDI. Its role in CDI is independent of the AcrA-AcrB-TolC efflux pump complex. {ECO:0000269|PubMed:18761695}. |
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| b0394 | b0394 | Fructokinase (EC 2.7.1.4) (D-fructose kinase) (Manno(fructo)kinase) | Cytoplasm | R_HEX7_enzyme | R_HEX7 | 302 | Translation: 302.0, Folding: 30.2 | 32,500 | UniprotID: P23917 ECnumber: EC 2.7.1.4 |
FUNCTION: Catalyzes the phosphorylation of fructose to fructose-6-P. Has also low level glucokinase activity in vitro. Is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine. {ECO:0000269|PubMed:11742072, ECO:0000269|PubMed:15157072}. | |
| b4169 | b4169 | N-acetylmuramoyl-L-alanine amidase AmiB (EC 3.5.1.28) | Periplasm | R_AGM3PApp_duplicate_3_enzyme R_AGM4PApp_duplicate_3_enzyme |
R_AGM3PApp_duplicate_3 R_AGM4PApp_duplicate_3 |
445 | Secretion: 445.0, Translation: 445.0, Folding: 44.5 | 47,985 | UniprotID: P26365 ECnumber: EC 3.5.1.28 |
FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors. {ECO:0000269|PubMed:11454209, ECO:0000269|PubMed:18390656}. | |
| b4160 | b4160 | Phosphatidylserine decarboxylase proenzyme (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase alpha chain; Phosphatidylserine decarboxylase beta chain | Cell_inner_membrane | R_PSD120 R_PSD140 R_PSD141 R_PSD160 R_PSD161 R_PSD180 R_PSD181 |
322 | Secretion: 322.0, Translation: 322.0, Folding: 32.2 | 35,934 | UniprotID: P0A8K1 ECnumber: EC 4.1.1.65 |
FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Only decarboxylates the lipid-linked form of the serine moiety, and not serine alone or derivatives like phosphoserine or glycerophosphoserine. {ECO:0000255|HAMAP-Rule:MF_00662, ECO:0000269|PubMed:4598120}. | ||
| b4161 | b4161 | Small ribosomal subunit biogenesis GTPase RsgA (EC 3.6.1.-) | Cytoplasm | R_NTP1_duplicate_2_enzyme R_NTP10_enzyme R_NTP3_enzyme R_NTP5_enzyme |
R_NTP1_duplicate_2 R_NTP10 R_NTP3 R_NTP5 |
350 | Translation: 350.0, Folding: 35.0 | 39,193 | UniprotID: P39286 ECnumber: EC 3.6.1.- |
FUNCTION: One of at least 4 proteins (Era, RbfA, RimM and RsgA/YjeQ) that assist in the late maturation steps of the functional core of the 30S ribosomal subunit (PubMed:18223068, PubMed:21102555, PubMed:21303937, PubMed:25904134, PubMed:27382067). Binds the 30S subunit contacting the head, platform, and rRNA helix 44, which may assist the last maturation stages (PubMed:21788480, PubMed:21960487). Removes RbfA from mature, but not immature 30S ribosomes in a GTP-dependent manner; 95% removal in the presence of GTP, 90% removal in GMP-PNP and 65% removal in the presence of GDP (PubMed:21102555, PubMed:25904134). Circulary permuted GTPase that catalyzes rapid hydrolysis of GTP with a slow catalytic turnover (PubMed:12220175). Dispensible for viability, but important for overall fitness. The intrinsic GTPase activity is stimulated by the presence of 30S (160-fold increase in kcat) or 70S (96-fold increase in kcat) ribosomes (PubMed:14973029). Mature 30S ribosomes stimulate intrinsic GTPase more than do immature 30S ribosomes (PubMed:25904134). Ribosome-associated GTPase activity is stimulated by RbfA (PubMed:21102555). The GTPase is inhibited by aminoglycoside antibiotics such as neomycin and paromycin (PubMed:15466596) streptomycin and spectinomycin (PubMed:15828870). This inhibition is not due to competition for binding sites on the 30S or 70S ribosome (PubMed:15828870). {ECO:0000269|PubMed:12220175, ECO:0000269|PubMed:14973029, ECO:0000269|PubMed:15466596, ECO:0000269|PubMed:15828870, ECO:0000269|PubMed:21102555, ECO:0000269|PubMed:25904134, ECO:0000305|PubMed:18223068, ECO:0000305|PubMed:27382067}. |
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| b4035 | b4035 | Maltose/maltodextrin import ATP-binding protein MalK (EC 3.6.3.19) | Cell_inner_membrane | R_14GLUCANabcpp R_MALTHXabcpp R_MALTPTabcpp R_MALTTRabcpp R_MALTTTRabcpp R_MALTabcpp |
371 | Secretion: 371.0, Translation: 371.0, Folding: 37.1 | 40,990 | UniprotID: P68187 ECnumber: EC 3.6.3.19 |
FUNCTION: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Responsible for energy coupling to the transport system. | ||
| b0088 | b0088 | UDP-N-acetylmuramoylalanine--D-glutamate ligase (EC 6.3.2.9) (D-glutamic acid-adding enzyme) (UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase) | Cytoplasm | R_UAMAGS_enzyme | R_UAMAGS | 438 | Translation: 438.0, Folding: 43.8 | 46,974 | UniprotID: P14900 ECnumber: EC 6.3.2.9 |
FUNCTION: Cell wall formation. Catalyzes the addition of glutamate to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanine (UMA). | |
| b0087 | b0087 | Phospho-N-acetylmuramoyl-pentapeptide-transferase (EC 2.7.8.13) (UDP-MurNAc-pentapeptide phosphotransferase) | Cell_inner_membrane | R_PAPPT3_enzyme | R_PAPPT3 | 360 | Secretion: 360.0, Translation: 360.0, Folding: 36.0 | 39,875 | UniprotID: P0A6W3 ECnumber: EC 2.7.8.13 |
FUNCTION: First step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan. {ECO:0000269|PubMed:1846850}. | |
| b0086 | b0086 | UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase (EC 6.3.2.10) (D-alanyl-D-alanine-adding enzyme) (UDP-MurNAc-pentapeptide synthetase) | Cytoplasm | R_UGMDDS_enzyme | R_UGMDDS | 452 | Translation: 452.0, Folding: 45.2 | 47,447 | UniprotID: P11880 ECnumber: EC 6.3.2.10 |
FUNCTION: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein. {ECO:0000255|HAMAP-Rule:MF_02019, ECO:0000269|PubMed:2186811}. | |
| b0085 | b0085 | UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase (EC 6.3.2.13) (Meso-A2pm-adding enzyme) (Meso-diaminopimelate-adding enzyme) (UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase) (UDP-MurNAc-tripeptide synthetase) (UDP-N-acetylmuramyl-tripeptide synthetase) | Cytoplasm | R_UAAGDS_enzyme | R_UAAGDS | 495 | Translation: 495.0, Folding: 49.5 | 53,344 | UniprotID: P22188 ECnumber: EC 6.3.2.13 |
FUNCTION: Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan. Is also able to use many meso-diaminopimelate analogs as substrates, although much less efficiently, but not L-lysine. {ECO:0000269|PubMed:11124264, ECO:0000269|PubMed:2269304, ECO:0000269|PubMed:3905407}. |
|
| b0084 | b0084 | Peptidoglycan D,D-transpeptidase FtsI (EC 3.4.16.4) (Essential cell division protein FtsI) (Murein transpeptidase) (Penicillin-binding protein 3) (PBP-3) (Peptidoglycan synthase FtsI) | Cell_inner_membrane | R_MCTP1App_duplicate_2_enzyme R_MCTP2App_duplicate_2_enzyme |
R_MCTP1App_duplicate_2 R_MCTP2App_duplicate_2 |
588 | Secretion: 588.0, Translation: 588.0, Folding: 58.8 | 63,877 | UniprotID: P0AD68 ECnumber: EC 3.4.16.4 |
FUNCTION: Essential cell division protein that catalyzes cross-linking of the peptidoglycan cell wall at the division septum (PubMed:1103132, PubMed:6450748, PubMed:9614966, PubMed:3531167, PubMed:7030331). Required for localization of FtsN (PubMed:9282742). {ECO:0000269|PubMed:1103132, ECO:0000269|PubMed:3531167, ECO:0000269|PubMed:6450748, ECO:0000269|PubMed:7030331, ECO:0000269|PubMed:9282742, ECO:0000269|PubMed:9614966}. |
|
| b0261 | b0261 | Homocysteine S-methyltransferase (EC 2.1.1.10) (S-methylmethionine:homocysteine methyltransferase) | Cytoplasm | R_HCYSMT_enzyme R_HCYSMT2_enzyme |
R_HCYSMT R_HCYSMT2 |
310 | Translation: 310.0, Folding: 31.0 | 33,423 | UniprotID: Q47690 ECnumber: EC 2.1.1.10 |
FUNCTION: Catalyzes methyl transfer from S-methylmethionine or S-adenosylmethionine (less efficient) to homocysteine, selenohomocysteine and less efficiently selenocysteine. {ECO:0000269|PubMed:9882684}. | |
| b0260 | b0260 | Probable S-methylmethionine permease | Cell_inner_membrane | R_MMETt2pp_enzyme | R_MMETt2pp | 467 | Secretion: 467.0, Translation: 467.0, Folding: 46.7 | 50,526 | UniprotID: Q47689 | FUNCTION: Transporter for the intake of S-methylmethionine. | |
| b0067 | b0067 | Thiamine transport system permease protein ThiP | Cell_inner_membrane | R_THMabcpp_enzyme | R_THMabcpp | 536 | Secretion: 536.0, Translation: 536.0, Folding: 53.6 | 59,533 | UniprotID: P31549 | FUNCTION: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:9535878}. | |
| b0066 | b0066 | Thiamine import ATP-binding protein ThiQ (EC 3.6.3.-) | Cell_inner_membrane | R_THMabcpp_enzyme | R_THMabcpp | 232 | Secretion: 232.0, Translation: 232.0, Folding: 23.2 | 24,999 | UniprotID: P31548 ECnumber: EC 3.6.3.- |
FUNCTION: Part of the ABC transporter complex ThiBPQ involved in thiamine import. Responsible for energy coupling to the transport system (Probable). {ECO:0000305|PubMed:12175925}. | |
| b0061 | b0061 | L-ribulose-5-phosphate 4-epimerase AraD (EC 5.1.3.4) (Phosphoribulose isomerase) | Cytoplasm | R_RBP4E_duplicate_3_enzyme | R_RBP4E_duplicate_3 | 231 | Translation: 231.0, Folding: 23.1 | 25,519 | UniprotID: P08203 ECnumber: EC 5.1.3.4 |
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| b0063 | b0063 | Ribulokinase (EC 2.7.1.16) | Cytoplasm | R_RBK_L1_enzyme R_XYLK_enzyme R_XYLK2_enzyme |
R_RBK_L1 R_XYLK R_XYLK2 |
566 | Translation: 566.0, Folding: 56.6 | 61,089 | UniprotID: P08204 ECnumber: EC 2.7.1.16 |
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| b0062 | b0062 | L-arabinose isomerase (EC 5.3.1.4) | Cytoplasm | R_ARAI_enzyme | R_ARAI | 500 | Translation: 500.0, Folding: 50.0 | 56,074 | UniprotID: P08202 ECnumber: EC 5.3.1.4 |
FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose. | |
| b0068 | b0068 | Thiamine-binding periplasmic protein | Periplasm | R_THMabcpp_enzyme | R_THMabcpp | 327 | Secretion: 327.0, Translation: 327.0, Folding: 32.7 | 36,163 | UniprotID: P31550 | FUNCTION: Part of the ABC transporter complex ThiBPQ involved in thiamine import. {ECO:0000269|PubMed:9535878}. | |
| b3052 | b3052 | Bifunctional protein HldE [Includes: D-beta-D-heptose 7-phosphate kinase (EC 2.7.1.167) (D-beta-D-heptose 7-phosphotransferase) (D-glycero-beta-D-manno-heptose-7-phosphate kinase); D-beta-D-heptose 1-phosphate adenylyltransferase (EC 2.7.7.70) (D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase) | Cytoplasm | R_GMHEPAT_enzyme R_GMHEPK_enzyme |
R_GMHEPAT R_GMHEPK |
477 | Translation: 477.0, Folding: 47.7 | 51,051 | UniprotID: P76658 ECnumber: EC 2.7.1.167; 2.7.7.70 |
FUNCTION: Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate. {ECO:0000269|PubMed:11751812}.; FUNCTION: Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose. {ECO:0000269|PubMed:11751812}. | |
| b3425 | b3425 | Thiosulfate sulfurtransferase GlpE (EC 2.8.1.1) | Cytoplasm | R_CYANST_enzyme | R_CYANST | 108 | Translation: 108.0, Folding: 10.8 | 12,082 | UniprotID: P0A6V5 ECnumber: EC 2.8.1.1 |
FUNCTION: Catalyzes, although with low efficiency, the sulfur transfer reaction from thiosulfate to cyanide. The relatively low affinity of GlpE for both thiosulfate and cyanide suggests that these compounds are not the physiological substrates. Thioredoxin 1 or related dithiol proteins could instead be the physiological sulfur-acceptor substrate. Possible association with the metabolism of glycerol-phosphate remains to be elucidated. |
|
| b3061 | b3061 | L(+)-tartrate dehydratase subunit alpha (L-TTD alpha) (EC 4.2.1.32) | Cytoplasm | R_TARTD_enzyme | R_TARTD | 303 | Translation: 303.0, Folding: 30.3 | 32,734 | UniprotID: P05847 ECnumber: EC 4.2.1.32 |
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| b3062 | b3062 | L(+)-tartrate dehydratase subunit beta (L-TTD beta) (EC 4.2.1.32) | Cytoplasm | R_TARTD_enzyme | R_TARTD | 201 | Translation: 201.0, Folding: 20.1 | 22,679 | UniprotID: P0AC35 ECnumber: EC 4.2.1.32 |
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| b3063 | b3063 | L-tartrate/succinate antiporter (Tartrate carrier) (Tartrate transporter) | Cell_inner_membrane | R_TARTRt7pp_enzyme | R_TARTRt7pp | 487 | Secretion: 487.0, Translation: 487.0, Folding: 48.7 | 52,906 | UniprotID: P39414 | FUNCTION: Catalyzes the uptake of tartrate in exchange for intracellular succinate. Essential for anaerobic L-tartrate fermentation. {ECO:0000269|PubMed:17172328}. | |
| b2901 | b2901 | 6-phospho-beta-glucosidase BglA (EC 3.2.1.86) (Phospho-beta-glucosidase A) | Cytoplasm | R_AB6PGH_enzyme | R_AB6PGH | 479 | Translation: 479.0, Folding: 47.9 | 55,361 | UniprotID: Q46829 ECnumber: EC 3.2.1.86 |
FUNCTION: Catalyzes the hydrolysis of phosphorylated beta-glucosides into glucose-6-phosphate (G-6-P) and aglycone. It has a high affinity for phosphorylated aromatic beta-glucosides (p-nitrophenyl-beta-glucoside, phenyl beta-glucoside, arbutin), with the exception of phosphorylated salicin, and a low affinity for phosphorylated beta-methyl-glucoside. Apparently, it has only a very limited role in the utilization of external beta-glucosides. {ECO:0000269|PubMed:4576407}. |
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| b2903 | b2903 | Glycine dehydrogenase (decarboxylating) (EC 1.4.4.2) (Glycine cleavage system P-protein) (Glycine decarboxylase) (Glycine dehydrogenase (aminomethyl-transferring)) | Cytoplasm | R_GLYCL_enzyme | R_GLYCL | 957 | Translation: 957.0, Folding: 95.7 | 104,376 | UniprotID: P33195 ECnumber: EC 1.4.4.2 |
FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. {ECO:0000255|HAMAP-Rule:MF_00711, ECO:0000269|PubMed:8375392}. | |
| b3714 | b3714 | Adenine permease AdeP | Cell_inner_membrane | R_ADEt2rpp_duplicate_2_enzyme | R_ADEt2rpp_duplicate_2 | 445 | Secretion: 445.0, Translation: 445.0, Folding: 44.5 | 46,866 | UniprotID: P31466 | FUNCTION: High-affinity transporter for adenine. {ECO:0000269|PubMed:24214977, ECO:0000269|PubMed:6198438, ECO:0000269|PubMed:8165228}. | |
| b3390 | b3390 | Shikimate kinase 1 (SK 1) (EC 2.7.1.71) (Shikimate kinase I) (SKI) | Cytoplasm | R_SHKK_enzyme | R_SHKK | 173 | Translation: 173.0, Folding: 17.3 | 19,538 | UniprotID: P0A6D7 ECnumber: EC 2.7.1.71 |
FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. {ECO:0000269|PubMed:1309529}. | |
| b3396 | b3396 | Penicillin-binding protein 1A (PBP-1a) (PBP1a) [Includes: Penicillin-insensitive transglycosylase (EC 2.4.1.129) (Peptidoglycan TGase); Penicillin-sensitive transpeptidase (EC 3.4.16.4) (DD-transpeptidase) | Cell_inner_membrane | R_MCTP1App_duplicate_4 R_MCTP1Bpp_duplicate_2 R_MCTP2App R_MPTG_duplicate_2 R_MPTG2_duplicate_2 |
850 | Secretion: 850.0, Translation: 850.0, Folding: 85.0 | 93,636 | UniprotID: P02918 ECnumber: EC 2.4.1.129; 3.4.16.4 |
FUNCTION: Cell wall formation. Synthesis of cross-linked peptidoglycan from the lipid intermediates. The enzyme has a penicillin-insensitive transglycosylase N-terminal domain (formation of linear glycan strands) and a penicillin-sensitive transpeptidase C-terminal domain (cross-linking of the peptide subunits). {ECO:0000269|PubMed:7006606}. | ||
| b3397 | b3397 | ADP compounds hydrolase NudE (EC 3.6.1.-) | Cytoplasm | R_ADPRDP_enzyme | R_ADPRDP | 186 | Translation: 186.0, Folding: 18.6 | 21,153 | UniprotID: P45799 ECnumber: EC 3.6.1.- |
FUNCTION: Active on adenosine(5)triphospho(5)adenosine (Ap3A), ADP-ribose, NADH, adenosine(5)diphospho(5)adenosine (Ap2A). | |
| b3666 | b3666 | Hexose-6-phosphate:phosphate antiporter | Cell_inner_membrane | R_F6Pt6_2pp_enzyme R_G6Pt6_2pp_enzyme R_GAM6Pt6_2pp_enzyme R_MAN6Pt6_2pp_enzyme |
R_F6Pt6_2pp R_G6Pt6_2pp R_GAM6Pt6_2pp R_MAN6Pt6_2pp |
463 | Secretion: 463.0, Translation: 463.0, Folding: 46.3 | 50,607 | UniprotID: P0AGC0 | FUNCTION: Mediates the exchange of external hexose 6-phosphate and internal inorganic phosphate. Can transport glucose-6-phosphate, fructose-6-phosphate and mannose-6-phosphate. Also catalyzes the neutral exchange of internal and external phosphate. {ECO:0000269|PubMed:2197272, ECO:0000269|PubMed:3038843, ECO:0000269|PubMed:3283129, ECO:0000269|PubMed:3522583, ECO:0000269|PubMed:5330662, ECO:0000269|PubMed:8402899}. |
|
| b3665 | b3665 | Adenine deaminase (Adenase) (Adenine aminase) (EC 3.5.4.2) | Cytoplasm | R_ADD_enzyme | R_ADD | 588 | Translation: 588.0, Folding: 58.8 | 63,739 | UniprotID: P31441 ECnumber: EC 3.5.4.2 |
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| b2283 | b2283 | NADH-quinone oxidoreductase subunit G (EC 1.6.5.11) (NADH dehydrogenase I subunit G) (NDH-1 subunit G) (NUO7) | Cytoplasm | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
908 | Translation: 908.0, Folding: 90.8 | 100,299 | UniprotID: P33602 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
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| b2282 | b2282 | NADH-quinone oxidoreductase subunit H (EC 1.6.5.11) (NADH dehydrogenase I subunit H) (NDH-1 subunit H) (NUO8) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
325 | Secretion: 325.0, Translation: 325.0, Folding: 32.5 | 36,219 | UniprotID: P0AFD4 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone. |
|
| b2281 | b2281 | NADH-quinone oxidoreductase subunit I (EC 1.6.5.11) (NADH dehydrogenase I subunit I) (NDH-1 subunit I) (NUO9) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
180 | Secretion: 180.0, Translation: 180.0, Folding: 18.0 | 20,538 | UniprotID: P0AFD6 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
|
| b2280 | b2280 | NADH-quinone oxidoreductase subunit J (EC 1.6.5.11) (NADH dehydrogenase I subunit J) (NDH-1 subunit J) (NUO10) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
184 | Secretion: 184.0, Translation: 184.0, Folding: 18.4 | 19,875 | UniprotID: P0AFE0 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
|
| b2287 | b2287 | NADH-quinone oxidoreductase subunit B (EC 1.6.5.11) (NADH dehydrogenase I subunit B) (NDH-1 subunit B) (NUO2) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
220 | Secretion: 220.0, Translation: 220.0, Folding: 22.0 | 25,056 | UniprotID: P0AFC7 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
|
| b2286 | b2286 | NADH-quinone oxidoreductase subunit C/D (EC 1.6.5.11) (NADH dehydrogenase I subunit C/D) (NDH-1 subunit C/D) (NUO3/NUO4) | Cytoplasm | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
596 | Translation: 596.0, Folding: 59.6 | 68,236 | UniprotID: P33599 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
|
| b2285 | b2285 | NADH-quinone oxidoreductase subunit E (EC 1.6.5.11) (NADH dehydrogenase I subunit E) (NDH-1 subunit E) (NUO5) | Cytoplasm | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
166 | Translation: 166.0, Folding: 16.6 | 18,590 | UniprotID: P0AFD1 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
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| b2284 | b2284 | NADH-quinone oxidoreductase subunit F (EC 1.6.5.11) (NADH dehydrogenase I subunit F) (NDH-1 subunit F) (NUO6) | Cytoplasm | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
445 | Translation: 445.0, Folding: 44.5 | 49,292 | UniprotID: P31979 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
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| b2827 | b2827 | Thymidylate synthase (TS) (TSase) (EC 2.1.1.45) | Cytoplasm | R_TMDS_enzyme | R_TMDS | 264 | Translation: 264.0, Folding: 26.4 | 30,480 | UniprotID: P0A884 ECnumber: EC 2.1.1.45 |
FUNCTION: Catalyzes the reductive methylation of 2-deoxyuridine-5-monophosphate (dUMP) to 2-deoxythymidine-5-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product (PubMed:3286637, PubMed:2223754, PubMed:9826509). This enzymatic reaction provides an intracellular de novo source of dTMP, an essential precursor for DNA biosynthesis. This protein also binds to its mRNA thus repressing its own translation (PubMed:7708505). {ECO:0000269|PubMed:2223754, ECO:0000269|PubMed:3286637, ECO:0000269|PubMed:7708505, ECO:0000269|PubMed:9826509}. |
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| b2288 | b2288 | NADH-quinone oxidoreductase subunit A (EC 1.6.5.11) (NADH dehydrogenase I subunit A) (NDH-1 subunit A) (NUO1) | Cell_inner_membrane | R_NADH16pp_enzyme R_NADH17pp_enzyme R_NADH18pp_enzyme |
R_NADH16pp R_NADH17pp R_NADH18pp |
147 | Secretion: 147.0, Translation: 147.0, Folding: 14.7 | 16,457 | UniprotID: P0AFC3 ECnumber: EC 1.6.5.11 |
FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. |
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| b2530 | b2530 | Cysteine desulfurase IscS (EC 2.8.1.7) (NifS protein homolog) (ThiI transpersulfidase) (TusA transpersulfidase) | Cytoplasm | R_I2FE2SR_enzyme R_I2FE2SS_enzyme R_I2FE2SS2_enzyme R_ICYSDS_enzyme R_MOADSUx_enzyme R_THZPSN3_enzyme |
R_I2FE2SR R_I2FE2SS R_I2FE2SS2 R_ICYSDS R_MOADSUx R_THZPSN3 |
404 | Translation: 404.0, Folding: 40.4 | 45,090 | UniprotID: P0A6B7 ECnumber: EC 2.8.1.7 |
FUNCTION: Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins. Preferentially binds to disordered IscU on which the Fe-S is assembled, IscU converts to the structured state and then dissociates from IscS to transfer the Fe-S to an acceptor protein. Also functions as a selenium delivery protein in the pathway for the biosynthesis of selenophosphate. Transfers sulfur onto Cys-456 of ThiI and onto Cys-19 of TusA in transpersulfidation reactions. {ECO:0000269|PubMed:10544286, ECO:0000269|PubMed:10600118, ECO:0000269|PubMed:10781558, ECO:0000269|PubMed:10781607, ECO:0000269|PubMed:10829016, ECO:0000269|PubMed:10908675, ECO:0000269|PubMed:11577100, ECO:0000269|PubMed:16387657, ECO:0000269|PubMed:22203963, ECO:0000269|PubMed:8663056}. |
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| b2533 | b2533 | Inositol-1-monophosphatase (I-1-Pase) (IMPase) (Inositol-1-phosphatase) (EC 3.1.3.25) | Cytoplasm | R_G2PP_enzyme R_MI1PP_enzyme |
R_G2PP R_MI1PP |
267 | Translation: 267.0, Folding: 26.7 | 29,172 | UniprotID: P0ADG4 ECnumber: EC 3.1.3.25 |
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| b3809 | b3809 | Diaminopimelate epimerase (DAP epimerase) (EC 5.1.1.7) (PLP-independent amino acid racemase) | Cytoplasm | R_DAPE_enzyme | R_DAPE | 274 | Translation: 274.0, Folding: 27.4 | 30,209 | UniprotID: P0A6K1 ECnumber: EC 5.1.1.7 |
FUNCTION: Involved in the succinylase branch of the L-lysine biosynthesis and in the biosynthesis of the pentapeptide incorporated in the peptidoglycan moiety (PubMed:3283102). Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP) (PubMed:6378903, PubMed:3031013, PubMed:3042781). {ECO:0000269|PubMed:3031013, ECO:0000269|PubMed:3042781, ECO:0000269|PubMed:3283102, ECO:0000269|PubMed:6378903}. |
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| b3803 | b3803 | Putative uroporphyrinogen-III C-methyltransferase (Urogen-III methylase) (EC 2.1.1.107) (ORF X) | Cell_inner_membrane | R_UPP3MT_enzyme | R_UPP3MT | 393 | Secretion: 393.0, Translation: 393.0, Folding: 39.3 | 42,963 | UniprotID: P09127 ECnumber: EC 2.1.1.107 |
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| b3806 | b3806 | Adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) | Cytoplasm | R_ADNCYC_enzyme | R_ADNCYC | 848 | Translation: 848.0, Folding: 84.8 | 97,586 | UniprotID: P00936 ECnumber: EC 4.6.1.1 |
FUNCTION: Catalyzes the formation of the second messenger cAMP from ATP. Its transcript is probably degraded by endoribonuclease LS (rnlA), decreasing cAMP levels and the negative regulator Crp-cAMP, which then induces its own transcription again. | |
| b3807 | b3807 | Protein CyaY | Cytoplasm | R_I2FE2SS_enzyme R_I2FE2SS2_enzyme R_S2FE2SS_enzyme R_S2FE2SS2_enzyme |
R_I2FE2SS R_I2FE2SS2 R_S2FE2SS R_S2FE2SS2 |
106 | Translation: 106.0, Folding: 10.6 | 12,231 | UniprotID: P27838 | ||
| b3804 | b3804 | Uroporphyrinogen-III synthase (UROS) (EC 4.2.1.75) (Hydroxymethylbilane hydrolyase [cyclizing]) (Uroporphyrinogen-III cosynthase) | Cytoplasm | R_UPP3S_enzyme | R_UPP3S | 246 | Translation: 246.0, Folding: 24.6 | 27,798 | UniprotID: P09126 ECnumber: EC 4.2.1.75 |
FUNCTION: Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. {ECO:0000250}. | |
| b3805 | b3805 | Porphobilinogen deaminase (PBG) (EC 2.5.1.61) (Hydroxymethylbilane synthase) (HMBS) (Pre-uroporphyrinogen synthase) | Cytoplasm | R_HMBS_enzyme | R_HMBS | 313 | Translation: 313.0, Folding: 31.3 | 33,852 | UniprotID: P06983 ECnumber: EC 2.5.1.61 |
FUNCTION: Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps. {ECO:0000269|PubMed:3529035}. | |
| b3480 | b3480 | Nickel import ATP-binding protein NikE (EC 3.6.3.24) | Cell_inner_membrane | R_NI2uabcpp_enzyme | R_NI2uabcpp | 268 | Secretion: 268.0, Translation: 268.0, Folding: 26.8 | 29,722 | UniprotID: P33594 ECnumber: EC 3.6.3.24 |
FUNCTION: Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01712}. | |
| b2751 | b2751 | Sulfate adenylyltransferase subunit 1 (EC 2.7.7.4) (ATP-sulfurylase large subunit) (Sulfate adenylate transferase) (SAT) | Cytoplasm | R_SADT2_enzyme | R_SADT2 | 475 | Translation: 475.0, Folding: 47.5 | 52,558 | UniprotID: P23845 ECnumber: EC 2.7.7.4 |
FUNCTION: May be the GTPase, regulating ATP sulfurylase activity. | |
| b2750 | b2750 | Adenylyl-sulfate kinase (EC 2.7.1.25) (APS kinase) (ATP adenosine-5-phosphosulfate 3-phosphotransferase) (Adenosine-5-phosphosulfate kinase) | Cytoplasm | R_ADSK_enzyme | R_ADSK | 201 | Translation: 201.0, Folding: 20.1 | 22,321 | UniprotID: P0A6J1 ECnumber: EC 2.7.1.25 |
FUNCTION: Catalyzes the synthesis of activated sulfate. | |
| b2752 | b2752 | Sulfate adenylyltransferase subunit 2 (EC 2.7.7.4) (ATP-sulfurylase small subunit) (Sulfate adenylate transferase) (SAT) | Cytoplasm | R_SADT2_enzyme | R_SADT2 | 302 | Translation: 302.0, Folding: 30.2 | 35,188 | UniprotID: P21156 ECnumber: EC 2.7.7.4 |
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| b3930 | b3930 | 1,4-dihydroxy-2-naphthoate octaprenyltransferase (DHNA-octaprenyltransferase) (EC 2.5.1.74) | Cell_inner_membrane | R_DHNAOT4_enzyme | R_DHNAOT4 | 308 | Secretion: 308.0, Translation: 308.0, Folding: 30.8 | 33,594 | UniprotID: P32166 ECnumber: EC 2.5.1.74 |
FUNCTION: Conversion of 1,4-dihydroxy-2-naphthoate (DHNA) to demethylmenaquinone (DMK). Attaches octaprenylpyrophosphate, a membrane-bound 40-carbon side chain to DHNA. The conversion of DHNA to DMK proceeds in three stages: the removal of the carboxyl group of DHNA as CO(2), the attachment of the isoprenoid side chain, and a quinol-to-quinone oxidation, which is thought to be spontaneous. {ECO:0000269|PubMed:9573170}. |
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| b3939 | b3939 | Cystathionine gamma-synthase (CGS) (EC 2.5.1.48) (O-succinylhomoserine (thiol)-lyase) | Cytoplasm | R_SHSL1_enzyme | R_SHSL1 | 386 | Translation: 386.0, Folding: 38.6 | 41,550 | UniprotID: P00935 ECnumber: EC 2.5.1.48 |
FUNCTION: Catalyzes the formation of L-cystathionine from O-succinyl-L-homoserine (OSHS) and L-cysteine, via a gamma-replacement reaction. In the absence of thiol, catalyzes gamma-elimination to form 2-oxobutanoate, succinate and ammonia. {ECO:0000269|PubMed:2405903}. | |
| b1638 | b1638 | Pyridoxine/pyridoxamine 5-phosphate oxidase (EC 1.4.3.5) (PNP/PMP oxidase) (PNPOx) (Pyridoxal 5-phosphate synthase) | Cytoplasm | R_PDX5POi_enzyme R_PYAM5PO_enzyme |
R_PDX5POi R_PYAM5PO |
218 | Translation: 218.0, Folding: 21.8 | 25,545 | UniprotID: P0AFI7 ECnumber: EC 1.4.3.5 |
FUNCTION: Catalyzes the oxidation of either pyridoxine 5-phosphate (PNP) or pyridoxamine 5-phosphate (PMP) into pyridoxal 5-phosphate (PLP). {ECO:0000269|PubMed:11786019, ECO:0000269|PubMed:7860596, ECO:0000269|PubMed:9693059}. | |
| b1637 | b1637 | Tyrosine--tRNA ligase (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) | Cytoplasm | R_TYRTRS_enzyme | R_TYRTRS | 424 | Translation: 424.0, Folding: 42.4 | 47,527 | UniprotID: P0AGJ9 ECnumber: EC 6.1.1.1 |
FUNCTION: Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Also mischarges tRNA(Tyr) with D-tyrosine, although Vmax is much lower (PubMed:4292198). {ECO:0000269|PubMed:4292198}. | |
| b1636 | b1636 | Pyridoxal kinase PdxY (PL kinase) (EC 2.7.1.35) (Pyridoxal kinase 2) (PL kinase 2) | Cytoplasm | R_PYDXK_enzyme | R_PYDXK | 287 | Translation: 287.0, Folding: 28.7 | 31,322 | UniprotID: P77150 ECnumber: EC 2.7.1.35 |
FUNCTION: Pyridoxal kinase involved in the salvage pathway of pyridoxal 5-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP in vivo, but shows very low activity compared to PdxK. Displays a low level of pyridoxine kinase activity when overexpressed, which is however not physiologically relevant. {ECO:0000269|PubMed:15249053, ECO:0000269|PubMed:9537380}. | |
| b1634 | b1634 | Dipeptide and tripeptide permease A | Cell_inner_membrane | R_LALADGLUtpp_duplicate_2_enzyme R_LALALGLUtpp_duplicate_2_enzyme |
R_LALADGLUtpp_duplicate_2 R_LALALGLUtpp_duplicate_2 |
500 | Secretion: 500.0, Translation: 500.0, Folding: 50.0 | 53,991 | UniprotID: P77304 | FUNCTION: Proton-dependent permease that transports di- and tripeptides as well as structurally related peptidomimetics such as aminocephalosporins into the cell. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate. {ECO:0000269|PubMed:15175316, ECO:0000269|PubMed:17158458, ECO:0000269|PubMed:18485005}. |
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| b3200 | b3200 | Lipopolysaccharide export system protein LptA | Periplasm | 185 | Secretion: 185.0, Translation: 185.0, Folding: 18.5 | 20,127 | UniprotID: P0ADV1 | FUNCTION: Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm. {ECO:0000255|HAMAP-Rule:MF_01914, ECO:0000269|PubMed:16765569, ECO:0000269|PubMed:17056748, ECO:0000269|PubMed:18424520, ECO:0000269|PubMed:18480051, ECO:0000269|PubMed:21169485}. |
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| b2379 | b2379 | Glutamate-pyruvate aminotransferase AlaC (EC 2.6.1.2) | Cytoplasm | R_ALATA_L_duplicate_2_enzyme | R_ALATA_L_duplicate_2 | 412 | Translation: 412.0, Folding: 41.2 | 46,216 | UniprotID: P77434 ECnumber: EC 2.6.1.2 |
FUNCTION: Involved in the biosynthesis of alanine. {ECO:0000269|PubMed:20729367, ECO:0000269|PubMed:21597182}. | |
| b3751 | b3751 | Ribose import binding protein RbsB | Periplasm | R_RIBabcpp_enzyme | R_RIBabcpp | 296 | Secretion: 296.0, Translation: 296.0, Folding: 29.6 | 30,950 | UniprotID: P02925 | FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose. Also serves as the primary chemoreceptor for chemotaxis. {ECO:0000269|PubMed:25533465, ECO:0000269|PubMed:4608146, ECO:0000269|PubMed:6327617, ECO:0000269|PubMed:7982928}. | |
| b1126 | b1126 | Spermidine/putrescine import ATP-binding protein PotA (EC 3.6.3.31) | Cell_inner_membrane | R_PTRCabcpp_enzyme R_SPMDabcpp_enzyme |
R_PTRCabcpp R_SPMDabcpp |
378 | Secretion: 378.0, Translation: 378.0, Folding: 37.8 | 43,028 | UniprotID: P69874 ECnumber: EC 3.6.3.31 |
FUNCTION: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01726, ECO:0000269|PubMed:1939142, ECO:0000269|PubMed:2249996, ECO:0000269|PubMed:8366082}. | |
| b1125 | b1125 | Spermidine/putrescine transport system permease protein PotB | Cell_inner_membrane | R_PTRCabcpp_enzyme R_SPMDabcpp_enzyme |
R_PTRCabcpp R_SPMDabcpp |
275 | Secretion: 275.0, Translation: 275.0, Folding: 27.5 | 31,062 | UniprotID: P0AFK4 | FUNCTION: Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine. | |
| b1124 | b1124 | Spermidine/putrescine transport system permease protein PotC | Cell_inner_membrane | R_PTRCabcpp_enzyme R_SPMDabcpp_enzyme |
R_PTRCabcpp R_SPMDabcpp |
264 | Secretion: 264.0, Translation: 264.0, Folding: 26.4 | 29,111 | UniprotID: P0AFK6 | FUNCTION: Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine. | |
| b1123 | b1123 | Spermidine/putrescine-binding periplasmic protein (SPBP) | Periplasm | R_PTRCabcpp_enzyme R_SPMDabcpp_enzyme |
R_PTRCabcpp R_SPMDabcpp |
348 | Secretion: 348.0, Translation: 348.0, Folding: 34.8 | 38,867 | UniprotID: P0AFK9 | FUNCTION: Required for the activity of the bacterial periplasmic transport system of putrescine and spermidine. Polyamine binding protein. {ECO:0000269|PubMed:1939142}. | |
| b1704 | b1704 | Phospho-2-dehydro-3-deoxyheptonate aldolase, Trp-sensitive (EC 2.5.1.54) (3-deoxy-D-arabino-heptulosonate 7-phosphate synthase) (DAHP synthase) (Phospho-2-keto-3-deoxyheptonate aldolase) | Cytoplasm | R_DDPA_duplicate_3_enzyme | R_DDPA_duplicate_3 | 348 | Translation: 348.0, Folding: 34.8 | 38,735 | UniprotID: P00887 ECnumber: EC 2.5.1.54 |
FUNCTION: Stereospecific condensation of phosphoenolpyruvate (PEP) and D-erythrose-4-phosphate (E4P) giving rise to 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP). | |
| b1250 | b1250 | Voltage-gated potassium channel Kch | Cell_inner_membrane | R_Kt2pp_duplicate_3_enzyme | R_Kt2pp_duplicate_3 | 417 | Secretion: 417.0, Translation: 417.0, Folding: 41.7 | 46,063 | UniprotID: P31069 | FUNCTION: K(+)-specific ion channel. May play a role in the defense against osmotic shock. {ECO:0000269|PubMed:12912904, ECO:0000269|PubMed:8170937}. | |
| b1701 | b1701 | Medium-chain fatty-acid--CoA ligase (EC 6.2.1.-) (Acyl-CoA synthetase) (ACS) (Fatty acyl-CoA synthetase FadK) | Cell_inner_membrane | 566 | Secretion: 566.0, Translation: 566.0, Folding: 56.6 | 62,759 | UniprotID: P38135 ECnumber: EC 6.2.1.- |
FUNCTION: Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Is maximally active on C6:0, C8:0 and C12:0 fatty acids, while has a low activity on C14-C18 chain length fatty acids (PubMed:15213221, PubMed:19477415). Is involved in the anaerobic beta-oxidative degradation of fatty acids, which allows anaerobic growth of E.coli on fatty acids as a sole carbon and energy source in the presence of nitrate or fumarate as a terminal electron acceptor (PubMed:12535077). Can functionally replace FadD under anaerobic conditions (PubMed:12535077). {ECO:0000269|PubMed:12535077, ECO:0000269|PubMed:15213221, ECO:0000269|PubMed:19477415}. |
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| b1252 | b1252 | Protein TonB | Cell_inner_membrane | 239 | Secretion: 239.0, Translation: 239.0, Folding: 23.9 | 26,094 | UniprotID: P02929 | FUNCTION: Interacts with outer membrane receptor proteins that carry out high-affinity binding and energy dependent uptake into the periplasmic space of specific substrates such as cobalamin, and various iron compounds (such as iron dicitrate, enterochelin, aerobactin, etc.). In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy-dependent, irreversible steps of bacteriophages phi 80 and T1 infection. It could act to transduce energy from the cytoplasmic membrane to specific energy-requiring processes in the outer membrane, resulting in the release into the periplasm of ligands bound by these outer membrane proteins. Implicated in hydroxy radical-mediated cell death induced by hydroxyurea treatment (PubMed:20005847). {ECO:0000269|PubMed:20005847}. |
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| b0657 | b0657 | Apolipoprotein N-acyltransferase (ALP N-acyltransferase) (EC 2.3.1.-) (Copper homeostasis protein CutE) | Cell_inner_membrane | R_ALPATE160pp_enzyme R_ALPATG160pp_enzyme |
R_ALPATE160pp R_ALPATG160pp |
512 | Secretion: 512.0, Translation: 512.0, Folding: 51.2 | 57,066 | UniprotID: P23930 ECnumber: EC 2.3.1.- |
FUNCTION: Transfers the fatty acyl group on membrane lipoproteins. | |
| b0654 | b0654 | Glutamate/aspartate import permease protein GltJ | Cell_inner_membrane | R_ASPabcpp_enzyme R_GLUabcpp_enzyme |
R_ASPabcpp R_GLUabcpp |
246 | Secretion: 246.0, Translation: 246.0, Folding: 24.6 | 27,503 | UniprotID: P0AER3 | FUNCTION: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000305|PubMed:9593292}. | |
| b0655 | b0655 | Glutamate/aspartate import solute-binding protein | Periplasm | R_ASPabcpp_enzyme R_GLUabcpp_enzyme |
R_ASPabcpp R_GLUabcpp |
302 | Secretion: 302.0, Translation: 302.0, Folding: 30.2 | 33,420 | UniprotID: P37902 | FUNCTION: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Binds to both glutamate and aspartate. {ECO:0000269|PubMed:1091635, ECO:0000269|PubMed:1091636, ECO:0000269|PubMed:336628, ECO:0000305|PubMed:9593292}. | |
| b0652 | b0652 | Glutamate/aspartate import ATP-binding protein GltL (EC 3.6.3.21) | Cell_inner_membrane | R_ASPabcpp_enzyme R_GLUabcpp_enzyme |
R_ASPabcpp R_GLUabcpp |
241 | Secretion: 241.0, Translation: 241.0, Folding: 24.1 | 26,661 | UniprotID: P0AAG3 ECnumber: EC 3.6.3.21 |
FUNCTION: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for energy coupling to the transport system. {ECO:0000305|PubMed:9593292}. | |
| b0653 | b0653 | Glutamate/aspartate import permease protein GltK | Cell_inner_membrane | R_ASPabcpp_enzyme R_GLUabcpp_enzyme |
R_ASPabcpp R_GLUabcpp |
224 | Secretion: 224.0, Translation: 224.0, Folding: 22.4 | 24,915 | UniprotID: P0AER5 | FUNCTION: Part of the ABC transporter complex GltIJKL involved in glutamate and aspartate uptake. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000305|PubMed:9593292}. | |
| b0650 | b0650 | Chaperone protein HscC (Hsc62) | Cytoplasm | R_NTP1_enzyme | R_NTP1 | 556 | Translation: 556.0, Folding: 55.6 | 61,986 | UniprotID: P77319 | FUNCTION: Probable chaperone. Has ATPase activity. Not stimulated by DnaJ. | |
| b0651 | b0651 | Pyrimidine-specific ribonucleoside hydrolase RihA (EC 3.2.-.-) (Cytidine/uridine-specific hydrolase) | Cytoplasm | R_CYTDH_enzyme R_URIH_enzyme |
R_CYTDH R_URIH |
311 | Translation: 311.0, Folding: 31.1 | 33,823 | UniprotID: P41409 ECnumber: EC 3.2.-.- |
FUNCTION: Hydrolyzes with equal efficiency cytidine or uridine to ribose and cytosine or uracil, respectively. | |
| b4374 | b4374 | Pyrimidine 5-nucleotidase YjjG (EC 3.1.3.5) (House-cleaning nucleotidase) (Non-canonical pyrimidine nucleotide phosphatase) (Nucleoside 5-monophosphate phosphohydrolase) (dUMP phosphatase) | Cytoplasm | R_NTD1_duplicate_3_enzyme R_NTD2_duplicate_2_enzyme R_NTD5_duplicate_3_enzyme |
R_NTD1_duplicate_3 R_NTD2_duplicate_2 R_NTD5_duplicate_3 |
225 | Translation: 225.0, Folding: 22.5 | 25,301 | UniprotID: P0A8Y1 ECnumber: EC 3.1.3.5 |
FUNCTION: Nucleotidase that shows high phosphatase activity toward non-canonical pyrimidine nucleotides and three canonical nucleoside 5-monophosphates (UMP, dUMP, and dTMP), and very low activity against TDP, IMP, UDP, GMP, dGMP, AMP, dAMP, and 6-phosphogluconate. Appears to function as a house-cleaning nucleotidase in vivo, since the general nucleotidase activity of YjjG allows it to protect cells against non-canonical pyrimidine derivatives such as 5-fluoro-2-deoxyuridine, 5-fluorouridine, 5-fluoroorotate, 5-fluorouracil, and 5-aza-2-deoxycytidine, and prevents the incorporation of potentially mutagenic nucleotides into DNA. Its dUMP phosphatase activity that catalyzes the hydrolysis of dUMP to deoxyuridine is necessary for thymine utilization via the thymine salvage pathway. Is strictly specific to substrates with 5-phosphates and shows no activity against nucleoside 2- or 3-monophosphates. {ECO:0000269|PubMed:15489502, ECO:0000269|PubMed:17189366, ECO:0000269|PubMed:17286574}. |
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| b0722 | b0722 | Succinate dehydrogenase hydrophobic membrane anchor subunit | Cell_inner_membrane | R_SUCDi_enzyme | R_SUCDi | 115 | Secretion: 115.0, Translation: 115.0, Folding: 11.5 | 12,868 | UniprotID: P0AC44 | FUNCTION: Membrane-anchoring subunit of succinate dehydrogenase (SDH). | |
| b0723 | b0723 | Succinate dehydrogenase flavoprotein subunit (EC 1.3.5.1) | Cell_inner_membrane | R_SUCDi_enzyme | R_SUCDi | 588 | Secretion: 588.0, Translation: 588.0, Folding: 58.8 | 64,422 | UniprotID: P0AC41 ECnumber: EC 1.3.5.1 |
FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. {ECO:0000269|PubMed:24374335, ECO:0000305|PubMed:12560550, ECO:0000305|PubMed:16407191, ECO:0000305|PubMed:19710024}. | |
| b1389 | b1389 | 1,2-phenylacetyl-CoA epoxidase, subunit B (1,2-phenylacetyl-CoA monooxygenase, subunit B) | Cytoplasm | R_PACCOAE_enzyme | R_PACCOAE | 95 | Translation: 95.0, Folding: 9.5 | 10,942 | UniprotID: P76078 | FUNCTION: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit B may play a regulatory role or be directly involved in electron transport. {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:9748275}. | |
| b0893 | b0893 | Serine--tRNA ligase (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) | Cytoplasm | R_SERTRS_enzyme R_SERTRS2_enzyme |
R_SERTRS R_SERTRS2 |
430 | Translation: 430.0, Folding: 43.0 | 48,414 | UniprotID: P0A8L1 ECnumber: EC 6.1.1.11 |
FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec). {ECO:0000269|PubMed:2963963, ECO:0000269|PubMed:7537870, ECO:0000269|PubMed:8065908}. | |
| b0726 | b0726 | 2-oxoglutarate dehydrogenase E1 component (EC 1.2.4.2) (Alpha-ketoglutarate dehydrogenase) | Cytoplasm | R_AKGDH_enzyme | R_AKGDH | 933 | Translation: 933.0, Folding: 93.3 | 105,062 | UniprotID: P0AFG3 ECnumber: EC 1.2.4.2 |
FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3). | |
| b0895 | b0895 | Anaerobic dimethyl sulfoxide reductase chain B (DMSO reductase iron-sulfur subunit) | Cytoplasm | R_DMSOR1_duplicate_2_enzyme R_DMSOR2_enzyme R_TMAOR1_enzyme R_TMAOR2_enzyme |
R_DMSOR1_duplicate_2 R_DMSOR2 R_TMAOR1 R_TMAOR2 |
205 | Translation: 205.0, Folding: 20.5 | 22,869 | UniprotID: P18776 | FUNCTION: Electron transfer subunit of the terminal reductase during anaerobic growth on various sulfoxide and N-oxide compounds. | |
| b0724 | b0724 | Succinate dehydrogenase iron-sulfur subunit (EC 1.3.5.1) | Cell_inner_membrane | R_SUCDi_enzyme | R_SUCDi | 238 | Secretion: 238.0, Translation: 238.0, Folding: 23.8 | 26,770 | UniprotID: P07014 ECnumber: EC 1.3.5.1 |
FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. | |
| b0728 | b0728 | Succinate--CoA ligase [ADP-forming] subunit beta (EC 6.2.1.5) (Succinyl-CoA synthetase subunit beta) (SCS-beta) | Cytoplasm | R_SUCOAS_enzyme | R_SUCOAS | 388 | Translation: 388.0, Folding: 38.8 | 41,393 | UniprotID: P0A836 ECnumber: EC 6.2.1.5 |
FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit. Can use either ATP or GTP, but prefers ATP. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. {ECO:0000255|HAMAP-Rule:MF_00558, ECO:0000269|PubMed:10353839}. |
|
| b0729 | b0729 | Succinate--CoA ligase [ADP-forming] subunit alpha (EC 6.2.1.5) (Succinyl-CoA synthetase subunit alpha) (SCS-alpha) | Cytoplasm | R_SUCOAS_enzyme | R_SUCOAS | 289 | Translation: 289.0, Folding: 28.9 | 29,777 | UniprotID: P0AGE9 ECnumber: EC 6.2.1.5 |
FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. Can use either ATP or GTP, but prefers ATP. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. {ECO:0000255|HAMAP-Rule:MF_01988, ECO:0000269|PubMed:10353839}. |
|
| b1387 | b1387 | Bifunctional protein PaaZ [Includes: 2-oxepin-2(3H)-ylideneacetyl-CoA hydrolase (EC 3.3.2.12) (Oxepin-CoA hydrolase); 3-oxo-5 6-dehydrosuberyl-CoA semialdehyde dehydrogenase (EC 1.2.1.91) | Cytoplasm | R_OXCOAHDH_enzyme | R_OXCOAHDH | 681 | Translation: 681.0, Folding: 68.1 | 73,003 | UniprotID: P77455 ECnumber: EC 3.3.2.12; 1.2.1.91 |
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| b1386 | b1386 | Primary amine oxidase (EC 1.4.3.21) (2-phenylethylamine oxidase) (Copper amine oxidase) (Tyramine oxidase) | Periplasm | R_42A12BOOXpp_enzyme R_PEAMNOpp_enzyme R_TYROXDApp_enzyme |
R_42A12BOOXpp R_PEAMNOpp R_TYROXDApp |
757 | Secretion: 757.0, Translation: 757.0, Folding: 75.7 | 84,379 | UniprotID: P46883 ECnumber: EC 1.4.3.21 |
FUNCTION: The enzyme prefers aromatic over aliphatic amines. | |
| b1385 | b1385 | Phenylacetaldehyde dehydrogenase (PAD) (EC 1.2.1.39) | Cytoplasm | R_ALDD19xr_enzyme | R_ALDD19xr | 499 | Translation: 499.0, Folding: 49.9 | 53,699 | UniprotID: P80668 ECnumber: EC 1.2.1.39 |
FUNCTION: Acts almost equally well on phenylacetaldehyde, 4-hydroxyphenylacetaldehyde and 3,4-dihydroxyphenylacetaldehyde. | |
| b0477 | b0477 | Inosine-guanosine kinase (EC 2.7.1.73) | Cytoplasm | R_GSNK_enzyme R_INSK_enzyme |
R_GSNK R_INSK |
434 | Translation: 434.0, Folding: 43.4 | 48,449 | UniprotID: P0AEW6 ECnumber: EC 2.7.1.73 |
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| b0474 | b0474 | Adenylate kinase (AK) (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase) | Cytoplasm | 214 | Translation: 214.0, Folding: 21.4 | 23,586 | UniprotID: P69441 ECnumber: EC 2.7.4.3 |
FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-Rule:MF_00235, ECO:0000269|PubMed:166976, ECO:0000269|PubMed:6243627}. | |||
| b0475 | b0475 | Ferrochelatase (EC 4.99.1.1) (Heme synthase) (Protoheme ferro-lyase) | Cytoplasm | R_FCLT_enzyme | R_FCLT | 320 | Translation: 320.0, Folding: 32.0 | 35,884 | UniprotID: P23871 ECnumber: EC 4.99.1.1 |
FUNCTION: Catalyzes the ferrous insertion into protoporphyrin IX. | |
| b4119 | b4119 | Alpha-galactosidase (EC 3.2.1.22) (Melibiase) | Cytoplasm | R_GALS3_enzyme | R_GALS3 | 451 | Translation: 451.0, Folding: 45.1 | 50,657 | UniprotID: P06720 ECnumber: EC 3.2.1.22 |
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| b4388 | b4388 | Phosphoserine phosphatase (PSP) (PSPase) (EC 3.1.3.3) (O-phosphoserine phosphohydrolase) | Cytoplasm | R_PSP_L_enzyme | R_PSP_L | 322 | Translation: 322.0, Folding: 32.2 | 35,043 | UniprotID: P0AGB0 ECnumber: EC 3.1.3.3 |
FUNCTION: Catalyzes the dephosphorylation of phosphoserine (P-Ser). Also catalyzes the hydrolysis of phosphothreonine (P-Thr). {ECO:0000269|PubMed:16990279}. | |
| b2150 | b2150 | D-galactose-binding periplasmic protein (GBP) (D-galactose/ D-glucose-binding protein) (GGBP) | Periplasm | R_GALabcpp_enzyme R_GLCabcpp_enzyme |
R_GALabcpp R_GLCabcpp |
332 | Secretion: 332.0, Translation: 332.0, Folding: 33.2 | 35,713 | UniprotID: P0AEE5 | FUNCTION: This protein is involved in the active transport of galactose and glucose. It plays a role in the chemotaxis towards the two sugars by interacting with the trg chemoreceptor. | |
| b1415 | b1415 | Lactaldehyde dehydrogenase (EC 1.2.1.22) (Aldehyde dehydrogenase A) (Glycolaldehyde dehydrogenase) (EC 1.2.1.21) | Cytoplasm | R_GCALDD_enzyme R_LCADi_enzyme |
R_GCALDD R_LCADi |
479 | Translation: 479.0, Folding: 47.9 | 52,273 | UniprotID: P25553 ECnumber: EC 1.2.1.22; 1.2.1.21 |
FUNCTION: Acts on lactaldehyde as well as other aldehydes. | |
| b4111 | b4111 | Proline/betaine transporter (Proline porter II) (PPII) | Cell_inner_membrane | R_CRNDt2rpp_enzyme R_CRNt2rpp_enzyme R_CTBTt2rpp_enzyme R_GLYBt2pp_duplicate_2_enzyme R_PROt2rpp_enzyme |
R_CRNDt2rpp R_CRNt2rpp R_CTBTt2rpp R_GLYBt2pp_duplicate_2 R_PROt2rpp |
500 | Secretion: 500.0, Translation: 500.0, Folding: 50.0 | 54,846 | UniprotID: P0C0L7 | FUNCTION: Proton symporter that senses osmotic shifts and responds by importing osmolytes such as proline, glycine betaine, stachydrine, pipecolic acid, ectoine and taurine. It is both an osmosensor and an osmoregulator which is available to participate early in the bacterial osmoregulatory response. {ECO:0000269|PubMed:10026245, ECO:0000269|PubMed:3082857, ECO:0000269|PubMed:8421314}. | |
| b4115 | b4115 | Arginine/agmatine antiporter | Cell_inner_membrane | R_ARGAGMt7pp_enzyme | R_ARGAGMt7pp | 445 | Secretion: 445.0, Translation: 445.0, Folding: 44.5 | 46,843 | UniprotID: P60061 | FUNCTION: Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach (By similarity). Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons. {ECO:0000250, ECO:0000269|PubMed:12867448, ECO:0000269|PubMed:14594828}. | |
| b4117 | b4117 | Biodegradative arginine decarboxylase (ADC) (EC 4.1.1.19) | Cytoplasm | R_ARGDC_enzyme | R_ARGDC | 755 | Translation: 755.0, Folding: 75.5 | 84,425 | UniprotID: P28629 ECnumber: EC 4.1.1.19 |
FUNCTION: ADC can be found in two forms: biodegradative and biosynthetic. The biodegradative form may play a role in regulating pH by consuming proteins. | |
| b4289 | b4289 | Fe(3+) dicitrate transport system permease protein FecC (Iron(III) dicitrate transport system permease protein FecC) | Cell_inner_membrane | R_FE3DCITabcpp_enzyme | R_FE3DCITabcpp | 332 | Secretion: 332.0, Translation: 332.0, Folding: 33.2 | 34,893 | UniprotID: P15030 | FUNCTION: Part of the binding-protein-dependent transport system for citrate-dependent Fe(3+). Probably responsible for the translocation of the substrate across the membrane. | |
| b4288 | b4288 | Fe(3+) dicitrate transport system permease protein FecD (Iron(III) dicitrate transport system permease protein FecD) | Cell_inner_membrane | R_FE3DCITabcpp_enzyme | R_FE3DCITabcpp | 318 | Secretion: 318.0, Translation: 318.0, Folding: 31.8 | 34,131 | UniprotID: P15029 | FUNCTION: Part of the binding-protein-dependent transport system for citrate-dependent Fe(3+). Probably responsible for the translocation of the substrate across the membrane. | |
| b4287 | b4287 | Fe(3+) dicitrate transport ATP-binding protein FecE (Iron(III) dicitrate transport ATP-binding protein FecE) | Cell_inner_membrane | R_FE3DCITabcpp_enzyme | R_FE3DCITabcpp | 255 | Secretion: 255.0, Translation: 255.0, Folding: 25.5 | 28,191 | UniprotID: P15031 | FUNCTION: Part of the binding-protein-dependent transport system for citrate-dependent Fe(3+). Probably responsible for energy coupling to the transport system. | |
| b0099 | b0099 | 8-oxo-dGTP diphosphatase (8-oxo-dGTPase) (EC 3.6.1.55) (7,8-dihydro-8-oxoguanine-triphosphatase) (Mutator protein MutT) (dGTP pyrophosphohydrolase) | Cytoplasm | R_DNTPPA_enzyme R_NTPP1_enzyme R_NTPP2_enzyme |
R_DNTPPA R_NTPP1 R_NTPP2 |
129 | Translation: 129.0, Folding: 12.9 | 14,927 | UniprotID: P08337 ECnumber: EC 3.6.1.55 |
FUNCTION: Involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA and the nucleotide pool. 8-oxo-dGTP is inserted opposite dA and dC residues of template DNA with almost equal efficiency thus leading to A.T to G.C transversions. MutT specifically degrades 8-oxo-dGTP to the monophosphate. {ECO:0000269|PubMed:1309939, ECO:0000269|PubMed:15850400}. |
|
| b0090 | b0090 | UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase (EC 2.4.1.227) (Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase) | Cell_inner_membrane | R_UAGPT3_enzyme | R_UAGPT3 | 355 | Secretion: 355.0, Translation: 355.0, Folding: 35.5 | 37,815 | UniprotID: P17443 ECnumber: EC 2.4.1.227 |
FUNCTION: Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II). | |
| b0091 | b0091 | UDP-N-acetylmuramate--L-alanine ligase (EC 6.3.2.8) (UDP-N-acetylmuramoyl-L-alanine synthetase) | Cytoplasm | R_UAMAS_enzyme | R_UAMAS | 491 | Translation: 491.0, Folding: 49.1 | 53,626 | UniprotID: P17952 ECnumber: EC 6.3.2.8 |
FUNCTION: Cell wall formation. {ECO:0000269|PubMed:7601127}. | |
| b0092 | b0092 | D-alanine--D-alanine ligase B (EC 6.3.2.4) (D-Ala-D-Ala ligase B) (D-alanylalanine synthetase B) | Cytoplasm | R_ALAALAr_duplicate_2_enzyme | R_ALAALAr_duplicate_2 | 306 | Translation: 306.0, Folding: 30.6 | 32,840 | UniprotID: P07862 ECnumber: EC 6.3.2.4 |
FUNCTION: Cell wall formation. | |
| b3430 | b3430 | Glucose-1-phosphate adenylyltransferase (EC 2.7.7.27) (ADP-glucose pyrophosphorylase) (ADPGlc PPase) (ADP-glucose synthase) | Cytoplasm | R_GLGC_enzyme | R_GLGC | 431 | Translation: 431.0, Folding: 43.1 | 48,698 | UniprotID: P0A6V1 ECnumber: EC 2.7.7.27 |
FUNCTION: Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc. {ECO:0000269|PubMed:1648099}. | |
| b0096 | b0096 | UDP-3-O-acyl-N-acetylglucosamine deacetylase (UDP-3-O-acyl-GlcNAc deacetylase) (EC 3.5.1.108) (Protein EnvA) (UDP-3-O-[R-3-hydroxymyristoyl]-N-acetylglucosamine deacetylase) | Cytoplasm | R_UHGADA_enzyme | R_UHGADA | 305 | Translation: 305.0, Folding: 30.5 | 33,956 | UniprotID: P0A725 ECnumber: EC 3.5.1.108 |
FUNCTION: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00388, ECO:0000269|PubMed:10026271, ECO:0000269|PubMed:8530464, ECO:0000269|PubMed:8824222, ECO:0000269|Ref.7}. | |
| b0273 | b0273 | Ornithine carbamoyltransferase subunit F (OTCase-2) (EC 2.1.3.3) | Cytoplasm | R_OCBT_duplicate_2_enzyme | R_OCBT_duplicate_2 | 334 | Translation: 334.0, Folding: 33.4 | 36,827 | UniprotID: P06960 ECnumber: EC 2.1.3.3 |
FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. {ECO:0000269|PubMed:789338}. | |
| b0026 | b0026 | Isoleucine--tRNA ligase (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (IleRS) | Cytoplasm | R_ILETRS_enzyme | R_ILETRS | 938 | Translation: 938.0, Folding: 93.8 | 104,297 | UniprotID: P00956 ECnumber: EC 6.1.1.5 |
FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as pretransfer editing and involves the hydrolysis of activated Val-AMP. The other activity is designated posttransfer editing and involves deacylation of mischarged Val-tRNA(Ile). |
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| b4025 | b4025 | Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) (Phosphoglucose isomerase) (PGI) (Phosphohexose isomerase) (PHI) | Cytoplasm | R_PGI_enzyme | R_PGI | 549 | Translation: 549.0, Folding: 54.9 | 61,530 | UniprotID: P0A6T1 ECnumber: EC 5.3.1.9 |
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| b0077 | b0077 | Acetolactate synthase isozyme 3 large subunit (EC 2.2.1.6) (AHAS-III) (ALS-III) (Acetohydroxy-acid synthase III large subunit) | Cytoplasm | R_ACHBS_duplicate_2_enzyme R_ACLS_duplicate_2_enzyme |
R_ACHBS_duplicate_2 R_ACLS_duplicate_2 |
574 | Translation: 574.0, Folding: 57.4 | 62,984 | UniprotID: P00893 ECnumber: EC 2.2.1.6 |
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| b0074 | b0074 | 2-isopropylmalate synthase (EC 2.3.3.13) (Alpha-IPM synthase) (Alpha-isopropylmalate synthase) | Cytoplasm | R_IPPS_enzyme | R_IPPS | 523 | Translation: 523.0, Folding: 52.3 | 57,298 | UniprotID: P09151 ECnumber: EC 2.3.3.13 |
FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). | |
| b0072 | b0072 | 3-isopropylmalate dehydratase large subunit (EC 4.2.1.33) (Alpha-IPM isomerase) (IPMI) (Isopropylmalate isomerase) | Cytoplasm | R_IPPMIa_enzyme R_IPPMIb_enzyme |
R_IPPMIa R_IPPMIb |
466 | Translation: 466.0, Folding: 46.6 | 49,882 | UniprotID: P0A6A6 ECnumber: EC 4.2.1.33 |
FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | |
| b0073 | b0073 | 3-isopropylmalate dehydrogenase (EC 1.1.1.85) (3-IPM-DH) (Beta-IPM dehydrogenase) (IMDH) | Cytoplasm | R_IPMD_enzyme | R_IPMD | 363 | Translation: 363.0, Folding: 36.3 | 39,517 | UniprotID: P30125 ECnumber: EC 1.1.1.85 |
FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. {ECO:0000255|HAMAP-Rule:MF_01033, ECO:0000269|PubMed:9003442}. | |
| b0070 | b0070 | Sugar efflux transporter A | Cell_inner_membrane | R_LCTSt3ipp_enzyme | R_LCTSt3ipp | 392 | Secretion: 392.0, Translation: 392.0, Folding: 39.2 | 42,713 | UniprotID: P31675 | FUNCTION: Involved in the efflux of sugars. The physiological role may be the detoxification of non-metabolizable sugar analogs. Can transport IPTG, lactose and glucose. Has broad substrate specificity, with preferences for glucosides or galactosides with alkyl or aryl substituents. | |
| b0071 | b0071 | 3-isopropylmalate dehydratase small subunit (EC 4.2.1.33) (Alpha-IPM isomerase) (IPMI) (Isopropylmalate isomerase) | Cytoplasm | R_IPPMIa_enzyme R_IPPMIb_enzyme |
R_IPPMIa R_IPPMIb |
201 | Translation: 201.0, Folding: 20.1 | 22,487 | UniprotID: P30126 ECnumber: EC 4.2.1.33 |
FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | |
| b0078 | b0078 | Acetolactate synthase isozyme 3 small subunit (EC 2.2.1.6) (ALS-III) (Acetohydroxy-acid synthase III small subunit) (AHAS-III) | Cytoplasm | R_ACHBS_duplicate_2_enzyme R_ACLS_duplicate_2_enzyme |
R_ACHBS_duplicate_2 R_ACLS_duplicate_2 |
163 | Translation: 163.0, Folding: 16.3 | 17,977 | UniprotID: P00894 ECnumber: EC 2.2.1.6 |
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| b0386 | b0386 | Pyrroline-5-carboxylate reductase (P5C reductase) (P5CR) (EC 1.5.1.2) (PCA reductase) | Cytoplasm | R_P5CR_enzyme | R_P5CR | 269 | Translation: 269.0, Folding: 26.9 | 28,145 | UniprotID: P0A9L8 ECnumber: EC 1.5.1.2 |
FUNCTION: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. Does not catalyze the reverse reaction. {ECO:0000255|HAMAP-Rule:MF_01925, ECO:0000269|PubMed:12133, ECO:0000269|PubMed:6296787}. | |
| b0381 | b0381 | D-alanine--D-alanine ligase A (EC 6.3.2.4) (D-Ala-D-Ala ligase A) (D-alanylalanine synthetase A) | Cytoplasm | R_ALAALAr_enzyme | R_ALAALAr | 364 | Translation: 364.0, Folding: 36.4 | 39,316 | UniprotID: P0A6J8 ECnumber: EC 6.3.2.4 |
FUNCTION: Cell wall formation. | |
| b0383 | b0383 | Alkaline phosphatase (APase) (EC 3.1.3.1) | Periplasm | R_PPTHpp_enzyme | R_PPTHpp | 471 | Secretion: 471.0, Translation: 471.0, Folding: 47.1 | 49,439 | UniprotID: P00634 ECnumber: EC 3.1.3.1 |
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| b0388 | b0388 | Shikimate kinase 2 (SK 2) (EC 2.7.1.71) (Shikimate kinase II) (SKII) | Cytoplasm | R_SHKK_duplicate_2_enzyme | R_SHKK_duplicate_2 | 174 | Translation: 174.0, Folding: 17.4 | 19,151 | UniprotID: P0A6E1 ECnumber: EC 2.7.1.71 |
FUNCTION: Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. {ECO:0000269|PubMed:3001029, ECO:0000269|PubMed:3026317}. | |
| b3972 | b3972 | UDP-N-acetylenolpyruvoylglucosamine reductase (EC 1.3.1.98) (UDP-N-acetylmuramate dehydrogenase) | Cytoplasm | R_UAPGR_enzyme | R_UAPGR | 342 | Translation: 342.0, Folding: 34.2 | 37,851 | UniprotID: P08373 ECnumber: EC 1.3.1.98 |
FUNCTION: Cell wall formation. | |
| b0731 | b0731 | PTS system 2-O-alpha-mannosyl-D-glycerate-specific EIIABC component (2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme MngA) (Protein-Npi-phosphohistidine--2-O-alpha-mannosyl-D-glycerate phosphotransferase) [Includes: 2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme IIA component (EC 2.7.1.195) (PTS system EIIA component); 2-O-alpha-mannosyl-D-glycerate-specific phosphotransferase enzyme IIB component (EC 2.7.1.195) (PTS system EIIB component); 2-O-alpha-mannosyl-D-glycerate-specific permease IIC component (PTS system EIIC component) |
Cell_inner_membrane | R_MANGLYCptspp_enzyme | R_MANGLYCptspp | 658 | Secretion: 658.0, Translation: 658.0, Folding: 65.8 | 69,668 | UniprotID: P54745 ECnumber: EC 2.7.1.195; 2.7.1.195 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane (PubMed:14645248, PubMed:9063979). This system is involved in mannosyl-D-glycerate transport (PubMed:14645248). Also involved in thermoinduction of ompC (PubMed:9063979). {ECO:0000269|PubMed:14645248, ECO:0000269|PubMed:9063979}. |
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| b0639 | b0639 | Nicotinate-nucleotide adenylyltransferase (EC 2.7.7.18) (Deamido-NAD(+) diphosphorylase) (Deamido-NAD(+) pyrophosphorylase) (Nicotinate mononucleotide adenylyltransferase) (NaMN adenylyltransferase) | Cytoplasm | R_NMNAT_duplicate_2_enzyme R_NNATr_enzyme |
R_NMNAT_duplicate_2 R_NNATr |
213 | Translation: 213.0, Folding: 21.3 | 24,528 | UniprotID: P0A752 ECnumber: EC 2.7.7.18 |
FUNCTION: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). {ECO:0000269|PubMed:10894752}. | |
| b3012 | b3012 | 2,5-diketo-D-gluconic acid reductase A (2,5-DKG reductase A) (2,5-DKGR A) (25DKGR-A) (EC 1.1.1.274) (AKR5C) | Cytoplasm | R_ALR2_duplicate_2_enzyme R_DKGLCNR1_duplicate_2_enzyme |
R_ALR2_duplicate_2 R_DKGLCNR1_duplicate_2 |
275 | Translation: 275.0, Folding: 27.5 | 31,110 | UniprotID: Q46857 ECnumber: EC 1.1.1.274 |
FUNCTION: Catalyzes the reduction of 2,5-diketo-D-gluconic acid (25DKG) to 2-keto-L-gulonic acid (2KLG). It is also capable of stereoselective -keto ester reductions on ethyl acetoacetate and other 2-substituted derivatives. | |
| b3018 | b3018 | 1-acyl-sn-glycerol-3-phosphate acyltransferase (1-AGP acyltransferase) (1-AGPAT) (EC 2.3.1.51) (EC 2.3.1.n4) (Lysophosphatidic acid acyltransferase) (LPAAT) (Phosphatidic acid synthase) (PA synthase) | Cell_inner_membrane | R_AGPAT120 R_AGPAT140 R_AGPAT141 R_AGPAT160 R_AGPAT161 R_AGPAT180 R_AGPAT181 |
245 | Secretion: 245.0, Translation: 245.0, Folding: 24.5 | 27,453 | UniprotID: P26647 ECnumber: EC 2.3.1.51; 2.3.1.n4 |
FUNCTION: Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating an acyl moiety at the 2 position. This enzyme can utilize either acyl-CoA or acyl-ACP as the fatty acyl donor. {ECO:0000269|PubMed:2211622}. | ||
| b3729 | b3729 | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] (EC 2.6.1.16) (D-fructose-6-phosphate amidotransferase) (GFAT) (Glucosamine-6-phosphate synthase) (Hexosephosphate aminotransferase) (L-glutamine--D-fructose-6-phosphate amidotransferase) | Cytoplasm | R_GF6PTA_enzyme | R_GF6PTA | 609 | Translation: 609.0, Folding: 60.9 | 66,894 | UniprotID: P17169 ECnumber: EC 2.6.1.16 |
FUNCTION: Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source. | |
| b3728 | b3728 | Phosphate-binding protein PstS (PBP) | Periplasm | R_PIuabcpp_enzyme | R_PIuabcpp | 346 | Secretion: 346.0, Translation: 346.0, Folding: 34.6 | 37,024 | UniprotID: P0AG82 | FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. | |
| b3722 | b3722 | PTS system beta-glucoside-specific EIIBCA component (EIIBCA-Bgl) (EII-Bgl) [Includes: Beta-glucoside-specific phosphotransferase enzyme IIB component (EC 2.7.1.-) (PTS system beta-glucoside-specific EIIB component); Beta-glucoside permease IIC component (PTS system beta-glucoside-specific EIIC component); Beta-glucoside-specific phosphotransferase enzyme IIA component (PTS system beta-glucoside-specific EIIA component) |
Cell_inner_membrane | R_ARBTptspp_enzyme | R_ARBTptspp | 625 | Secretion: 625.0, Translation: 625.0, Folding: 62.5 | 66,483 | UniprotID: P08722 ECnumber: EC 2.7.1.- |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active -transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in beta-glucoside transport.; FUNCTION: Acts as both a kinase and a phosphatase on BglG. | |
| b3727 | b3727 | Phosphate transport system permease protein PstC | Cell_inner_membrane | R_PIuabcpp_enzyme | R_PIuabcpp | 319 | Secretion: 319.0, Translation: 319.0, Folding: 31.9 | 34,121 | UniprotID: P0AGH8 | FUNCTION: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane. | |
| b3726 | b3726 | Phosphate transport system permease protein PstA | Cell_inner_membrane | R_PIuabcpp_enzyme | R_PIuabcpp | 296 | Secretion: 296.0, Translation: 296.0, Folding: 29.6 | 32,322 | UniprotID: P07654 | FUNCTION: Part of the binding-protein-dependent transport system for phosphate; probably responsible for the translocation of the substrate across the membrane. | |
| b3725 | b3725 | Phosphate import ATP-binding protein PstB (EC 3.6.3.27) (ABC phosphate transporter) (Phosphate-transporting ATPase) | Cell_inner_membrane | R_PIuabcpp_enzyme | R_PIuabcpp | 257 | Secretion: 257.0, Translation: 257.0, Folding: 25.7 | 29,027 | UniprotID: P0AAH0 ECnumber: EC 3.6.3.27 |
FUNCTION: Part of the ABC transporter complex PstSACB involved in phosphate import. Responsible for energy coupling to the transport system. | |
| b3236 | b3236 | Malate dehydrogenase (EC 1.1.1.37) | Cytoplasm | R_MDH_enzyme | R_MDH | 312 | Translation: 312.0, Folding: 31.2 | 32,337 | UniprotID: P61889 ECnumber: EC 1.1.1.37 |
FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate. {ECO:0000255|HAMAP-Rule:MF_01516, ECO:0000269|PubMed:2993232, ECO:0000269|PubMed:7028159}. | |
| b2478 | b2478 | 4-hydroxy-tetrahydrodipicolinate synthase (HTPA synthase) (EC 4.3.3.7) | Cytoplasm | R_DHDPS_enzyme | R_DHDPS | 292 | Translation: 292.0, Folding: 29.2 | 31,270 | UniprotID: P0A6L2 ECnumber: EC 4.3.3.7 |
FUNCTION: Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). {ECO:0000255|HAMAP-Rule:MF_00418, ECO:0000269|PubMed:20503968, ECO:0000269|PubMed:8993314}. | |
| b3092 | b3092 | Uronate isomerase (EC 5.3.1.12) (Glucuronate isomerase) (Uronic isomerase) | Cytoplasm | R_GUI1_enzyme R_GUI2_enzyme |
R_GUI1 R_GUI2 |
470 | Translation: 470.0, Folding: 47.0 | 53,987 | UniprotID: P0A8G3 ECnumber: EC 5.3.1.12 |
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| b3128 | b3128 | Galactarate dehydratase (L-threo-forming) (GalcD) (EC 4.2.1.42) | Cytoplasm | R_GALCTD_enzyme | R_GALCTD | 523 | Translation: 523.0, Folding: 52.3 | 56,402 | UniprotID: P39829 ECnumber: EC 4.2.1.42 |
FUNCTION: Catalyzes the dehydration of galactarate to form 5-dehydro-4-deoxy-D-glucarate. {ECO:0000255|HAMAP-Rule:MF_02031, ECO:0000269|PubMed:9772162}. | |
| b3125 | b3125 | 2-hydroxy-3-oxopropionate reductase (EC 1.1.1.60) (Tartronate semialdehyde reductase) (TSAR) | Cytoplasm | R_TRSARr_duplicate_2_enzyme | R_TRSARr_duplicate_2 | 294 | Translation: 294.0, Folding: 29.4 | 30,427 | UniprotID: P0ABQ2 ECnumber: EC 1.1.1.60 |
FUNCTION: Catalyzes the reduction of tatronate semialdehyde to D-glycerate. {ECO:0000255|HAMAP-Rule:MF_02032, ECO:0000269|PubMed:9772162}. | |
| b3124 | b3124 | Glycerate 2-kinase (EC 2.7.1.165) (Glycerate kinase 1) (GK1) | Cytoplasm | R_GLYCK2_enzyme | R_GLYCK2 | 381 | Translation: 381.0, Folding: 38.1 | 39,104 | UniprotID: P23524 ECnumber: EC 2.7.1.165 |
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| b3127 | b3127 | Probable galactarate transporter (D-galactarate permease) | Cell_inner_membrane | R_GALCTt2rpp_duplicate_2_enzyme R_GLCRt2rpp_enzyme R_GLYCAt2rpp_duplicate_2_enzyme |
R_GALCTt2rpp_duplicate_2 R_GLCRt2rpp R_GLYCAt2rpp_duplicate_2 |
444 | Secretion: 444.0, Translation: 444.0, Folding: 44.4 | 49,009 | UniprotID: P0AA80 | FUNCTION: Uptake of D-galactarate. | |
| b3654 | b3654 | Xanthine permease XanP | Cell_inner_membrane | R_ADEt2rpp_enzyme R_GUAt2pp_enzyme R_XANt2pp_enzyme |
R_ADEt2rpp R_GUAt2pp R_XANt2pp |
463 | Secretion: 463.0, Translation: 463.0, Folding: 46.3 | 48,868 | UniprotID: P0AGM9 | FUNCTION: Specific, proton motive force-dependent high-affinity transporter for xanthine. {ECO:0000269|PubMed:16096267}. | |
| b3653 | b3653 | Sodium/glutamate symporter (Glutamate permease) | Cell_inner_membrane | R_GLUt4pp_enzyme | R_GLUt4pp | 401 | Secretion: 401.0, Translation: 401.0, Folding: 40.1 | 42,425 | UniprotID: P0AER8 | FUNCTION: Catalyzes the sodium-dependent, binding-protein-independent transport of glutamate. {ECO:0000255|HAMAP-Rule:MF_02062, ECO:0000269|PubMed:2537813, ECO:0000269|PubMed:336628, ECO:0000269|PubMed:8596452}. | |
| b3650 | b3650 | Bifunctional (p)ppGpp synthase/hydrolase SpoT [Includes: GTP pyrophosphokinase (EC 2.7.6.5) ((p)ppGpp synthase) (ATP:GTP 3-pyrophosphotransferase) (Stringent response-like protein) (ppGpp synthase II); Guanosine-3 5-bis(diphosphate) 3-pyrophosphohydrolase (EC 3.1.7.2) (Penta-phosphate guanosine-3-pyrophosphohydrolase) ((ppGpp)ase) | Cytoplasm | R_GDPDPK_duplicate_2_enzyme R_GDPTPDP_enzyme R_PPGPPDP_enzyme |
R_GDPDPK_duplicate_2 R_GDPTPDP R_PPGPPDP |
702 | Translation: 702.0, Folding: 70.2 | 79,342 | UniprotID: P0AG24 ECnumber: EC 2.7.6.5; 3.1.7.2 |
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| b2838 | b2838 | Diaminopimelate decarboxylase (DAP decarboxylase) (DAPDC) (EC 4.1.1.20) | Cytoplasm | R_DAPDC_enzyme | R_DAPDC | 420 | Translation: 420.0, Folding: 42.0 | 46,177 | UniprotID: P00861 ECnumber: EC 4.1.1.20 |
FUNCTION: Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine. Is not active against the DD- or LL-isomers of diaminopimelate. {ECO:0000269|PubMed:11856852, ECO:0000269|PubMed:14343156, ECO:0000269|PubMed:18508763}. | |
| b3835 | b3835 | Probable protein kinase UbiB (EC 2.7.-.-) (Ubiquinone biosynthesis protein UbiB) | Cell_inner_membrane | R_OPHHX_enzyme | R_OPHHX | 546 | Secretion: 546.0, Translation: 546.0, Folding: 54.6 | 63,203 | UniprotID: P0A6A0 ECnumber: EC 2.7.-.- |
FUNCTION: Is probably a protein kinase regulator of UbiI activity which is involved in aerobic coenzyme Q (ubiquinone) biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00414, ECO:0000269|PubMed:10960098, ECO:0000269|PubMed:9422602}. | |
| b3833 | b3833 | Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE (EC 2.1.1.163) (EC 2.1.1.201) (2-methoxy-6-polyprenyl-1,4-benzoquinol methylase) (Demethylmenaquinone methyltransferase) | Cytoplasm | R_AMMQLT8_enzyme R_OMBZLM_enzyme |
R_AMMQLT8 R_OMBZLM |
251 | Translation: 251.0, Folding: 25.1 | 28,073 | UniprotID: P0A887 ECnumber: EC 2.1.1.163; 2.1.1.201 |
FUNCTION: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2). {ECO:0000255|HAMAP-Rule:MF_01813, ECO:0000269|PubMed:9045837}. | |
| b2528 | b2528 | Iron-binding protein IscA (Iron-sulfur cluster assembly protein) | Cytoplasm | R_I2FE2ST_enzyme R_I4FE4ST_enzyme |
R_I2FE2ST R_I4FE4ST |
107 | Translation: 107.0, Folding: 10.7 | 11,556 | UniprotID: P0AAC8 | FUNCTION: Is able to transfer iron-sulfur clusters to apo-ferredoxin. Multiple cycles of [2Fe2S] cluster formation and transfer are observed, suggesting that IscA acts catalytically. Recruits intracellular free iron so as to provide iron for the assembly of transient iron-sulfur cluster in IscU in the presence of IscS, L-cysteine and the thioredoxin reductase system TrxA/TrxB. | |
| b2529 | b2529 | Iron-sulfur cluster assembly scaffold protein IscU (Sulfur acceptor protein IscU) | Cytoplasm | R_I2FE2SR_enzyme R_I2FE2SS_enzyme R_I2FE2SS2_enzyme R_I2FE2ST_enzyme R_I4FE4SR_enzyme R_I4FE4ST_enzyme |
R_I2FE2SR R_I2FE2SS R_I2FE2SS2 R_I2FE2ST R_I4FE4SR R_I4FE4ST |
128 | Translation: 128.0, Folding: 12.8 | 13,849 | UniprotID: P0ACD4 | FUNCTION: A scaffold on which IscS assembles Fe-S clusters. Exists as 2 interconverting forms, a structured (S) and disordered (D) form. The D-state is the preferred substrate for IscS. Converts to the S-state when an Fe-S cluster is assembled, which helps it dissociate from IscS to transfer the Fe-S to an acceptor. It is likely that Fe-S cluster coordination is flexible as the role of this complex is to build and then hand off Fe-S clusters. {ECO:0000269|PubMed:11577100, ECO:0000269|PubMed:22203963}. |
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| b2296 | b2296 | Acetate kinase (EC 2.7.2.1) (Acetokinase) | Cytoplasm | R_ACKr_enzyme | R_ACKr | 400 | Translation: 400.0, Folding: 40.0 | 43,290 | UniprotID: P0A6A3 ECnumber: EC 2.7.2.1 |
FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. During anaerobic growth of the organism, this enzyme is also involved in the synthesis of most of the ATP formed catabolically. | |
| b2297 | b2297 | Phosphate acetyltransferase (EC 2.3.1.8) (Phosphotransacetylase) | Cytoplasm | R_PTA2_enzyme R_PTAr_enzyme |
R_PTA2 R_PTAr |
714 | Translation: 714.0, Folding: 71.4 | 77,172 | UniprotID: P0A9M8 ECnumber: EC 2.3.1.8 |
FUNCTION: Involved in acetate metabolism. Catalyzes the reversible interconversion of acetyl-CoA and acetyl phosphate. The direction of the overall reaction changes depending on growth conditions. On minimal medium acetyl-CoA is generated. In rich medium acetyl-CoA is converted to acetate and allowing the cell to dump the excess of acetylation potential in exchange for energy in the form of ATP. {ECO:0000269|PubMed:15687190}. |
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| b2290 | b2290 | Glutamate-pyruvate aminotransferase AlaA (EC 2.6.1.2) | Cytoplasm | R_ALATA_L_enzyme | R_ALATA_L | 405 | Translation: 405.0, Folding: 40.5 | 45,517 | UniprotID: P0A959 ECnumber: EC 2.6.1.2 |
FUNCTION: Involved in the biosynthesis of alanine. {ECO:0000269|PubMed:20729367}. | |
| b2291 | b2291 | 5-deoxynucleotidase YfbR (EC 3.1.3.89) (5-deoxyribonucleotidase) (Nucleoside 5-monophosphate phosphohydrolase) | Cytoplasm | R_NTD1_duplicate_2 R_NTD12 R_NTD3_duplicate_2 R_NTD5_duplicate_2 R_NTD6 R_NTD8 |
199 | Translation: 199.0, Folding: 19.9 | 22,708 | UniprotID: P76491 ECnumber: EC 3.1.3.89 |
FUNCTION: Essential component of the deoxycytidine triphosphate (dCTP) pathway for de novo synthesis of thymidylate. Catalyzes the strictly specific dephosphorylation of 2-deoxyribonucleoside 5-monophosphates (dAMP, dGMP, dTMP, dUMP, dIMP and dCMP) and does not dephosphorylate 5-ribonucleotides or ribonucleoside 3-monophosphates. {ECO:0000269|PubMed:15489502, ECO:0000269|PubMed:17827303, ECO:0000269|PubMed:18353368}. |
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| b2836 | b2836 | Bifunctional protein Aas [Includes: 2-acylglycerophosphoethanolamine acyltransferase (EC 2.3.1.40) (2-acyl-GPE acyltransferase) (Acyl-[acyl-carrier-protein]--phospholipid O-acyltransferase); Acyl-[acyl-carrier-protein] synthetase (EC 6.2.1.20) (Acyl-ACP synthetase) (Long-chain-fatty-acid--[acyl-carrier-protein] ligase) | Cell_inner_membrane | R_2AGPEAT120_enzyme R_2AGPEAT140_enzyme R_2AGPEAT141_enzyme R_2AGPEAT160_enzyme R_2AGPEAT161_enzyme R_2AGPEAT180_enzyme R_2AGPEAT181_enzyme R_2AGPGAT120_enzyme R_2AGPGAT140_enzyme R_2AGPGAT141_enzyme R_2AGPGAT160_enzyme R_2AGPGAT161_enzyme R_2AGPGAT180_enzyme R_2AGPGAT181_enzyme R_AACPS1_enzyme R_AACPS2_enzyme R_AACPS3_enzyme R_AACPS4_enzyme R_AACPS5_enzyme R_AACPS6_enzyme R_AACPS7_enzyme R_AACPS8_enzyme R_AACPS9_enzyme |
719 | Secretion: 719.0, Translation: 719.0, Folding: 71.9 | 80,700 | UniprotID: P31119 ECnumber: EC 2.3.1.40; 6.2.1.20 |
FUNCTION: Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3-phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1. {ECO:0000255|HAMAP-Rule:MF_01162, ECO:0000269|PubMed:1649829}. |
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| b2521 | b2521 | 3-mercaptopyruvate sulfurtransferase (MST) (EC 2.8.1.2) (Rhodanese-like protein) | Cytoplasm | R_MCPST_enzyme | R_MCPST | 281 | Translation: 281.0, Folding: 28.1 | 30,812 | UniprotID: P31142 ECnumber: EC 2.8.1.2 |
FUNCTION: Transfers a sulfur ion to cyanide or to other thiol compounds. Also has weak rhodanese activity (130-fold lower). Its participation in detoxification of cyanide may be small. May be involved in the enhancement of serine sensitivity. | |
| b3479 | b3479 | Nickel import ATP-binding protein NikD (EC 3.6.3.24) | Cell_inner_membrane | R_NI2uabcpp_enzyme | R_NI2uabcpp | 254 | Secretion: 254.0, Translation: 254.0, Folding: 25.4 | 26,820 | UniprotID: P33593 ECnumber: EC 3.6.3.24 |
FUNCTION: Part of the ABC transporter complex NikABCDE involved in nickel import. Responsible for energy coupling to the transport system. {ECO:0000255|HAMAP-Rule:MF_01711}. | |
| b2746 | b2746 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (MECDP-synthase) (MECPP-synthase) (MECPS) (EC 4.6.1.12) | Cytoplasm | R_MECDPS_enzyme | R_MECDPS | 159 | Translation: 159.0, Folding: 15.9 | 16,898 | UniprotID: P62617 ECnumber: EC 4.6.1.12 |
FUNCTION: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP). Also converts 4-diphosphocytidyl-2-C-methyl-D-erythritol into 2-C-methyl-D-erythritol 3,4-cyclophosphate and CMP. {ECO:0000269|PubMed:10694574, ECO:0000269|PubMed:22839733}. |
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| b2747 | b2747 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (EC 2.7.7.60) (4-diphosphocytidyl-2C-methyl-D-erythritol synthase) (CDP-ME synthase) (MEP cytidylyltransferase) (MCT) | Cytoplasm | R_MEPCT_enzyme | R_MEPCT | 236 | Translation: 236.0, Folding: 23.6 | 25,737 | UniprotID: Q46893 ECnumber: EC 2.7.7.60 |
FUNCTION: Catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP). | |
| b2744 | b2744 | 5/3-nucleotidase SurE (EC 3.1.3.5) (EC 3.1.3.6) (Exopolyphosphatase) (EC 3.6.1.11) (Nucleoside monophosphate phosphohydrolase) (Stationary-phase survival protein SurE) | Cytoplasm | 253 | Translation: 253.0, Folding: 25.3 | 26,900 | UniprotID: P0A840 ECnumber: EC 3.1.3.5; 3.1.3.6; 3.6.1.11 |
FUNCTION: Nucleotidase with a broad substrate specificity as it can dephosphorylate various ribo- and deoxyribonucleoside 5-monophosphates and ribonucleoside 3-monophosphates with highest affinity to 3-AMP. Also hydrolyzes polyphosphate (exopolyphosphatase activity) with the preference for short-chain-length substrates (P20-25). Might be involved in the regulation of dNTP and NTP pools, and in the turnover of 3-mononucleotides produced by numerous intracellular RNases (T1, T2, and F) during the degradation of various RNAs. Also plays a significant physiological role in stress-response and is required for the survival of E.coli in stationary growth phase. {ECO:0000269|PubMed:15489502}. |
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| b3903 | b3903 | L-rhamnose isomerase (EC 5.3.1.14) | Cytoplasm | R_LYXI_enzyme R_RMI_enzyme |
R_LYXI R_RMI |
419 | Translation: 419.0, Folding: 41.9 | 47,199 | UniprotID: P32170 ECnumber: EC 5.3.1.14 |
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| b3902 | b3902 | Rhamnulose-1-phosphate aldolase (EC 4.1.2.19) | Cytoplasm | R_RMPA_enzyme | R_RMPA | 274 | Translation: 274.0, Folding: 27.4 | 30,145 | UniprotID: P32169 ECnumber: EC 4.1.2.19 |
FUNCTION: Catalyzes the reversible cleavage of L-rhamnulose-1-phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde (PubMed:12962479). Also catalyzes the dephosphorylation of phospho-serine in vitro (PubMed:25848029). {ECO:0000269|PubMed:12962479, ECO:0000269|PubMed:25848029}. | |
| b3907 | b3907 | L-rhamnose-proton symporter (L-rhamnose-H(+) transport protein) | Cell_inner_membrane | R_LYXt2pp_enzyme R_RMNtpp_enzyme |
R_LYXt2pp R_RMNtpp |
344 | Secretion: 344.0, Translation: 344.0, Folding: 34.4 | 37,320 | UniprotID: P27125 | FUNCTION: Uptake of L-rhamnose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Can also transport L-mannose and L-xylose, but at reduced rates. | |
| b3904 | b3904 | L-Rhamnulokinase (RhaB) (RhuK) (EC 2.7.1.5) (ATP:L-rhamnulose phosphotransferase) (L-rhamnulose 1-kinase) (Rhamnulose kinase) | Cytoplasm | R_RMK_enzyme | R_RMK | 489 | Translation: 489.0, Folding: 48.9 | 54,069 | UniprotID: P32171 ECnumber: EC 2.7.1.5 |
FUNCTION: Involved in the catabolism of L-rhamnose (6-deoxy-L-mannose). It could also play a role in the metabolism of some rare sugars such as L-fructose. Catalyzes the transfer of the gamma-phosphate group from ATP to the 1-hydroxyl group of L-rhamnulose to yield L-rhamnulose 1-phosphate. Uridine triphosphate (UTP), cytidine 5-triphosphate (CTP), guanosine 5-triphosphate (GTP), and thymidine triphosphate (TTP) also can act as phosphoryl donors. It can also phosphorylate L-fuculose and L-xylulose. {ECO:0000255|HAMAP-Rule:MF_01535, ECO:0000269|PubMed:14264882, ECO:0000269|PubMed:16674975, ECO:0000269|PubMed:5341476}. |
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| b3909 | b3909 | 2-keto-3-deoxygluconate permease (KDG permease) | Cell_inner_membrane | R_DDGLCNt2rpp_enzyme R_GLCURt2rpp_enzyme |
R_DDGLCNt2rpp R_GLCURt2rpp |
327 | Secretion: 327.0, Translation: 327.0, Folding: 32.7 | 33,669 | UniprotID: P0A712 | FUNCTION: The 2-keto-3-deoxygluconate permease transports the degraded pectin products into the bacterial cell, where they serve as carbon and energy sources. This is a hydrogen coupled transport system. | |
| b3908 | b3908 | Superoxide dismutase [Mn] (EC 1.15.1.1) (MnSOD) | Cytoplasm | R_SPODM_enzyme | R_SPODM | 206 | Translation: 206.0, Folding: 20.6 | 23,097 | UniprotID: P00448 ECnumber: EC 1.15.1.1 |
FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | |
| b1982 | b1982 | AMP nucleosidase (EC 3.2.2.4) | Cytoplasm | R_AMPN_enzyme | R_AMPN | 484 | Translation: 484.0, Folding: 48.4 | 53,995 | UniprotID: P0AE12 ECnumber: EC 3.2.2.4 |
FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond of AMP to form adenine and ribose 5-phosphate. Involved in regulation of AMP concentrations. {ECO:0000255|HAMAP-Rule:MF_01932, ECO:0000269|PubMed:7000783}. | |
| b1131 | b1131 | Adenylosuccinate lyase (ASL) (EC 4.3.2.2) (Adenylosuccinase) (ASase) | Cytoplasm | R_ADSL1r_enzyme R_ADSL2r_enzyme |
R_ADSL1r R_ADSL2r |
456 | Translation: 456.0, Folding: 45.6 | 51,543 | UniprotID: P0AB89 ECnumber: EC 4.3.2.2 |
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| b1134 | b1134 | Phosphatase NudJ (EC 3.6.1.-) | Cytoplasm | R_2MAHMP_duplicate_2_enzyme R_TDP_enzyme |
R_2MAHMP_duplicate_2 R_TDP |
153 | Translation: 153.0, Folding: 15.3 | 17,433 | UniprotID: P0AEI6 ECnumber: EC 3.6.1.- |
FUNCTION: Catalyzes the hydrolysis of 4-amino-2-methyl-5-hydroxymethylpyrimidine pyrophosphate (HMP-PP) to 4-amino-2-methyl-5-hydroxymethylpyrimidine phosphate (HMP-P), and hydrolysis of thiamine pyrophosphate (TPP) to thiamine monophosphate (TMP). Can hydrolyze other substrates such as MeO-HMP-PP, CF(3)-HMP-PP and MeO-TPP. Is also a non-specific nucleoside tri- and diphosphatase that releases inorganic orthophosphate. {ECO:0000269|PubMed:15292217, ECO:0000269|PubMed:16766526}. |
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| b1136 | b1136 | Isocitrate dehydrogenase [NADP] (IDH) (EC 1.1.1.42) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) | Cytoplasm | R_ICDHyr_enzyme | R_ICDHyr | 416 | Translation: 416.0, Folding: 41.6 | 45,757 | UniprotID: P08200 ECnumber: EC 1.1.1.42 |
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| b1246 | b1246 | Oligopeptide transport ATP-binding protein OppD | Cell_inner_membrane | R_3PEPTabcpp_enzyme R_4PEPTabcpp_enzyme |
R_3PEPTabcpp R_4PEPTabcpp |
337 | Secretion: 337.0, Translation: 337.0, Folding: 33.7 | 37,188 | UniprotID: P76027 | FUNCTION: Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system. | |
| b1247 | b1247 | Oligopeptide transport ATP-binding protein OppF | Cell_inner_membrane | R_3PEPTabcpp_enzyme R_4PEPTabcpp_enzyme |
R_3PEPTabcpp R_4PEPTabcpp |
334 | Secretion: 334.0, Translation: 334.0, Folding: 33.4 | 37,198 | UniprotID: P77737 | FUNCTION: Part of the binding-protein-dependent transport system for oligopeptides. Probably responsible for energy coupling to the transport system. | |
| b1244 | b1244 | Oligopeptide transport system permease protein OppB | Cell_inner_membrane | R_3PEPTabcpp_enzyme R_4PEPTabcpp_enzyme |
R_3PEPTabcpp R_4PEPTabcpp |
306 | Secretion: 306.0, Translation: 306.0, Folding: 30.6 | 33,443 | UniprotID: P0AFH2 | FUNCTION: Part of the binding-protein-dependent transport system for oligopeptides; probably responsible for the translocation of the substrate across the membrane. | |
| b1713 | b1713 | Phenylalanine--tRNA ligase beta subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase beta subunit) (PheRS) | Cytoplasm | R_PHETRS_enzyme | R_PHETRS | 795 | Translation: 795.0, Folding: 79.5 | 87,378 | UniprotID: P07395 ECnumber: EC 6.1.1.20 |
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| b1714 | b1714 | Phenylalanine--tRNA ligase alpha subunit (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase alpha subunit) (PheRS) | Cytoplasm | R_PHETRS_enzyme | R_PHETRS | 327 | Translation: 327.0, Folding: 32.7 | 36,832 | UniprotID: P08312 ECnumber: EC 6.1.1.20 |
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| b1243 | b1243 | Periplasmic oligopeptide-binding protein | Periplasm | R_4PEPTabcpp_enzyme | R_4PEPTabcpp | 543 | Secretion: 543.0, Translation: 543.0, Folding: 54.3 | 60,899 | UniprotID: P23843 | FUNCTION: This protein is a component of the oligopeptide permease, a binding protein-dependent transport system, it binds peptides up to five amino acids long with high affinity. | |
| b1241 | b1241 | Aldehyde-alcohol dehydrogenase [Includes: Alcohol dehydrogenase (ADH) (EC 1.1.1.1); Acetaldehyde dehydrogenase [acetylating] (ACDH) (EC 1.2.1.10); Pyruvate-formate-lyase deactivase (PFL deactivase) | Cytoplasm | R_ACALD_duplicate_2_enzyme R_ALCD2x_enzyme |
R_ACALD_duplicate_2 R_ALCD2x |
891 | Translation: 891.0, Folding: 89.1 | 96,127 | UniprotID: P0A9Q7 ECnumber: EC 1.1.1.1; 1.2.1.10 |
FUNCTION: This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction. | |
| b1719 | b1719 | Threonine--tRNA ligase (EC 6.1.1.3) (Threonyl-tRNA synthetase) (ThrRS) | Cytoplasm | R_THRTRS_enzyme | R_THRTRS | 642 | Translation: 642.0, Folding: 64.2 | 74,014 | UniprotID: P0A8M3 ECnumber: EC 6.1.1.3 |
FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr) (PubMed:15079065, PubMed:10881191, PubMed:18997014). The rate-limiting step is amino acid activation in the presence of tRNA (PubMed:18997014). The 2-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively (PubMed:18997014). The zinc ion in the active site discriminates against charging of the isosteric amino acid valine (PubMed:10881191). Also activates L-serine, but does not detectably transfer it to tRNA(Thr) (PubMed:15079065). Edits incorrectly charged L-seryl-tRNA(Thr) via its editing domain (PubMed:15079065, PubMed:11136973, PubMed:15525511), in a post-transfer reaction probably via water-mediated hydrolysis (PubMed:15525511). {ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:10881191, ECO:0000269|PubMed:11136973, ECO:0000269|PubMed:15079065, ECO:0000269|PubMed:15525511, ECO:0000269|PubMed:18997014}.; FUNCTION: ThrS is also a translational repressor protein, it controls binds its own mRNA in the operator region upstream of the start codon (PubMed:3086882). The mRNA region upstream of the start codon has a tRNA-like secondary structure; mRNA and tRNA compete for binding to ThrRS (PubMed:2254931). ThrRS represses translation by preventing the ribosome from to mRNA, and tRNA(Thr) acts as an antirepressor allowing fine level control of enzyme synthesis (PubMed:2254931). X-ray structures prove that operator mRNA and tRNA bind to overlapping sites in the protein (PubMed:10319817, PubMed:11953757). {ECO:0000269|PubMed:10319817, ECO:0000269|PubMed:11953757, ECO:0000269|PubMed:2254931, ECO:0000269|PubMed:3086882}. |
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| b1249 | b1249 | Cardiolipin synthase A (CL synthase) (EC 2.7.8.-) | Cell_inner_membrane | 486 | Secretion: 486.0, Translation: 486.0, Folding: 48.6 | 54,822 | UniprotID: P0A6H8 ECnumber: EC 2.7.8.- |
FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol. {ECO:0000255|HAMAP-Rule:MF_00190, ECO:0000269|PubMed:1663113, ECO:0000269|PubMed:22988102}. | |||
| b3639 | b3639 | Coenzyme A biosynthesis bifunctional protein CoaBC (DNA/pantothenate metabolism flavoprotein) [Includes: Phosphopantothenoylcysteine decarboxylase (PPCDC) (EC 4.1.1.36) (CoaC); Phosphopantothenate--cysteine ligase (EC 6.3.2.5) (CoaB) (PPC synthetase) (PPCS) (Phosphopantothenoylcysteine synthase) | Cytoplasm | R_PPCDC_enzyme R_PPNCL2_enzyme |
R_PPCDC R_PPNCL2 |
406 | Translation: 406.0, Folding: 40.6 | 43,438 | UniprotID: P0ABQ0 ECnumber: EC 4.1.1.36; 6.3.2.5 |
FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4-phosphopantothenate to form 4-phosphopantothenoylcysteine (PubMed:11278255). In the second the latter compound is decarboxylated to form 4-phosphopantotheine (PubMed:10922366). {ECO:0000269|PubMed:10922366, ECO:0000269|PubMed:11278255}. | |
| b1394 | b1394 | 1,2-epoxyphenylacetyl-CoA isomerase (EC 5.3.3.18) | Cytoplasm | R_OXDHCOAT_enzyme R_REPHACCOAI_enzyme |
R_OXDHCOAT R_REPHACCOAI |
262 | Translation: 262.0, Folding: 26.2 | 28,405 | UniprotID: P77467 ECnumber: EC 5.3.3.18 |
FUNCTION: Catalyzes the reversible conversion of the epoxide to 2-oxepin-2(3H)-ylideneacetyl-CoA (oxepin-CoA). {ECO:0000269|PubMed:12846838, ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:9748275}. | |
| b1395 | b1395 | 3-hydroxyadipyl-CoA dehydrogenase (EC 1.1.1.-) | Cytoplasm | R_HADPCOADH3_enzyme | R_HADPCOADH3 | 475 | Translation: 475.0, Folding: 47.5 | 51,733 | UniprotID: P76083 ECnumber: EC 1.1.1.- |
FUNCTION: Catalyzes the oxidation of 3-hydroxyadipyl-CoA to yield 3-oxoadipyl-CoA. {ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:9748275}. | |
| b1397 | b1397 | 3-oxoadipyl-CoA/3-oxo-5,6-dehydrosuberyl-CoA thiolase (EC 2.3.1.174) (EC 2.3.1.223) | Cytoplasm | R_3OXCOAT_enzyme R_OXDHCOAT_enzyme |
R_3OXCOAT R_OXDHCOAT |
401 | Translation: 401.0, Folding: 40.1 | 42,277 | UniprotID: P0C7L2 ECnumber: EC 2.3.1.174; 2.3.1.223 |
FUNCTION: Catalyzes the thiolytic cleavage of the beta-keto C8 intermediate 3-oxo-5,6-dehydrosuberyl-CoA with CoA to yield the C6 intermediate 2,3-dehydroadipyl-CoA and acetyl-CoA. Besides it catalyzes also the last step of the pathway, in which 3-oxoadipyl-CoA similarly is cleaved to acetyl-CoA and succinyl-CoA. {ECO:0000269|PubMed:17259607, ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:9748275}. |
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| b1390 | b1390 | 1,2-phenylacetyl-CoA epoxidase, subunit C (1,2-phenylacetyl-CoA epoxidase, structural subunit beta) (1,2-phenylacetyl-CoA monooxygenase, subunit C) | Cytoplasm | R_PACCOAE_enzyme | R_PACCOAE | 248 | Translation: 248.0, Folding: 24.8 | 27,877 | UniprotID: P76079 | FUNCTION: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit C may be essential for structural integrity of the alpha subunit. {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:9748275}. | |
| b1391 | b1391 | Putative 1,2-phenylacetyl-CoA epoxidase, subunit D (1,2-phenylacetyl-CoA monooxygenase, subunit D) | Cytoplasm | R_PACCOAE_enzyme | R_PACCOAE | 165 | Translation: 165.0, Folding: 16.5 | 18,324 | UniprotID: P76080 | FUNCTION: Possible component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit D may have a function related to the maturation of the monooxygenase complex, rather than direct involvement in catalysis. PaaD could assist either in maturation of PaaE or PaaA. {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:9748275}. |
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| b1392 | b1392 | 1,2-phenylacetyl-CoA epoxidase, subunit E (EC 1.-.-.-) (1,2-phenylacetyl-CoA epoxidase, reductase subunit) (1,2-phenylacetyl-CoA monooxygenase, subunit E) | Cytoplasm | R_PACCOAE_enzyme | R_PACCOAE | 356 | Translation: 356.0, Folding: 35.6 | 39,320 | UniprotID: P76081 ECnumber: EC 1.-.-.- |
FUNCTION: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit E is a reductase with a preference for NADPH and FAD, capable of reducing cytochrome c. {ECO:0000269|PubMed:16997993, ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:21247899, ECO:0000269|PubMed:9748275}. | |
| b1393 | b1393 | 2,3-dehydroadipyl-CoA hydratase (EC 4.2.1.17) (Enoyl-CoA hydratase) | Cytoplasm | R_DHACOAH_enzyme | R_DHACOAH | 255 | Translation: 255.0, Folding: 25.5 | 27,237 | UniprotID: P76082 ECnumber: EC 4.2.1.17 |
FUNCTION: Catalyzes the reversible conversion of enzymatically produced 2,3-dehydroadipyl-CoA into 3-hydroxyadipyl-CoA. {ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:9748275}. | |
| b1398 | b1398 | Phenylacetate-coenzyme A ligase (EC 6.2.1.30) (Phenylacetyl-CoA ligase) (PA-CoA ligase) | Cytoplasm | R_PACCOAL_enzyme | R_PACCOAL | 437 | Translation: 437.0, Folding: 43.7 | 48,953 | UniprotID: P76085 ECnumber: EC 6.2.1.30 |
FUNCTION: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). {ECO:0000269|PubMed:20660314, ECO:0000269|PubMed:9748275}. | |
| b1621 | b1621 | PTS system maltose-specific EIICB component [Includes: Maltose permease IIC component (PTS system maltose-specific EIIC component); Maltose-specific phosphotransferase enzyme IIB component (EC 2.7.1.208) (PTS system maltose-specific EIIB component) | Cell_inner_membrane | R_GLCptspp_duplicate_2_enzyme R_MALTptspp_enzyme |
R_GLCptspp_duplicate_2 R_MALTptspp |
530 | Secretion: 530.0, Translation: 530.0, Folding: 53.0 | 56,627 | UniprotID: P19642 ECnumber: EC 2.7.1.208 |
FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. This system is involved in maltose transport. MalX can also recognize and transport glucose even though this sugar may not represent the natural substrate of the system. {ECO:0000269|PubMed:1856179}. |
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| b1622 | b1622 | Protein MalY [Includes: Cystathionine beta-lyase MalY (CBL) (EC 4.4.1.8) (Beta-cystathionase) (Cysteine lyase); Maltose regulon modulator | Cytoplasm | R_CYSTL_enzyme | R_CYSTL | 390 | Translation: 390.0, Folding: 39.0 | 43,642 | UniprotID: P23256 ECnumber: EC 4.4.1.8 |
FUNCTION: Acts as a beta-cystathionase and as a repressor of the maltose regulon. | |
| b1623 | b1623 | Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase) | Cytoplasm | R_ADA_enzyme R_DADA_enzyme |
R_ADA R_DADA |
333 | Translation: 333.0, Folding: 33.3 | 36,397 | UniprotID: P22333 ECnumber: EC 3.5.4.4 |
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| b0864 | b0864 | Arginine transport ATP-binding protein ArtP (EC 3.6.3.-) | Cell_inner_membrane | R_ARGabcpp_duplicate_2_enzyme | R_ARGabcpp_duplicate_2 | 242 | Secretion: 242.0, Translation: 242.0, Folding: 24.2 | 27,022 | UniprotID: P0AAF6 ECnumber: EC 3.6.3.- |
FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Probably responsible for energy coupling to the transport system. {ECO:0000269|PubMed:8801422}. | |
| b0861 | b0861 | Arginine ABC transporter permease protein ArtM | Cell_inner_membrane | R_ARGabcpp_duplicate_2_enzyme | R_ARGabcpp_duplicate_2 | 222 | Secretion: 222.0, Translation: 222.0, Folding: 22.2 | 24,914 | UniprotID: P0AE30 | FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:8801422}. | |
| b0860 | b0860 | ABC transporter arginine-binding protein 1 | Periplasm | R_ARGabcpp_duplicate_2_enzyme | R_ARGabcpp_duplicate_2 | 243 | Secretion: 243.0, Translation: 243.0, Folding: 24.3 | 26,829 | UniprotID: P30860 | FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Binds L-arginine with high affinity. {ECO:0000269|PubMed:8801422}. | |
| b0863 | b0863 | Putative ABC transporter arginine-binding protein 2 | Periplasm | R_ARGabcpp_duplicate_2_enzyme | R_ARGabcpp_duplicate_2 | 243 | Secretion: 243.0, Translation: 243.0, Folding: 24.3 | 26,930 | UniprotID: P30859 | FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. {ECO:0000269|PubMed:8801422}. | |
| b0862 | b0862 | Arginine ABC transporter permease protein ArtQ | Cell_inner_membrane | R_ARGabcpp_duplicate_2_enzyme | R_ARGabcpp_duplicate_2 | 238 | Secretion: 238.0, Translation: 238.0, Folding: 23.8 | 26,217 | UniprotID: P0AE34 | FUNCTION: Part of the ABC transporter complex ArtPIQMJ involved in arginine transport. Probably responsible for the translocation of the substrate across the membrane. {ECO:0000269|PubMed:8801422}. | |
| b4290 | b4290 | Fe(3+) dicitrate-binding periplasmic protein (Iron(III) dicitrate-binding periplasmic protein) | Periplasm | R_FE3DCITabcpp_enzyme | R_FE3DCITabcpp | 300 | Secretion: 300.0, Translation: 300.0, Folding: 30.0 | 33,146 | UniprotID: P15028 | FUNCTION: Binds citrate-dependent Fe(3+); part of the binding-protein-dependent transport system for uptake of citrate-dependent Fe(3+). | |
| b4291 | b4291 | Fe(3+) dicitrate transport protein FecA (Iron(III) dicitrate transport protein FecA) | Cell_outer_membrane | R_FE3DCITtonex_enzyme | R_FE3DCITtonex | 774 | Secretion: 774.0, Translation: 774.0, Folding: 77.4 | 85,322 | UniprotID: P13036 | FUNCTION: FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system. | |
| b4036 | b4036 | Maltoporin (Lambda receptor protein) (Maltose-inducible porin) | Cell_outer_membrane | 446 | Secretion: 446.0, Translation: 446.0, Folding: 44.6 | 49,912 | UniprotID: P02943 | FUNCTION: Involved in the transport of maltose and maltodextrins, indispensable for translocation of dextrins containing more than three glucosyl moieties. A hydrophobic path ('greasy slide') of aromatic residues serves to guide and select the sugars for transport through the channel. Also acts as a receptor for several bacteriophages including lambda. | |||
| b4034 | b4034 | Maltose-binding periplasmic protein (MBP) (MMBP) (Maltodextrin-binding protein) | Periplasm | R_14GLUCANabcpp R_MALTHXabcpp R_MALTPTabcpp R_MALTTRabcpp R_MALTTTRabcpp R_MALTabcpp |
396 | Secretion: 396.0, Translation: 396.0, Folding: 39.6 | 43,388 | UniprotID: P0AEX9 | FUNCTION: Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides. | ||
| b0040 | b0040 | L-carnitine/gamma-butyrobetaine antiporter | Cell_inner_membrane | R_CRNt7pp_enzyme R_CRNt8pp_enzyme |
R_CRNt7pp R_CRNt8pp |
504 | Secretion: 504.0, Translation: 504.0, Folding: 50.4 | 56,587 | UniprotID: P31553 | FUNCTION: Catalyzes the exchange of L-carnitine for gamma-butyrobetaine and related betaines. | |
| b0047 | b0047 | Glutathione-regulated potassium-efflux system protein KefC (K(+)/H(+) antiporter) | Cell_inner_membrane | R_Kt3pp_duplicate_4_enzyme | R_Kt3pp_duplicate_4 | 620 | Secretion: 620.0, Translation: 620.0, Folding: 62.0 | 67,796 | UniprotID: P03819 | FUNCTION: Pore-forming subunit of a potassium efflux system that confers protection against electrophiles. Catalyzes K(+)/H(+) antiport. Can also export rubidium, lithium and sodium. {ECO:0000255|HAMAP-Rule:MF_01413, ECO:0000269|PubMed:17679694, ECO:0000269|PubMed:21041667, ECO:0000269|PubMed:9023177}. | |
| b4033 | b4033 | Maltose transport system permease protein MalF | Cell_inner_membrane | R_14GLUCANabcpp R_MALTHXabcpp R_MALTPTabcpp R_MALTTRabcpp R_MALTTTRabcpp R_MALTabcpp |
514 | Secretion: 514.0, Translation: 514.0, Folding: 51.4 | 57,013 | UniprotID: P02916 | FUNCTION: Part of the binding-protein-dependent transport system for maltose; probably responsible for the translocation of the substrate across the membrane. | ||
| b4031 | b4031 | D-xylose-proton symporter (D-xylose transporter) | Cell_inner_membrane | R_XYLt2pp_enzyme | R_XYLt2pp | 491 | Secretion: 491.0, Translation: 491.0, Folding: 49.1 | 53,608 | UniprotID: P0AGF4 | FUNCTION: Uptake of D-xylose across the boundary membrane with the concomitant transport of protons into the cell (symport system). Glucose is not transported, but can compete for xylose binding sites and can inhibit xylose transport (in vitro). {ECO:0000269|PubMed:23075985}. | |
| b0049 | b0049 | Bis(5-nucleosyl)-tetraphosphatase [symmetrical] (EC 3.6.1.41) (Ap4A hydrolase) (Diadenosine 5,5-P1,P4-tetraphosphate pyrophosphohydrolase) (Diadenosine tetraphosphatase) | Cytoplasm | R_AP4AH_enzyme R_AP5AH_enzyme R_GP4GH_enzyme |
R_AP4AH R_AP5AH R_GP4GH |
280 | Translation: 280.0, Folding: 28.0 | 31,297 | UniprotID: P05637 ECnumber: EC 3.6.1.41 |
FUNCTION: Hydrolyzes diadenosine 5,5-P1,P4-tetraphosphate to yield ADP. {ECO:0000269|PubMed:6317672}. | |
| b0048 | b0048 | Dihydrofolate reductase (EC 1.5.1.3) | Cytoplasm | R_DHFR_duplicate_2_enzyme | R_DHFR_duplicate_2 | 159 | Translation: 159.0, Folding: 15.9 | 17,999 | UniprotID: P0ABQ4 ECnumber: EC 1.5.1.3 |
FUNCTION: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. | |
| b4039 | b4039 | Chorismate pyruvate-lyase (CL) (CPL) (EC 4.1.3.40) | Cytoplasm | R_CHRPL_enzyme | R_CHRPL | 165 | Translation: 165.0, Folding: 16.5 | 18,777 | UniprotID: P26602 ECnumber: EC 4.1.3.40 |
FUNCTION: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway. {ECO:0000269|PubMed:11825618, ECO:0000269|PubMed:16343413, ECO:0000269|PubMed:1644758, ECO:0000269|PubMed:8012607}. | |
| b0915 | b0915 | Tetraacyldisaccharide 4-kinase (EC 2.7.1.130) (Lipid A 4-kinase) | Cytoplasm | R_TDSK_enzyme | R_TDSK | 328 | Translation: 328.0, Folding: 32.8 | 35,589 | UniprotID: P27300 ECnumber: EC 2.7.1.130 |
FUNCTION: Transfers the gamma-phosphate of ATP to the 4-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4-bis-phosphate (lipid IVA). {ECO:0000269|PubMed:9268317, ECO:0000269|PubMed:9575203}. | |
| b0914 | b0914 | Lipid A export ATP-binding/permease protein MsbA (EC 3.6.3.-) | Cell_inner_membrane | R_COLIPAabcpp_enzyme R_K2L4Aabcpp_enzyme R_LIPACabcpp_enzyme R_LIPAabcpp_enzyme R_PA120abcpp_enzyme R_PA140abcpp_enzyme R_PA141abcpp_enzyme R_PA160abcpp_enzyme R_PA161abcpp_enzyme R_PA180abcpp_enzyme R_PA181abcpp_enzyme R_PE120abcpp_enzyme R_PE140abcpp_enzyme R_PE141abcpp_enzyme R_PE160abcpp_enzyme R_PE161abcpp_enzyme R_PE180abcpp_enzyme R_PE181abcpp_enzyme R_PG120abcpp_enzyme R_PG140abcpp_enzyme R_PG141abcpp_enzyme R_PG160abcpp_enzyme R_PG161abcpp_enzyme R_PG180abcpp_enzyme R_PG181abcpp_enzyme R_PGP120abcpp_enzyme R_PGP140abcpp_enzyme R_PGP141abcpp_enzyme R_PGP160abcpp_enzyme R_PGP161abcpp_enzyme R_PGP180abcpp_enzyme R_PGP181abcpp_enzyme |
R_COLIPAabcpp R_K2L4Aabcpp R_LIPACabcpp R_LIPAabcpp R_PA120abcpp R_PA140abcpp R_PA141abcpp R_PA160abcpp R_PA161abcpp R_PA180abcpp R_PA181abcpp R_PE120abcpp R_PE140abcpp R_PE141abcpp R_PE160abcpp R_PE161abcpp R_PE180abcpp R_PE181abcpp R_PG120abcpp R_PG140abcpp R_PG141abcpp R_PG160abcpp R_PG161abcpp R_PG180abcpp R_PG181abcpp R_PGP120abcpp R_PGP140abcpp R_PGP141abcpp R_PGP160abcpp R_PGP161abcpp R_PGP180abcpp R_PGP181abcpp |
582 | Secretion: 582.0, Translation: 582.0, Folding: 58.2 | 64,461 | UniprotID: P60752 ECnumber: EC 3.6.3.- |
FUNCTION: Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation. {ECO:0000269|PubMed:12119303, ECO:0000269|PubMed:8809774, ECO:0000269|PubMed:9575204}. | |
| b0444 | b0444 | 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) (7-cyano-7-carbaguanine synthase) (PreQ(0) synthase) (Queuosine biosynthesis protein QueC) | Cytoplasm | R_CCGS_enzyme | R_CCGS | 231 | Translation: 231.0, Folding: 23.1 | 25,514 | UniprotID: P77756 ECnumber: EC 6.3.4.20 |
FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). {ECO:0000250, ECO:0000269|PubMed:16199558}. | |
| b0910 | b0910 | Cytidylate kinase (CK) (EC 2.7.4.25) (Cytidine monophosphate kinase) (CMP kinase) (Protein MssA) (p25) | Cytoplasm | R_CYTK1_enzyme R_CYTK2_enzyme R_UMPK_enzyme |
R_CYTK1 R_CYTK2 R_UMPK |
227 | Translation: 227.0, Folding: 22.7 | 24,746 | UniprotID: P0A6I0 ECnumber: EC 2.7.4.25 |
FUNCTION: ATP, dATP, and GTP are equally effective as phosphate donors. CMP and dCMP are the best phosphate acceptors. {ECO:0000269|PubMed:7836281, ECO:0000269|PubMed:8190075}. | |
| b0918 | b0918 | 3-deoxy-manno-octulosonate cytidylyltransferase (EC 2.7.7.38) (CMP-2-keto-3-deoxyoctulosonic acid synthase) (CKS) (CMP-KDO synthase) | Cytoplasm | R_KDOCT2_enzyme | R_KDOCT2 | 248 | Translation: 248.0, Folding: 24.8 | 27,614 | UniprotID: P04951 ECnumber: EC 2.7.7.38 |
FUNCTION: Activates KDO (a required 8-carbon sugar) for incorporation into bacterial lipopolysaccharide in Gram-negative bacteria. {ECO:0000255|HAMAP-Rule:MF_00057}. | |
| b4485 | b4485 | Uncharacterized ABC transporter ATP-binding protein YtfR | Cytoplasm | R_GALabcpp_duplicate_2_enzyme R_RIBabcpp_duplicate_2_enzyme |
R_GALabcpp_duplicate_2 R_RIBabcpp_duplicate_2 |
500 | Translation: 500.0, Folding: 50.0 | 55,260 | UniprotID: Q6BEX0 | ||
| b3001 | b3001 | L-glyceraldehyde 3-phosphate reductase (GAP reductase) (EC 1.1.1.-) | Cytoplasm | R_ALR2_duplicate_4_enzyme | R_ALR2_duplicate_4 | 346 | Translation: 346.0, Folding: 34.6 | 38,832 | UniprotID: Q46851 ECnumber: EC 1.1.1.- |
FUNCTION: Catalyzes the stereospecific, NADPH-dependent reduction of L-glyceraldehyde 3-phosphate (L-GAP). The physiological role of gpr is the detoxification of L-GAP, which may be formed by non-enzymatic racemization of GAP. Also involved in the stress response as a methylglyoxal reductase which converts the toxic metabolite methylglyoxal to acetol in vitro and in vivo. {ECO:0000269|PubMed:12583903, ECO:0000269|PubMed:16077126, ECO:0000269|PubMed:18620424}. |
|
| b3006 | b3006 | Biopolymer transport protein ExbB | Cell_inner_membrane | 244 | Secretion: 244.0, Translation: 244.0, Folding: 24.4 | 26,287 | UniprotID: P0ABU7 | FUNCTION: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. Protects ExbD from proteolytic degradation and functionally stabilizes TonB. | |||
| b3005 | b3005 | Biopolymer transport protein ExbD | Cell_inner_membrane | 141 | Secretion: 141.0, Translation: 141.0, Folding: 14.1 | 15,527 | UniprotID: P0ABV2 | FUNCTION: Involved in the TonB-dependent energy-dependent transport of various receptor-bound substrates. | |||
| b3008 | b3008 | Cystathionine beta-lyase MetC (CBL) (EC 4.4.1.8) (Beta-cystathionase) (Cysteine lyase) | Cytoplasm | R_CYSDS_duplicate_2_enzyme R_CYSTL_duplicate_2_enzyme |
R_CYSDS_duplicate_2 R_CYSTL_duplicate_2 |
395 | Translation: 395.0, Folding: 39.5 | 43,212 | UniprotID: P06721 ECnumber: EC 4.4.1.8 |
||
| b4231 | b4231 | Inner membrane ABC transporter permease protein YjfF | Cell_inner_membrane | R_GALabcpp_duplicate_2_enzyme R_RIBabcpp_duplicate_2_enzyme |
R_GALabcpp_duplicate_2 R_RIBabcpp_duplicate_2 |
331 | Secretion: 331.0, Translation: 331.0, Folding: 33.1 | 34,978 | UniprotID: P37772 | FUNCTION: Probably part of a binding-protein-dependent transport system. Probably responsible for the translocation of the substrate across the membrane. | |
| b0751 | b0751 | Nicotinamide riboside transporter PnuC | Cell_inner_membrane | R_NMNPtpp_enzyme | R_NMNPtpp | 239 | Secretion: 239.0, Translation: 239.0, Folding: 23.9 | 26,996 | UniprotID: P0AFK2 | FUNCTION: Required for nicotinamide riboside transport across the inner membrane. {ECO:0000269|PubMed:15561822}. | |
| b0750 | b0750 | Quinolinate synthase A (EC 2.5.1.72) | Cytoplasm | R_QULNS_enzyme | R_QULNS | 347 | Translation: 347.0, Folding: 34.7 | 38,241 | UniprotID: P11458 ECnumber: EC 2.5.1.72 |
FUNCTION: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. {ECO:0000269|PubMed:10648170, ECO:0000269|PubMed:15898769, ECO:0000269|PubMed:15967443}. | |
| b3222 | b3222 | N-acetylmannosamine kinase (EC 2.7.1.60) (ManNAc kinase) (N-acetyl-D-mannosamine kinase) | Cytoplasm | R_AMANK_enzyme | R_AMANK | 291 | Translation: 291.0, Folding: 29.1 | 29,644 | UniprotID: P45425 ECnumber: EC 2.7.1.60 |
FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. Has also low level glucokinase activity in vitro. {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:17979299}. | |
| b3223 | b3223 | Putative N-acetylmannosamine-6-phosphate 2-epimerase (EC 5.1.3.9) (ManNAc-6-P epimerase) | Cytoplasm | R_AMANAPEr_enzyme | R_AMANAPEr | 229 | Translation: 229.0, Folding: 22.9 | 24,074 | UniprotID: P0A761 ECnumber: EC 5.1.3.9 |
FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000305}. | |
| b3224 | b3224 | Sialic acid transporter NanT (Sialic acid permease) (Sialic acid/H(+) symporter) | Cell_inner_membrane | R_ACNAMt2pp_enzyme | R_ACNAMt2pp | 496 | Secretion: 496.0, Translation: 496.0, Folding: 49.6 | 53,551 | UniprotID: P41036 | FUNCTION: Catalyzes the proton-dependent transport of sialic acid (PubMed:22167185, PubMed:23848303). Can transport the common sialic acid N-acetylneuraminic acid (Neu5Ac) and the related sialic acids N-glycolylneuraminic acid (Neu5Gc) and 3-keto-3-deoxy-D-glycero-D-galactonononic acid (KDN) (PubMed:23848303). Functions as a bidirectional transporter in vitro (PubMed:22167185). {ECO:0000269|PubMed:22167185, ECO:0000269|PubMed:23848303}. |
|
| b3225 | b3225 | N-acetylneuraminate lyase (NAL) (Neu5Ac lyase) (EC 4.1.3.3) (N-acetylneuraminate pyruvate-lyase) (N-acetylneuraminic acid aldolase) (NALase) (Sialate lyase) (Sialic acid aldolase) (Sialic acid lyase) | Cytoplasm | R_ACNML_enzyme | R_ACNML | 297 | Translation: 297.0, Folding: 29.7 | 32,593 | UniprotID: P0A6L4 ECnumber: EC 4.1.3.3 |
FUNCTION: Catalyzes the reversible aldol cleavage of N-acetylneuraminic acid (sialic acid; Neu5Ac) to form pyruvate and N-acetylmannosamine (ManNAc) via a Schiff base intermediate. | |
| b4237 | b4237 | Anaerobic ribonucleoside-triphosphate reductase-activating protein (EC 1.97.1.-) (Class III anaerobic ribonucleotide reductase small component) | Cytoplasm | 154 | Translation: 154.0, Folding: 15.4 | 17,446 | UniprotID: P0A9N8 ECnumber: EC 1.97.1.- |
FUNCTION: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5-deoxy-adenosine. {ECO:0000269|PubMed:1460049, ECO:0000269|PubMed:7852304, ECO:0000269|PubMed:9305874}. | |||
| b3126 | b3126 | 5-keto-4-deoxy-D-glucarate aldolase (KDGluc aldolase) (KDGlucA) (EC 4.1.2.20) (2-dehydro-3-deoxy-D-glucarate aldolase) (2-keto-3-deoxy-D-glucarate aldolase) (5-dehydro-4-deoxy-D-glucarate aldolase) (Alpha-keto-beta-deoxy-D-glucarate aldolase) | Cytoplasm | R_GLCRAL_enzyme | R_GLCRAL | 256 | Translation: 256.0, Folding: 25.6 | 27,384 | UniprotID: P23522 ECnumber: EC 4.1.2.20 |
FUNCTION: Catalyzes the reversible retro-aldol cleavage of both 5-keto-4-deoxy-D-glucarate and 2-keto-3-deoxy-D-glucarate to pyruvate and tartronic semialdehyde. {ECO:0000269|PubMed:9772162, ECO:0000269|Ref.5}. | |
| b3648 | b3648 | Guanylate kinase (EC 2.7.4.8) (GMP kinase) | Cytoplasm | R_DGK1_enzyme R_GK1_enzyme |
R_DGK1 R_GK1 |
207 | Translation: 207.0, Folding: 20.7 | 23,593 | UniprotID: P60546 ECnumber: EC 2.7.4.8 |
FUNCTION: Essential for recycling GMP and indirectly, cGMP. {ECO:0000269|PubMed:8390989}. | |
| b3640 | b3640 | Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) | Cytoplasm | R_DUTPDP_enzyme | R_DUTPDP | 151 | Translation: 151.0, Folding: 15.1 | 16,155 | UniprotID: P06968 ECnumber: EC 3.6.1.23 |
FUNCTION: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA. | |
| b3137 | b3137 | D-tagatose-1,6-bisphosphate aldolase subunit KbaY (TBPA) (TagBP aldolase) (EC 4.1.2.40) (D-tagatose-bisphosphate aldolase class II) (Ketose 1,6-bisphosphate aldolase class II) (Tagatose-bisphosphate aldolase) | Cytoplasm | R_TGBPA_enzyme | R_TGBPA | 286 | Translation: 286.0, Folding: 28.6 | 31,294 | UniprotID: P0AB74 ECnumber: EC 4.1.2.40 |
FUNCTION: Catalytic subunit of the tagatose-1,6-bisphosphate aldolase KbaYZ, which catalyzes the reversible aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to produce tagatose 1,6-bisphosphate (TBP). Requires KbaZ subunit for full activity and stability. {ECO:0000269|PubMed:10712619, ECO:0000269|PubMed:11976750}. | |
| b3642 | b3642 | Orotate phosphoribosyltransferase (OPRT) (OPRTase) (EC 2.4.2.10) | Cytoplasm | R_ORPT_enzyme | R_ORPT | 213 | Translation: 213.0, Folding: 21.3 | 23,567 | UniprotID: P0A7E3 ECnumber: EC 2.4.2.10 |
FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000269|PubMed:8620002}. | |
| b3132 | b3132 | D-tagatose-1,6-bisphosphate aldolase subunit KbaZ | Cytoplasm | R_TGBPA_enzyme | R_TGBPA | 426 | Translation: 426.0, Folding: 42.6 | 47,192 | UniprotID: P0C8K0 | FUNCTION: Component of the tagatose-1,6-bisphosphate aldolase KbaYZ that is required for full activity and stability of the Y subunit. Could have a chaperone-like function for the proper and stable folding of KbaY. When expressed alone, KbaZ does not show any aldolase activity. {ECO:0000269|PubMed:11976750}. | |
| average_protein_Cell_inner_membrane | average_protein_Cell_inner_membrane | Cell_inner_membrane | NaN |
Secretion: 301.0, Translation: 301.0, Folding: 30.1 | NaN |
||||||
| average_protein_Cytoplasm | average_protein_Cytoplasm | Cytoplasm | R_ACALDtpp_enzyme R_ACONIs_enzyme R_AOBUTDs_enzyme R_ARBTNexs_enzyme R_ATPHs_enzyme R_CBMD_enzyme R_CO2tpp_enzyme R_CPGNexs_enzyme R_DATPHs_enzyme R_DHPTDCs2_enzyme R_DMSOtpp_enzyme R_ETOHtrpp_enzyme R_FALDtpp_enzyme R_FALGTHLs_enzyme R_FE3HOXexs_enzyme R_FECRMexs_enzyme R_FEENTERexs_enzyme R_FEOXAMexs_enzyme R_FESD1s_enzyme R_FESD2s_enzyme R_G5SADs_enzyme R_GLYCtpp_duplicate_2_enzyme R_GTPHs_enzyme R_H2Otex_duplicate_4_enzyme R_H2Otpp_enzyme R_H2St1pp_enzyme R_H2tpp_enzyme R_MEOHtrpp_enzyme R_METOX1s_enzyme R_METOX2s_enzyme R_MTHTHFSs_enzyme R_N2Otpp_enzyme R_NH4tpp_duplicate_2_enzyme R_NOVBCNtex_enzyme R_NOtpp_enzyme R_O2tpp_enzyme R_OMCDC_enzyme R_QUINDH_enzyme R_RFAMPtex_enzyme R_SHK3Dr_enzyme R_SO2tpp_enzyme |
R_ACALDtpp R_ACONIs R_AOBUTDs R_ARBTNexs R_ATPHs R_CBMD R_CO2tpp R_CPGNexs R_DATPHs R_DHPTDCs2 R_DMSOtpp R_ETOHtrpp R_FALDtpp R_FALGTHLs R_FE3HOXexs R_FECRMexs R_FEENTERexs R_FEOXAMexs R_FESD1s R_FESD2s R_G5SADs R_GLYCtpp_duplicate_2 R_GTPHs R_H2Otex_duplicate_4 R_H2Otpp R_H2St1pp R_H2tpp R_MEOHtrpp R_METOX1s R_METOX2s R_MTHTHFSs R_N2Otpp R_NH4tpp_duplicate_2 R_NOVBCNtex R_NOtpp R_O2tpp R_OMCDC R_QUINDH R_RFAMPtex R_SHK3Dr R_SO2tpp |
NaN |
Translation: 301.0, Folding: 30.1 | NaN |
||||
| average_protein_Cell_outer_membrane | average_protein_Cell_outer_membrane | Cell_outer_membrane | NaN |
Secretion: 301.0, Translation: 301.0, Folding: 30.1 | NaN |
||||||
| average_protein_Periplasm | average_protein_Periplasm | Periplasm | NaN |
Secretion: 301.0, Translation: 301.0, Folding: 30.1 | NaN |
||||||
| average_protein_Secreted | average_protein_Secreted | Secreted | NaN |
Translation: 301.0, Folding: 30.1 | NaN |
||||||
| b0911 | b0911 | 30S ribosomal protein S1 (Bacteriophage Q beta RNA-directed RNA polymerase subunit I) (Small ribosomal subunit protein bS1) | Cytoplasm | Translation | 557 | Translation: 557.0, Folding: 55.7 | 61,158 | UniprotID: P0AG67 | FUNCTION: Required for translation of most natural mRNAs except for leaderless mRNA (PubMed:9677288, PubMed:7003157, PubMed:12068815, PubMed:17376482, PubMed:24339747). Binds mRNA upstream of the Shine-Dalgarno (SD) sequence and helps it bind to the 30S ribosomal subunit; acts as an RNA chaperone to unfold structured mRNA on the ribosome but is not essential for mRNAs with strong SDs and little 5-UTR structure, thus it may help fine-tune which mRNAs that are translated (PubMed:24339747). Unwinds dsRNA by binding to transiently formed ssRNA regions; binds about 10 nucleotides (PubMed:22908248). Has a preference for polypyrimidine tracts (PubMed:778845). Negatively autoregulates its own translation (PubMed:2120211). {ECO:0000269|PubMed:12068815, ECO:0000269|PubMed:15340139, ECO:0000269|PubMed:1712292, ECO:0000269|PubMed:17376482, ECO:0000269|PubMed:2120211, ECO:0000269|PubMed:22908248, ECO:0000269|PubMed:24339747, ECO:0000269|PubMed:7003157, ECO:0000269|PubMed:778845, ECO:0000269|PubMed:9677288}.; FUNCTION: It is not clear if it plays a role in trans-translation (a process which rescues stalled ribosomes). Evidence for its role; binds to tmRNA with very high affinity, is required for binding of tmRNA to 30S subunit (PubMed:11101533, PubMed:15340139). Thought to play a role only in translation of the tmRNA in vitro (PubMed:17392345). Evidence against its role; overexpression of whole protein or various S1 fragments inhibits translation, they have no effect on trans-translation, and an in vitro system with S1-less ribosomes performs trans-translation (PubMed:15340139, PubMed:17376482). In trans-translation Ala-aminoacylated transfer-messenger RNA (tmRNA, product of the ssrA gene; the 2 termini fold to resemble tRNA(Ala) while it encodes a short internal open reading frame (the tag peptide)) acts like a tRNA, entering the A-site of the ribosome and displacing the stalled mRNA (which is subsequently degraded). The ribosome then switches to translate the ORF on the tmRNA, the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and thus targeted for degradation. {ECO:0000269|PubMed:11101533, ECO:0000269|PubMed:15340139, ECO:0000269|PubMed:17376482, ECO:0000269|PubMed:17392345}.; FUNCTION: In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex; this subunit is required for RNA replication initiation activity during synthesis of (-) strand RNA from the (+) strand genomic RNA but not for (+) strand synthesis from the (-) strand (PubMed:6358207, PubMed:25122749). Binds an approximately 70 mucleotide RNA internal to the viral replicase gene (the M-site) (PubMed:25122749). Others have reported it is not involved in RNA replication initiation but rather in termination of RNA synthesis and is required for termination whether it is the (+) or (-) strand that is being synthesized (PubMed:23653193). {ECO:0000269|PubMed:23653193, ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:6358207, ECO:0000269|PubMed:816798}.; FUNCTION: In case of infection by bacteriophage T4, plays a significant role in substrate choice by viral endoribonuclease RegB. {ECO:0000269|PubMed:17130171}. |
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| b0169 | b0169 | 30S ribosomal protein S2 (Small ribosomal subunit protein uS2) | Cytoplasm | Translation | 241 | Translation: 241.0, Folding: 24.1 | 26,744 | UniprotID: P0A7V0 | FUNCTION: Required for ribosomal protein S1 to bind to the 30S subunit. {ECO:0000269|PubMed:12068815}. | ||
| b3314 | b3314 | 30S ribosomal protein S3 (Small ribosomal subunit protein uS3) | Cytoplasm | Translation | 233 | Translation: 233.0, Folding: 23.3 | 25,983 | UniprotID: P0A7V3 | FUNCTION: Binds the lower part of the 30S subunit head. Binds mRNA in the 70S ribosome, positioning it for translation (By similarity). {ECO:0000250}.; FUNCTION: Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. {ECO:0000269|PubMed:15652481}. | ||
| b3296 | b3296 | 30S ribosomal protein S4 (Small ribosomal subunit protein uS4) | Cytoplasm | Translation | 206 | Translation: 206.0, Folding: 20.6 | 23,469 | UniprotID: P0A7V8 | FUNCTION: One of two assembly initiator proteins for the 30S subunit, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit. {ECO:0000269|PubMed:2461734}.; FUNCTION: With S5 and S12 plays an important role in translational accuracy; many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations).; FUNCTION: Plays a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. {ECO:0000269|PubMed:15652481}.; FUNCTION: Protein S4 is also a translational repressor protein, it controls the translation of the alpha-operon (which codes for S13, S11, S4, RNA polymerase alpha subunit, and L17) by binding to its mRNA. {ECO:0000269|PubMed:3309351}.; FUNCTION: Also functions as a rho-dependent antiterminator of rRNA transcription, increasing the synthesis of rRNA under conditions of excess protein, allowing a more rapid return to homeostasis. Binds directly to RNA polymerase. {ECO:0000269|PubMed:11447122}. |
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| b3303 | b3303 | 30S ribosomal protein S5 (Small ribosomal subunit protein uS5) | Cytoplasm | Translation | 167 | Translation: 167.0, Folding: 16.7 | 17,603 | UniprotID: P0A7W1 | FUNCTION: With S4 and S12 plays an important role in translational accuracy. Many suppressors of streptomycin-dependent mutants of protein S12 are found in this protein, some but not all of which decrease translational accuracy (ram, ribosomal ambiguity mutations). {ECO:0000269|PubMed:15652481}.; FUNCTION: Located at the back of the 30S subunit body where it stabilizes the conformation of the head with respect to the body. {ECO:0000269|PubMed:15652481}.; FUNCTION: The physical location of this protein suggests it may also play a role in mRNA unwinding by the ribosome, possibly by forming part of a processivity clamp. {ECO:0000269|PubMed:15652481}. |
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| b4200 | b4200 | 30S ribosomal protein S6 (Small ribosomal subunit protein bS6) [Cleaved into: 30S ribosomal protein S6 fully modified isoform; 30S ribosomal protein S6 non-modified isoform | Cytoplasm | Translation | 135 | Translation: 135.0, Folding: 13.5 | 15,703 | ||||
| b3341 | b3341 | 30S ribosomal protein S7 (Small ribosomal subunit protein uS7) | Cytoplasm | Translation | 179 | Translation: 179.0, Folding: 17.9 | 20,019 | UniprotID: P02359 | FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the head domain of the 30S subunit (PubMed:2461734). Is located at the subunit interface close to the decoding center, where it has been shown to contact mRNA (PubMed:10606263). Has been shown to contact tRNA in both the P and E sites; it probably blocks exit of the E site tRNA (PubMed:8524654). {ECO:0000269|PubMed:10606263, ECO:0000269|PubMed:2461734, ECO:0000269|PubMed:8524654}.; FUNCTION: Protein S7 is also a translational repressor protein; it regulates the expression of the str operon members to different degrees by binding to its mRNA. {ECO:0000269|PubMed:7507167}. |
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| b3306 | b3306 | 30S ribosomal protein S8 (Small ribosomal subunit protein uS8) | Cytoplasm | Translation | 130 | Translation: 130.0, Folding: 13.0 | 14,127 | UniprotID: P0A7W7 | FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit. {ECO:0000250}.; FUNCTION: Protein S8 is a translational repressor protein, it controls the translation of the spc operon by binding to its mRNA. {ECO:0000269|PubMed:6262737}. | ||
| b3230 | b3230 | 30S ribosomal protein S9 (Small ribosomal subunit protein uS9) | Cytoplasm | Translation | 130 | Translation: 130.0, Folding: 13.0 | 14,856 | UniprotID: P0A7X3 | FUNCTION: The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. Mutations that decrease this affinity are suppressed in the 70S ribosome. {ECO:0000269|PubMed:15308780}. | ||
| b3321 | b3321 | 30S ribosomal protein S10 (Small ribosomal subunit protein uS10) | Cytoplasm | Translation | 103 | Translation: 103.0, Folding: 10.3 | 11,736 | UniprotID: P0A7R5 | FUNCTION: Involved in the binding of tRNA to the ribosomes (PubMed:6759118). In addition, in complex with NusB, is involved in the regulation of ribosomal RNA (rRNA) biosynthesis by transcriptional antitermination. S10 binds RNA non-specifically and increases the affinity of NusB for the boxA RNA sequence (PubMed:7678781, PubMed:11884128, PubMed:16109710). S10 may constitute the critical antitermination component of the NusB-S10 complex (PubMed:19111659). {ECO:0000269|PubMed:11884128, ECO:0000269|PubMed:16109710, ECO:0000269|PubMed:19111659, ECO:0000269|PubMed:6759118, ECO:0000269|PubMed:7678781}. |
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| b3297 | b3297 | 30S ribosomal protein S11 (Small ribosomal subunit protein uS11) | Cytoplasm | Translation | 129 | Translation: 129.0, Folding: 12.9 | 13,845 | UniprotID: P0A7R9 | FUNCTION: Located on the platform of the 30S subunit, it bridges several disparate RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome (By similarity). {ECO:0000250}. | ||
| b3342 | b3342 | 30S ribosomal protein S12 (Small ribosomal subunit protein uS12) | Cytoplasm | Translation | 124 | Translation: 124.0, Folding: 12.4 | 13,737 | UniprotID: P0A7S3 | FUNCTION: With S4 and S5 plays an important role in translational accuracy.; FUNCTION: Interacts with and stabilizes bases of the 16S rRNA that are involved in tRNA selection in the A site and with the mRNA backbone. Located at the interface of the 30S and 50S subunits, it traverses the body of the 30S subunit contacting proteins on the other side and probably holding the rRNA structure together. The combined cluster of proteins S8, S12 and S17 appears to hold together the shoulder and platform of the 30S subunit (By similarity). {ECO:0000250|UniProtKB:Q5SHN3, ECO:0000269|PubMed:7556101}.; FUNCTION: Cryo-EM studies suggest that S12 contacts the EF-Tu bound tRNA in the A-site during codon-recognition. This contact is most likely broken as the aminoacyl-tRNA moves into the peptidyl transferase center in the 50S subunit. {ECO:0000305|PubMed:12093756}. |
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| b3298 | b3298 | 30S ribosomal protein S13 (Small ribosomal subunit protein uS13) | Cytoplasm | Translation | 118 | Translation: 118.0, Folding: 11.8 | 13,099 | UniprotID: P0A7S9 | FUNCTION: Located at the top of the head of the 30S subunit, it contacts several helices of the 16S rRNA. {ECO:0000269|PubMed:15308780}.; FUNCTION: In the E.coli 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact the 23S rRNA (bridge B1a) and protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits; bridge B1a is broken in the model with bound EF-G, while the protein-protein contacts between S13 and L5 in B1b change (PubMed:12809609). The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:16272117), contacting alternately S13 or S19. In the two 3.5 angstroms resolved ribosome structures (PubMed:12859903) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder. {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:12859903, ECO:0000269|PubMed:15308780, ECO:0000269|PubMed:16272117}.; FUNCTION: Contacts the tRNAs in the A and P sites. {ECO:0000269|PubMed:15308780}.; FUNCTION: The C-terminal tail plays a role in the affinity of the 30S P site for different tRNAs. {ECO:0000269|PubMed:15308780}. |
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| b3307 | b3307 | 30S ribosomal protein S14 (Small ribosomal subunit protein uS14) | Cytoplasm | Translation | 101 | Translation: 101.0, Folding: 10.1 | 11,580 | UniprotID: P0AG59 | FUNCTION: Binds 16S rRNA, required for the assembly of 30S particles and may also be responsible for determining the conformation of the 16S rRNA at the A site. | ||
| b3165 | b3165 | 30S ribosomal protein S15 (Small ribosomal subunit protein uS15) | Cytoplasm | Translation | 89 | Translation: 89.0, Folding: 8.9 | 10,269 | UniprotID: P0ADZ4 | FUNCTION: One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it helps nucleate assembly of the platform of the 30S subunit by binding and bridging several RNA helices of the 16S rRNA (PubMed:12809609, PubMed:16272117). Binds to its own mRNA, stabilizing it 5-UTR and preventing its translation (PubMed:24339747). {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:24339747}.; FUNCTION: In the E.coli 70S ribosome it has been modeled (PubMed:12809609) to contact the 23S rRNA of the 50S subunit forming part of bridge B4. In the two 3.5 A resolved ribosome structures (PubMed:16272117) there are minor differences between side-chain conformations. {ECO:0000269|PubMed:12244297, ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117}. |
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| b2609 | b2609 | 30S ribosomal protein S16 (Small ribosomal subunit protein bS16) | Cytoplasm | Translation | 82 | Translation: 82.0, Folding: 8.2 | 9,191 | UniprotID: P0A7T3 | FUNCTION: In addition to being a ribosomal protein, S16 also has a cation-dependent endonuclease activity. {ECO:0000269|PubMed:8730873}.; FUNCTION: In-frame fusions with the ribosome maturation factor rimM suppress mutations in the latter (probably due to increased rimM expression) and are found in translationally active 70S ribosomes. {ECO:0000269|PubMed:11514519}. | ||
| b3311 | b3311 | 30S ribosomal protein S17 (Small ribosomal subunit protein uS17) | Cytoplasm | Translation | 84 | Translation: 84.0, Folding: 8.4 | 9,704 | UniprotID: P0AG63 | FUNCTION: One of the primary rRNA binding proteins, it binds specifically to the 5-end of 16S ribosomal RNA (PubMed:4598121). Also plays a role in translational accuracy; neamine-resistant ribosomes show reduced neamine-induced misreading in vitro (PubMed:765484, PubMed:781296). {ECO:0000269|PubMed:4598121, ECO:0000269|PubMed:765484, ECO:0000269|PubMed:781296}. | ||
| b4202 | b4202 | 30S ribosomal protein S18 (Small ribosomal subunit protein bS18) | Cytoplasm | Translation | 75 | Translation: 75.0, Folding: 7.5 | 8,986 | UniprotID: P0A7T7 | FUNCTION: Binds as a heterodimer with protein S6 to the central domain of the 16S rRNA, where it helps stabilize the platform of the 30S subunit. | ||
| b3316 | b3316 | 30S ribosomal protein S19 (Small ribosomal subunit protein uS19) | Cytoplasm | Translation | 92 | Translation: 92.0, Folding: 9.2 | 10,430 | UniprotID: P0A7U3 | FUNCTION: In the E.coli 70S ribosome in the initiation state (PubMed:12809609) it has been modeled to contact the 23S rRNA of the 50S subunit forming part of bridge B1a; this bridge is broken in the model with bound EF-G. The 23S rRNA contact site in bridge B1a is modeled to differ in different ribosomal states (PubMed:12859903), contacting alternately S13 or S19. In the 3.5 angstroms resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 bridge B1b are different, confirming the dynamic nature of this interaction. Bridge B1a is not visible in the crystallized ribosomes due to 23S rRNA disorder. {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:12859903, ECO:0000269|PubMed:16272117}.; FUNCTION: Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA. Contacts the A site tRNA. |
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| b0023 | b0023 | 30S ribosomal protein S20 (Small ribosomal subunit protein bS20) | Cytoplasm | Translation | 87 | Translation: 87.0, Folding: 8.7 | 9,684 | UniprotID: P0A7U7 | FUNCTION: Binds directly to 16S ribosomal RNA. | ||
| b3065 | b3065 | 30S ribosomal protein S21 (Small ribosomal subunit protein bS21) | Cytoplasm | Translation | 71 | Translation: 71.0, Folding: 7.1 | 8,500 | UniprotID: P68679 | |||
| b1480 | b1480 | Stationary-phase-induced ribosome-associated protein (Protein D) (SRA) (30S ribosomal protein S22) | Cytoplasm | Translation | 45 | Translation: 45.0, Folding: 4.5 | 5,096 | UniprotID: P68191 | FUNCTION: Although this protein associates with the 30S subunit of the ribosome it is not considered to be a bona fide ribosomal protein. {ECO:0000269|PubMed:11292794, ECO:0000269|PubMed:17277072}. | ||
| b3984 | b3984 | 50S ribosomal protein L1 (Large ribosomal subunit protein uL1) | Cytoplasm | Translation | 234 | Translation: 234.0, Folding: 23.4 | 24,730 | UniprotID: P0A7L0 | FUNCTION: One of the primary rRNA binding proteins, it binds very close to the 3-end of the 23S rRNA. Forms part of the L1 stalk. It is often not seen in high-resolution crystal structures, but can be seen in cryo_EM and 3D reconstruction models. These indicate that the distal end of the stalk moves by approximately 20 angstroms (PubMed:12859903, PubMed:16272117). This stalk movement is thought to be coupled to movement of deacylated tRNA into and out of the E site, and thus to participate in tRNA translocation (PubMed:12859903, PubMed:16272117). Contacts the P and E site tRNAs. {ECO:0000269|PubMed:12859903, ECO:0000269|PubMed:16272117}.; FUNCTION: Protein L1 is also a translational repressor protein, it controls the translation of the L11 operon by binding to its mRNA. |
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| b3317 | b3317 | 50S ribosomal protein L2 (Large ribosomal subunit protein uL2) | Cytoplasm | Translation | 273 | Translation: 273.0, Folding: 27.3 | 29,860 | UniprotID: P60422 | FUNCTION: One of the primary rRNA binding proteins (PubMed:3298242). Located near the base of the L1 stalk, it is probably also mobile. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation (PubMed:8722025). It has been suggested to have peptidyltransferase activity; this is highly controversial. {ECO:0000269|PubMed:10756104, ECO:0000269|PubMed:11013226, ECO:0000269|PubMed:11114255, ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:8722025}.; FUNCTION: In the E.coli 70S ribosome in the initiation state it has been modeled to make several contacts with the 16S rRNA (forming bridge B7b, PubMed:12809609); these contacts are broken in the model with bound EF-G. {ECO:0000269|PubMed:12809609}. |
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| b3320 | b3320 | 50S ribosomal protein L3 (Large ribosomal subunit protein uL3) | Cytoplasm | Translation | 209 | Translation: 209.0, Folding: 20.9 | 22,244 | UniprotID: P60438 | FUNCTION: One of two assembly initiator proteins, it binds directly near the 3-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. {ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:6760192}. | ||
| b3319 | b3319 | 50S ribosomal protein L4 (Large ribosomal subunit protein uL4) | Cytoplasm | Translation | 201 | Translation: 201.0, Folding: 20.1 | 22,087 | UniprotID: P60723 | FUNCTION: One of the primary rRNA binding proteins, this protein initially binds near the 5-end of the 23S rRNA (PubMed:3298242). It is important during the early stages of 50S assembly (PubMed:3298242). It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome (PubMed:7556101, PubMed:6170935). {ECO:0000269|PubMed:13130133, ECO:0000269|PubMed:2442760, ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:6170935, ECO:0000269|PubMed:7556101}.; FUNCTION: Protein L4 is a both a transcriptional repressor and a translational repressor protein; these two functions are independent of each other. It regulates transcription of the S10 operon (to which L4 belongs) by causing premature termination of transcription within the S10 leader; termination absolutely requires the NusA protein. L4 controls the translation of the S10 operon by binding to its mRNA. The regions of L4 that control regulation (residues 131-210) are different from those required for ribosome assembly (residues 89-103). {ECO:0000269|PubMed:13130133, ECO:0000269|PubMed:1692593, ECO:0000269|PubMed:2157208, ECO:0000269|PubMed:2442760}.; FUNCTION: Forms part of the polypeptide exit tunnel. {ECO:0000269|PubMed:11511371, ECO:0000269|PubMed:2442760}.; FUNCTION: Can regulate expression from Citrobacter freundii, Haemophilus influenzae, Morganella morganii, Salmonella typhimurium, Serratia marcescens, Vibrio cholerae and Yersinia enterocolitica (but not Pseudomonas aeruginosa) S10 leaders in vitro. {ECO:0000269|PubMed:10498727}. |
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| b3308 | b3308 | 50S ribosomal protein L5 (Large ribosomal subunit protein uL5) | Cytoplasm | Translation | 179 | Translation: 179.0, Folding: 17.9 | 20,302 | UniprotID: P62399 | FUNCTION: This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. Its 5S rRNA binding is significantly enhanced in the presence of L18. {ECO:0000269|PubMed:354687, ECO:0000269|PubMed:7038683, ECO:0000269|PubMed:8925931}.; FUNCTION: In the 70S ribosome in the initiation state (PubMed:12809609) was modeled to contact protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; the protein-protein contacts between S13 and L5 in B1b change in the model with bound EF-G implicating this bridge in subunit movement (PubMed:12809609 and PubMed:18723842). In the two 3.5 A resolved ribosome structures (PubMed:16272117) the contacts between L5, S13 and S19 are different, confirming the dynamic nature of this interaction. {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:12859903, ECO:0000269|PubMed:16272117}.; FUNCTION: Contacts the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. {ECO:0000269|PubMed:8524654}. |
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| b3305 | b3305 | 50S ribosomal protein L6 (Large ribosomal subunit protein uL6) | Cytoplasm | Translation | 177 | Translation: 177.0, Folding: 17.7 | 18,904 | UniprotID: P0AG55 | FUNCTION: This protein binds directly to at least 2 domains of the 23S ribosomal RNA, thus is important in its secondary structure. It is located near the subunit interface in the base of the L7/L12 stalk, and near the tRNA binding site of the peptidyltransferase center. {ECO:0000269|PubMed:6170935}.; FUNCTION: Gentamicin-resistant mutations in this protein affect translation fidelity. {ECO:0000269|PubMed:369594}. |
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| b3986 | b3986 | 50S ribosomal protein L7/L12 (L8) (Large ribosomal subunit protein bL12) | Cytoplasm | Translation | 121 | Translation: 121.0, Folding: 12.1 | 12,295 | UniprotID: P0A7K2 | FUNCTION: The binding site for several of the GTPase factors involved in protein synthesis (IF-2, EF-Tu, EF-G and RF3). Is thus essential for accurate translation. Deletion of 1 of the L12 dimers from the ribosome (by deleting the binding site on L10) leads to decreased IF-2 association with the 70S ribosome and decreased stimulation of the GTPase activity of EF-G. {ECO:0000269|PubMed:15989950, ECO:0000269|PubMed:22102582}. |
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| b4203 | b4203 | 50S ribosomal protein L9 (Large ribosomal subunit protein bL9) | Cytoplasm | Translation | 149 | Translation: 149.0, Folding: 14.9 | 15,769 | UniprotID: P0A7R1 | FUNCTION: One of the primary rRNA binding proteins, it binds very close to the 3 end of the 23S rRNA. {ECO:0000269|PubMed:3298242}. | ||
| b3985 | b3985 | 50S ribosomal protein L10 (50S ribosomal protein L8) (Large ribosomal subunit protein uL10) | Cytoplasm | Translation | 165 | Translation: 165.0, Folding: 16.5 | 17,712 | UniprotID: P0A7J3 | FUNCTION: Forms part of the ribosomal stalk, playing a central role in the interaction of the ribosome with GTP-bound translation factors. {ECO:0000269|PubMed:15923259}.; FUNCTION: Protein L10 is also a translational repressor protein. It controls the translation of the rplJL-rpoBC operon by binding to its mRNA. {ECO:0000269|PubMed:2448482}. | ||
| b3983 | b3983 | 50S ribosomal protein L11 (Large ribosomal subunit protein uL11) | Cytoplasm | Translation | 142 | Translation: 142.0, Folding: 14.2 | 14,875 | UniprotID: P0A7J7 | FUNCTION: Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. | ||
| b3231 | b3231 | 50S ribosomal protein L13 (Large ribosomal subunit protein uL13) | Cytoplasm | Translation | 142 | Translation: 142.0, Folding: 14.2 | 16,019 | UniprotID: P0AA10 | FUNCTION: This protein is one of the early assembly proteins of the 50S ribosomal subunit, although it is not seen to bind rRNA by itself. It is important during the early stages of 50S assembly. {ECO:0000269|PubMed:3298242}. | ||
| b3310 | b3310 | 50S ribosomal protein L14 (Large ribosomal subunit protein uL14) | Cytoplasm | Translation | 123 | Translation: 123.0, Folding: 12.3 | 13,541 | UniprotID: P0ADY3 | FUNCTION: This protein binds directly to 23S ribosomal RNA. In the E.coli 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit, forming part of bridges B5 and B8, connecting the 2 subunits (PubMed:12809609). Although the protein undergoes significant rotation during the transition from an initiation to and EF-G bound state, the bridges remain stable. In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA in bridges B5 and B8 (PubMed:16272117). {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:22829778}.; FUNCTION: Can also interact with RsfS, in this case bridge B8 probably cannot form, and the 30S and 50S ribosomal subunits do not associate, which represses translation. {ECO:0000269|PubMed:22829778}. |
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| b3301 | b3301 | 50S ribosomal protein L15 (Large ribosomal subunit protein uL15) | Cytoplasm | Translation | 144 | Translation: 144.0, Folding: 14.4 | 14,980 | UniprotID: P02413 | FUNCTION: This protein binds the 5S rRNA. It is required for the late stages of subunit assembly, and is essential for 5S rRNA assembly onto the ribosome. {ECO:0000269|PubMed:3298242}. | ||
| b3313 | b3313 | 50S ribosomal protein L16 (Large ribosomal subunit protein uL16) | Cytoplasm | Translation | 136 | Translation: 136.0, Folding: 13.6 | 15,281 | UniprotID: P0ADY7 | FUNCTION: This protein binds directly to 23S ribosomal RNA and is located at the A site of the peptidyltransferase center. It contacts the A and P site tRNAs (PubMed:8524654). It has an essential role in subunit assembly, which is not well understood (PubMed:3298242). {ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:8524654}. | ||
| b3294 | b3294 | 50S ribosomal protein L17 (Large ribosomal subunit protein bL17) | Cytoplasm | Translation | 127 | Translation: 127.0, Folding: 12.7 | 14,365 | UniprotID: P0AG44 | FUNCTION: Requires L15 for assembly into the 50S subunit. {ECO:0000269|PubMed:3298242}. | ||
| b3304 | b3304 | 50S ribosomal protein L18 (Large ribosomal subunit protein uL18) | Cytoplasm | Translation | 117 | Translation: 117.0, Folding: 11.7 | 12,770 | UniprotID: P0C018 | FUNCTION: This is one of the proteins that mediates the attachment of the 5S rRNA subcomplex onto the large ribosomal subunit where it forms part of the central protuberance. Binds stably to 5S rRNA; increases binding abilities of L5 in a cooperative fashion; both proteins together confer 23S rRNA binding. The 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs. {ECO:0000269|PubMed:109811, ECO:0000269|PubMed:353728, ECO:0000269|PubMed:354687, ECO:0000269|PubMed:6159586, ECO:0000269|PubMed:7038683}. |
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| b2606 | b2606 | 50S ribosomal protein L19 (Large ribosomal subunit protein bL19) | Cytoplasm | Translation | 115 | Translation: 115.0, Folding: 11.5 | 13,133 | UniprotID: P0A7K6 | FUNCTION: This protein is located at the 30S-50S ribosomal subunit interface. In the 70S ribosome it has been modeled to make two contacts with the 16S rRNA of the 30S subunit forming part of bridges B6 and B8 (PubMed:12809609). In the 3.5 A resolved structures L14 and L19 interact and together make contact with the 16S rRNA (PubMed:16272117). The protein conformation is quite different between the 50S and 70S structures, which may be necessary for translocation. {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:16272117}. |
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| b1716 | b1716 | 50S ribosomal protein L20 (Large ribosomal subunit protein bL20) | Cytoplasm | Translation | 118 | Translation: 118.0, Folding: 11.8 | 13,497 | UniprotID: P0A7L3 | FUNCTION: One of the primary rRNA binding proteins, it binds close to the 5-end of the 23S rRNA. It is important during the early stages of 50S assembly. {ECO:0000269|PubMed:3298242}. | ||
| b3186 | b3186 | 50S ribosomal protein L21 (Large ribosomal subunit protein bL21) | Cytoplasm | Translation | 103 | Translation: 103.0, Folding: 10.3 | 11,564 | UniprotID: P0AG48 | FUNCTION: This protein binds to 23S rRNA in the presence of protein L20. {ECO:0000269|PubMed:2665813, ECO:0000269|PubMed:6170935}. | ||
| b3315 | b3315 | 50S ribosomal protein L22 (Large ribosomal subunit protein uL22) | Cytoplasm | Translation | 110 | Translation: 110.0, Folding: 11.0 | 12,226 | UniprotID: P61175 | FUNCTION: This protein binds specifically to 23S rRNA; its binding is stimulated by other ribosomal proteins, e.g. L4, L17, and L20. It is important during the early stages of 50S assembly. It makes multiple contacts with different domains of the 23S rRNA in the assembled 50S subunit and ribosome. {ECO:0000269|PubMed:7766155}.; FUNCTION: The globular domain of the protein is one of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit, while an extended beta-hairpin is found that penetrates into the center of the 70S ribosome where it lines the wall of the exit tunnel. Removal of most of this hairpin (residues 85-95) does not prevent its incorporation into 70S ribosomes. Two of the hairpin residues (91 and 93) seem to be involved in translation elongation arrest of the SecM protein, as their replacement by larger amino acids alleviates the arrest. {ECO:0000269|PubMed:11893334, ECO:0000269|PubMed:13130133}. |
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| b3318 | b3318 | 50S ribosomal protein L23 (Large ribosomal subunit protein uL23) | Cytoplasm | Translation | 100 | Translation: 100.0, Folding: 10.0 | 11,199 | UniprotID: P0ADZ0 | FUNCTION: One of the early assembly proteins, it binds 23S rRNA; is essential for growth. One of the proteins that surround the polypeptide exit tunnel on the outside of the subunit. Acts as the docking site for trigger factor (PubMed:12226666) for Ffh binding to the ribosome (SRP54, PubMed:12756233 and PubMed:12702815) and to nascent polypeptide chains (PubMed:12756233). {ECO:0000269|PubMed:12226666, ECO:0000269|PubMed:12702815, ECO:0000269|PubMed:12756233, ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:6170935}. |
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| b3309 | b3309 | 50S ribosomal protein L24 (Large ribosomal subunit protein uL24) | Cytoplasm | Translation | 104 | Translation: 104.0, Folding: 10.4 | 11,316 | UniprotID: P60624 | FUNCTION: One of two assembly initiator proteins, it binds directly to the 5-end of the 23S rRNA, where it nucleates assembly of the 50S subunit. It is not thought to be involved in the functions of the mature 50S subunit in vitro. {ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:357435, ECO:0000269|PubMed:6760192}.; FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. {ECO:0000269|PubMed:16292303, ECO:0000269|PubMed:357435}. |
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| b2185 | b2185 | 50S ribosomal protein L25 (Large ribosomal subunit protein bL25) | Cytoplasm | Translation | 94 | Translation: 94.0, Folding: 9.4 | 10,693 | UniprotID: P68919 | FUNCTION: This is one of the proteins that binds to the 5S RNA in the ribosome where it forms part of the central protuberance. Binds to the 5S rRNA independently of L5 and L18. Not required for binding of the 5S rRNA/L5/L18 subcomplex to 23S rRNA. {ECO:0000269|PubMed:3298242, ECO:0000269|PubMed:354687, ECO:0000269|PubMed:8925931}. | ||
| b3185 | b3185 | 50S ribosomal protein L27 (Large ribosomal subunit protein bL27) | Cytoplasm | Translation | 85 | Translation: 85.0, Folding: 8.5 | 9,124 | UniprotID: P0A7L8 | |||
| b3637 | b3637 | 50S ribosomal protein L28 (Large ribosomal subunit protein bL28) | Cytoplasm | Translation | 78 | Translation: 78.0, Folding: 7.8 | 9,006 | UniprotID: P0A7M2 | |||
| b3312 | b3312 | 50S ribosomal protein L29 (Large ribosomal subunit protein uL29) | Cytoplasm | Translation | 63 | Translation: 63.0, Folding: 6.3 | 7,273 | UniprotID: P0A7M6 | FUNCTION: Binds 23S rRNA. It is not essential for growth. {ECO:0000269|PubMed:12226666, ECO:0000269|PubMed:6170935}.; FUNCTION: One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (PubMed:12226666). {ECO:0000269|PubMed:12226666}. | ||
| b3302 | b3302 | 50S ribosomal protein L30 (Large ribosomal subunit protein uL30) | Cytoplasm | Translation | 59 | Translation: 59.0, Folding: 5.9 | 6,542 | UniprotID: P0AG51 | |||
| b3936 | b3936 | 50S ribosomal protein L31 (Large ribosomal subunit protein bL31-A) | Cytoplasm | Translation | 70 | Translation: 70.0, Folding: 7.0 | 7,871 | UniprotID: P0A7M9 | FUNCTION: Binds the 23S rRNA. {ECO:0000250}. | ||
| b1089 | b1089 | 50S ribosomal protein L32 (Large ribosomal subunit protein bL32) | Cytoplasm | Translation | 57 | Translation: 57.0, Folding: 5.7 | 6,446 | UniprotID: P0A7N4 | |||
| b3636 | b3636 | 50S ribosomal protein L33 (Large ribosomal subunit protein bL33) | Cytoplasm | Translation | 55 | Translation: 55.0, Folding: 5.5 | 6,372 | UniprotID: P0A7N9 | |||
| b3703 | b3703 | 50S ribosomal protein L34 (Large ribosomal subunit protein bL34) | Cytoplasm | Translation | 46 | Translation: 46.0, Folding: 4.6 | 5,380 | UniprotID: P0A7P5 | |||
| b1717 | b1717 | 50S ribosomal protein L35 (Large ribosomal subunit protein bL35) (Ribosomal protein A) | Cytoplasm | Translation | 65 | Translation: 65.0, Folding: 6.5 | 7,289 | UniprotID: P0A7Q1 | |||
| b3299 | b3299 | 50S ribosomal protein L36 (Large ribosomal subunit protein bL36-A) (Ribosomal protein B) | Cytoplasm | Translation | 38 | Translation: 38.0, Folding: 3.8 | 4,364 | UniprotID: P0A7Q6 | |||
| b0884 | b0884 | Translation initiation factor IF-1 | Cytoplasm | Translation | 72 | Translation: 72.0, Folding: 7.2 | 8,250 | UniprotID: P69222 | FUNCTION: One of the essential components for the initiation of protein synthesis. Binds in the vicinity of the A-site. Stabilizes the binding of IF-2 and IF-3 on the 30S subunit to which N-formylmethionyl-tRNA(fMet) subsequently binds. Helps modulate mRNA selection, yielding the 30S pre-initiation complex (PIC). Upon addition of the 50S ribosomal subunit, IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex. {ECO:0000269|PubMed:22562136, ECO:0000269|PubMed:376343}. |
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| b3168 | b3168 | Translation initiation factor IF-2 | Cytoplasm | Translation | 890 | Translation: 890.0, Folding: 89.0 | 97,350 | UniprotID: P0A705 | FUNCTION: One of the essential components for the initiation of protein synthesis. May protect N-formylmethionyl-tRNA(fMet) from spontaneous hydrolysis. Promotes N-formylmethionyl-tRNA(fMet) binding to the 30S pre-initiation complex (PIC) (PubMed:1764105, PubMed:20224578). Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex. Upon addition of the 50S ribosomal subunit, IF-1, IF-2 and IF-3 are released leaving the mature 70S translation initation complex. {ECO:0000269|PubMed:1764105, ECO:0000269|PubMed:20224578, ECO:0000269|PubMed:22562136, ECO:0000269|PubMed:2444251}. |
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| b1718 | b1718 | Translation initiation factor IF-3 [Cleaved into: Translation initiation factor IF-3 N-terminally processed; Translation initiation factor IF-3S | Cytoplasm | Translation | 180 | Translation: 180.0, Folding: 18.0 | 20,564 | UniprotID: P0A707 | |||
| b0170 | b0170 | Elongation factor Ts (EF-Ts) (Bacteriophage Q beta RNA-directed RNA polymerase subunit IV) | Cytoplasm | Translation | 283 | Translation: 283.0, Folding: 28.3 | 30,423 | UniprotID: P0A6P1 | FUNCTION: Associates with the EF-Tu.GDP complex and induces the exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.; FUNCTION: In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Tu may provide a stabilizing scaffold for the beta (catalytic) subunit, implicated in the elongation step of viral RNA synthesis where it fixes EF-Tu in an open conformation. {ECO:0000269|PubMed:20534494, ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418, ECO:0000269|PubMed:25122749, ECO:0000269|PubMed:816798}. |
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| b3339 | b3339 | Elongation factor Tu 1 (EF-Tu 1) (Bacteriophage Q beta RNA-directed RNA polymerase subunit III) (P-43) | Cytoplasm | Translation | 394 | Translation: 394.0, Folding: 39.4 | 43,284 | UniprotID: P0CE47 | FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.; FUNCTION: May play an important regulatory role in cell growth and in the bacterial response to nutrient deprivation.; FUNCTION: In case of infection by bacteriophage Qbeta, part of the viral RNA-dependent RNA polymerase complex. With EF-Ts may provide a stabilizing scaffold for the beta (catalytic) subunit. Helps separate the double-stranded RNA of the template and growing RNA during elongation. With the beta subunit helps form the exit tunnel for template RNA. {ECO:0000269|PubMed:816798, ECO:0000305}.; FUNCTION: Plays a stimulatory role in trans-translation; binds tmRNA. {ECO:0000269|PubMed:15069072}.; FUNCTION: Protects glycyl-tRNA(Gly) from hydrolysis by E.coli D-aminoacyl-tRNA deacylase (dtd) (By similarity). {ECO:0000250|UniProtKB:Q5SHN6}. |
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| b3340 | b3340 | Elongation factor G (EF-G) | Cytoplasm | Translation | 704 | Translation: 704.0, Folding: 70.4 | 77,581 | UniprotID: P0A6M8 | FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome. |
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| b4147 | b4147 | Elongation factor P (EF-P) | Cytoplasm | Translation | 188 | Translation: 188.0, Folding: 18.8 | 20,591 | UniprotID: P0A6N4 | FUNCTION: Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Beta-lysylation at Lys-34 is required for alleviation. The Pro codons and their context do not affect activity; only consecutive Pro residues (not another amino acid) are affected by EF-P. Has stimulatory effects on peptide bond formation between ribosome-bound initiator tRNA(fMet) and puromycin, and N-acetyl-Phe tRNA(Phe)-primed poly(U)-directed poly(Phe) synthesis. {ECO:0000269|PubMed:23239623, ECO:0000269|PubMed:23239624}. |
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| b1211 | b1211 | Peptide chain release factor RF1 (RF-1) | Cytoplasm | Translation | 360 | Translation: 360.0, Folding: 36.0 | 40,517 | UniprotID: P0A7I0 | FUNCTION: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA. | ||
| b2891 | b2891 | Peptide chain release factor RF2 (RF-2) | Cytoplasm | Translation | 365 | Translation: 365.0, Folding: 36.5 | 41,251 | UniprotID: P07012 | FUNCTION: Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA (PubMed:11118225, PubMed:17932046). Acts as a peptidyl-tRNA hydrolase (PubMed:22857598, PubMed:27934701). In the presence of truncated mRNA in the 70S ribosome, ArfA and RF2 interact such that the GGQ peptide hydrolysis motif of RF2 rises into the peptidyl-transferase center and releases the ribosome (PubMed:27906160, PubMed:27906161, PubMed:27934701, PubMed:28077875). Recruited by ArfA to rescue stalled ribosomes in the absence of a normal stop codon (PubMed:22857598, PubMed:22922063, PubMed:25355516). {ECO:0000269|PubMed:11118225, ECO:0000269|PubMed:17932046, ECO:0000269|PubMed:22857598, ECO:0000269|PubMed:22922063, ECO:0000269|PubMed:25355516, ECO:0000269|PubMed:27906160, ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701, ECO:0000269|PubMed:28077875, ECO:0000305|PubMed:22857598}. |
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| b0436 | b0436 | Trigger factor (TF) (EC 5.2.1.8) (PPIase) | Cytoplasm | Folding | 432 | Translation: 432.0, Folding: 43.2 | 48,193 | UniprotID: P0A850 ECnumber: EC 5.2.1.8 |
FUNCTION: Involved in protein export. Acts as a chaperone by maintaining the newly synthesized secretory and non-secretory proteins in an open conformation. Binds to 3 regions of unfolded substrate PhoA, preferring aromatic and hydrophobic residues, keeping it stretched out and unable to form aggregates (PubMed:24812405). Binds to nascent polypeptide chains via ribosomal protein L23 (PubMed:12226666). Functions as a peptidyl-prolyl cis-trans isomerase in vitro, this activity is dispensible in vivo for chaperone activity. {ECO:0000269|PubMed:12226666, ECO:0000269|PubMed:24812405, ECO:0000269|PubMed:8521806, ECO:0000269|PubMed:8633085}. |
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| b4143 | b4143 | 60 kDa chaperonin (GroEL protein) (Protein Cpn60) | Cytoplasm | Folding | 548 | Translation: 548.0, Folding: 54.8 | 57,329 | UniprotID: P0A6F5 | FUNCTION: Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.; FUNCTION: Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell. | ||
| b4142 | b4142 | 10 kDa chaperonin (GroES protein) (Protein Cpn10) | Cytoplasm | Folding | 97 | Translation: 97.0, Folding: 9.7 | 10,387 | UniprotID: P0A6F9 | FUNCTION: Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter. | ||
| b0014 | b0014 | Chaperone protein DnaK (HSP70) (Heat shock 70 kDa protein) (Heat shock protein 70) | Cytoplasm | Folding | 638 | Translation: 638.0, Folding: 63.8 | 69,115 | UniprotID: P0A6Y8 | FUNCTION: Plays an essential role in the initiation of phage lambda DNA replication, where it acts in an ATP-dependent fashion with the DnaJ protein to release lambda O and P proteins from the preprimosomal complex. DnaK is also involved in chromosomal DNA replication, possibly through an analogous interaction with the DnaA protein. Also participates actively in the response to hyperosmotic shock. |
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| b2614 | b2614 | Protein GrpE (HSP-70 cofactor) (HSP24) (Heat shock protein B25.3) | Cytoplasm | Folding | 197 | Translation: 197.0, Folding: 19.7 | 21,798 | UniprotID: P09372 | FUNCTION: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. {ECO:0000269|PubMed:15102842, ECO:0000269|PubMed:8890154}. |
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| b0015 | b0015 | Chaperone protein DnaJ (HSP40) (Heat shock protein J) | Cytoplasm | Folding | 376 | Translation: 376.0, Folding: 37.6 | 41,100 | UniprotID: P08622 | FUNCTION: Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. {ECO:0000269|PubMed:15044009, ECO:0000269|PubMed:15302880, ECO:0000269|PubMed:15485812, ECO:0000269|PubMed:1826368}. |