Escherichia-coli-CO2-fixing RBAmodel

Proteins

Proteins are localised in cell compartments and can be (or be part of) metabolic enzymes.

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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
Q2RSN9	Q2RSN9		Cytoplasm		R_CA_enzyme	R_CA	NaN		NaN
Q31PL2	Q31PL2		Cytoplasm		R_prkA_enzyme	R_prkA	NaN		NaN
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.
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}.
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}.
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.
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}.
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}.
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		R_NDPK1_duplicate_2_enzyme R_NDPK2_duplicate_2_enzyme R_NDPK3_enzyme R_NDPK4_duplicate_2_enzyme R_NDPK5_duplicate_2_enzyme R_NDPK6_enzyme R_NDPK7_duplicate_2_enzyme R_NDPK8_duplicate_2_enzyme	R_NDPK1_duplicate_2 R_NDPK2_duplicate_2 R_NDPK3 R_NDPK4_duplicate_2 R_NDPK5_duplicate_2 R_NDPK6 R_NDPK7_duplicate_2 R_NDPK8_duplicate_2	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
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.
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}.
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.
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}.
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
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}.
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_enzyme R_CDAPPA140_enzyme R_CDAPPA141_enzyme R_CDAPPA160_enzyme R_CDAPPA161_enzyme R_CDAPPA180_enzyme R_CDAPPA181_enzyme	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
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_enzyme R_COBALT2t3pp_duplicate_2_enzyme R_FE2t3pp_enzyme R_HG2t3pp_enzyme R_MN2t3pp_enzyme R_NI2t3pp_enzyme R_ZN2t3pp_enzyme	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
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		R_3OAS100_duplicate_2_enzyme R_3OAS120_enzyme R_3OAS140_duplicate_2_enzyme R_3OAS160_duplicate_2_enzyme R_3OAS180_enzyme R_3OAS181_enzyme R_3OAS60_enzyme R_3OAS80_duplicate_2_enzyme R_KAS14_duplicate_2_enzyme	R_3OAS100_duplicate_2 R_3OAS120 R_3OAS140_duplicate_2 R_3OAS160_duplicate_2 R_3OAS180 R_3OAS181 R_3OAS60 R_3OAS80_duplicate_2 R_KAS14_duplicate_2	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	R_AACPS1 R_AACPS2 R_AACPS3 R_AACPS4 R_AACPS5 R_AACPS6 R_AACPS7 R_AACPS8 R_AACPS9 R_ACOATA R_ACPPAT120 R_ACPPAT140 R_ACPPAT141 R_ACPPAT160 R_ACPPAT161 R_ACPPAT180 R_ACPPAT181 R_G3PAT120 R_G3PAT140 R_G3PAT141 R_G3PAT160 R_G3PAT161 R_G3PAT180 R_G3PAT181 R_MCOATA R_UAGAAT	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		R_3OAR100_enzyme R_3OAR120_enzyme R_3OAR121_enzyme R_3OAR140_enzyme R_3OAR141_enzyme R_3OAR160_enzyme R_3OAR161_enzyme R_3OAR180_enzyme R_3OAR181_enzyme R_3OAR40_enzyme R_3OAR60_enzyme R_3OAR80_enzyme R_OGMEACPR_enzyme R_OPMEACPR_enzyme	R_3OAR100 R_3OAR120 R_3OAR121 R_3OAR140 R_3OAR141 R_3OAR160 R_3OAR161 R_3OAR180 R_3OAR181 R_3OAR40 R_3OAR60 R_3OAR80 R_OGMEACPR R_OPMEACPR	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
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.
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_enzyme R_ACPPAT140_enzyme R_ACPPAT141_enzyme R_ACPPAT160_enzyme R_ACPPAT161_enzyme R_ACPPAT180_enzyme R_ACPPAT181_enzyme	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}.
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}.
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}.
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
b1654	b1654	Glutaredoxin 4 (Grx4) (Monothiol glutaredoxin)	Cytoplasm		R_GRXR_enzyme R_PAPSR2_enzyme R_RNDR1b_enzyme R_RNDR2b_duplicate_4_enzyme R_RNDR3b_enzyme R_RNDR4b_duplicate_4_enzyme	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
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
b4138	b4138	Anaerobic C4-dicarboxylate transporter DcuA	Cell_inner_membrane		R_ASPt2_3pp_enzyme R_FUMt2_3pp_duplicate_2_enzyme R_MALt2_3pp_duplicate_2_enzyme R_SUCASPtpp_duplicate_2_enzyme R_SUCCt2_3pp_duplicate_2_enzyme R_SUCFUMtpp_duplicate_3_enzyme R_SUCMALtpp_duplicate_2_enzyme	R_ASPt2_3pp R_FUMt2_3pp_duplicate_2 R_MALt2_3pp_duplicate_2 R_SUCASPtpp_duplicate_2 R_SUCCt2_3pp_duplicate_2 R_SUCFUMtpp_duplicate_3 R_SUCMALtpp_duplicate_2	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
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}.
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
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
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_enzyme R_OBTFL_duplicate_2_enzyme R_OBTFL_duplicate_3_enzyme R_PFL_duplicate_2_enzyme R_PFL_duplicate_3_enzyme R_PFL_duplicate_4_enzyme	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
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}.
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	R_CMtpp R_CMtpp_duplicate_2 R_DOXRBCNtpp R_DOXRBCNtpp_duplicate_2 R_FEENTERtex R_FUSAtpp R_FUSAtpp_duplicate_2 R_INDOLEt2pp R_MINCYCtpp R_MINCYCtpp_duplicate_2 R_NOVBCNtpp R_NOVBCNtpp_duplicate_2 R_RFAMPtpp R_RFAMPtpp_duplicate_2 R_TTRCYCtpp R_TTRCYCtpp_duplicate_2	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}.
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}.
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}.
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
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}.
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
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_enzyme R_HDCAtexi_enzyme R_HDCEAtexi_enzyme R_OCDCAtexi_enzyme R_OCDCEAtexi_enzyme R_TTDCAtexi_enzyme R_TTDCEAtexi_enzyme	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		R_ACACT1r_enzyme R_ACACT2r_enzyme R_ACACT3r_enzyme R_ACACT4r_enzyme R_ACACT5r_enzyme R_ACACT6r_enzyme R_ACACT7r_enzyme R_ACACT8r_enzyme	R_ACACT1r R_ACACT2r R_ACACT3r R_ACACT4r R_ACACT5r R_ACACT6r R_ACACT7r R_ACACT8r	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}.
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}.
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}.
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}.
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
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}.
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
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}.
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
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}.
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_enzyme R_PAPSR_duplicate_2_enzyme R_PAPSR2_enzyme R_PAPSR2_duplicate_2_enzyme R_PAPSR2_duplicate_3_enzyme R_PAPSR2_duplicate_4_enzyme	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}.
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
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		R_GRXR_duplicate_4_enzyme R_PAPSR2_duplicate_2_enzyme R_RNDR1b_duplicate_4_enzyme R_RNDR2b_duplicate_2_enzyme R_RNDR3b_duplicate_2_enzyme R_RNDR4b_duplicate_2_enzyme	R_GRXR_duplicate_4 R_PAPSR2_duplicate_2 R_RNDR1b_duplicate_4 R_RNDR2b_duplicate_2 R_RNDR3b_duplicate_2 R_RNDR4b_duplicate_2	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}.
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}.
b4123	b4123	Anaerobic C4-dicarboxylate transporter DcuB	Cell_inner_membrane		R_ASPt2_3pp_duplicate_2_enzyme R_FUMt2_3pp_enzyme R_MALt2_3pp_enzyme R_SUCASPtpp_enzyme R_SUCCt2_3pp_enzyme R_SUCFUMtpp_duplicate_2_enzyme R_SUCMALtpp_enzyme R_SUCTARTtpp_enzyme R_TARTt2_3pp_enzyme	R_ASPt2_3pp_duplicate_2 R_FUMt2_3pp R_MALt2_3pp R_SUCASPtpp R_SUCCt2_3pp R_SUCFUMtpp_duplicate_2 R_SUCMALtpp R_SUCTARTtpp R_TARTt2_3pp	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}.
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}.
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.
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}.
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}.
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}.
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}.
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
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}.
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
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
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}.
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}.
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}.
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}.
b4032	b4032	Maltose transport system permease protein MalG	Cell_inner_membrane		R_14GLUCANabcpp_enzyme R_MALTHXabcpp_enzyme R_MALTPTabcpp_enzyme R_MALTTRabcpp_enzyme R_MALTTTRabcpp_enzyme R_MALTabcpp_enzyme	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}.
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}.
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		R_ACOLIPAabctex_enzyme R_CLIPAabctex_enzyme R_COLIPAPabctex_enzyme R_COLIPAabctex_enzyme R_ECA4COLIPAabctex_enzyme R_ENLIPAabctex_enzyme R_K2L4Aabctex_enzyme R_LIPAabctex_enzyme R_O16A4COLIPAabctex_enzyme	R_ACOLIPAabctex R_CLIPAabctex R_COLIPAPabctex R_COLIPAabctex R_ECA4COLIPAabctex R_ENLIPAabctex R_K2L4Aabctex R_LIPAabctex R_O16A4COLIPAabctex	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}.
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
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}.
b2406	b2406	Xanthosine permease (Xanthosine transporter)	Cell_inner_membrane		R_ADNt2pp_copy2_enzyme R_CYTDt2pp_copy2_enzyme R_INSt2pp_copy2_enzyme R_THMDt2pp_copy2_enzyme R_URIt2pp_copy2_enzyme R_XTSNt2rpp_enzyme	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}.
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
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
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
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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
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
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}.
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}.
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
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}.
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).
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}.
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.
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
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}.
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
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
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
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
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		R_RNDR1_enzyme R_RNDR1_duplicate_2_enzyme R_RNDR2_enzyme R_RNDR2_duplicate_2_enzyme R_RNDR3_enzyme R_RNDR3_duplicate_2_enzyme R_RNDR4_enzyme R_RNDR4_duplicate_2_enzyme	R_RNDR1 R_RNDR1_duplicate_2 R_RNDR2 R_RNDR2_duplicate_2 R_RNDR3 R_RNDR3_duplicate_2 R_RNDR4 R_RNDR4_duplicate_2	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
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
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
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
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}.
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
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.
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	R_ACGAptspp R_ACGAptspp_duplicate_2 R_ACMANAptspp R_ACMUMptspp R_ARBTptspp R_ARBTptspp_duplicate_2 R_ASCBptspp R_CHTBSptspp R_DHAPT R_FRUpts2pp R_FRUptspp R_GALTptspp R_GAMptspp R_GLCptspp R_GLCptspp_duplicate_2 R_GLCptspp_duplicate_3 R_MALTptspp R_MANGLYCptspp R_MANptspp R_MNLptspp R_SBTptspp R_SUCptspp R_TREptspp	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}.
b2417	b2417	PTS system glucose-specific EIIA component (EIIA-Glc) (EIII-Glc) (Glucose-specific phosphotransferase enzyme IIA component) (EC 2.7.1.199)	Cytoplasm		R_ACGAptspp_enzyme R_ACMUMptspp_enzyme R_GLCptspp_enzyme R_GLCptspp_duplicate_2_enzyme R_MALTptspp_enzyme R_SUCptspp_enzyme R_TREptspp_enzyme	R_ACGAptspp R_ACMUMptspp R_GLCptspp R_GLCptspp_duplicate_2 R_MALTptspp R_SUCptspp R_TREptspp	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}.
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}.
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		R_DSBDR_duplicate_2_enzyme R_METSOXR1_duplicate_3_enzyme R_METSOXR1_duplicate_4_enzyme R_METSOXR2_duplicate_2_enzyme R_PAPSR_duplicate_2_enzyme R_RNDR1_duplicate_2_enzyme R_RNDR2_enzyme R_RNDR3_enzyme R_RNDR4_enzyme R_THIORDXi_duplicate_2_enzyme R_TRDR_enzyme	R_DSBDR_duplicate_2 R_METSOXR1_duplicate_3 R_METSOXR1_duplicate_4 R_METSOXR2_duplicate_2 R_PAPSR_duplicate_2 R_RNDR1_duplicate_2 R_RNDR2 R_RNDR3 R_RNDR4 R_THIORDXi_duplicate_2 R_TRDR	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		R_ADNt2pp_copy1_enzyme R_CYTDt2pp_copy1_duplicate_2_enzyme R_DADNt2pp_enzyme R_DCYTt2pp_duplicate_2_enzyme R_DGSNt2pp_enzyme R_DINSt2pp_enzyme R_DURIt2pp_enzyme R_GSNt2pp_enzyme R_INSt2pp_copy1_enzyme R_THMDt2pp_copy1_duplicate_2_enzyme R_URIt2pp_copy1_duplicate_2_enzyme	R_ADNt2pp_copy1 R_CYTDt2pp_copy1_duplicate_2 R_DADNt2pp R_DCYTt2pp_duplicate_2 R_DGSNt2pp R_DINSt2pp R_DURIt2pp R_GSNt2pp R_INSt2pp_copy1 R_THMDt2pp_copy1_duplicate_2 R_URIt2pp_copy1_duplicate_2	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
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}.
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}.
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
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}.
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_enzyme R_MPTG_duplicate_2_enzyme R_MPTG_duplicate_3_enzyme R_MPTG2_enzyme R_MPTG2_duplicate_2_enzyme R_MPTG2_duplicate_3_enzyme	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		R_ASR_enzyme R_GRXR_duplicate_2_enzyme R_PAPSR2_duplicate_3_enzyme R_RNDR1b_duplicate_2_enzyme R_RNDR2b_enzyme R_RNDR3b_duplicate_4_enzyme R_RNDR4b_duplicate_3_enzyme	R_ASR R_GRXR_duplicate_2 R_PAPSR2_duplicate_3 R_RNDR1b_duplicate_2 R_RNDR2b R_RNDR3b_duplicate_4 R_RNDR4b_duplicate_3	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
b2895	b2895	Flavodoxin 2	Cytoplasm		R_FLDR2_duplicate_2_enzyme R_MECDPDH5_enzyme R_POR5_duplicate_2_enzyme R_RNTR1c2_duplicate_3_enzyme R_RNTR1c2_duplicate_4_enzyme R_RNTR2c2_duplicate_3_enzyme R_RNTR2c2_duplicate_4_enzyme R_RNTR3c2_duplicate_3_enzyme R_RNTR3c2_duplicate_4_enzyme R_RNTR4c2_duplicate_3_enzyme R_RNTR4c2_duplicate_4_enzyme	R_FLDR2_duplicate_2 R_MECDPDH5 R_POR5_duplicate_2 R_RNTR1c2_duplicate_3 R_RNTR1c2_duplicate_4 R_RNTR2c2_duplicate_3 R_RNTR2c2_duplicate_4 R_RNTR3c2_duplicate_3 R_RNTR3c2_duplicate_4 R_RNTR4c2_duplicate_3 R_RNTR4c2_duplicate_4	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		R_NTPP1_duplicate_2_enzyme R_NTPP2_duplicate_2_enzyme R_NTPP3_duplicate_2_enzyme R_NTPP4_duplicate_2_enzyme R_NTPP5_enzyme R_NTPP6_enzyme R_NTPP7_enzyme R_NTPP8_enzyme	R_NTPP1_duplicate_2 R_NTPP2_duplicate_2 R_NTPP3_duplicate_2 R_NTPP4_duplicate_2 R_NTPP5 R_NTPP6 R_NTPP7 R_NTPP8	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}.
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}.
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}.
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}.
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}.
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}.
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
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}.
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}.
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		R_NTD10pp_enzyme R_NTD11pp_enzyme R_NTD12pp_enzyme R_NTD1pp_enzyme R_NTD2pp_enzyme R_NTD3pp_enzyme R_NTD4pp_enzyme R_NTD5pp_enzyme R_NTD6pp_enzyme R_NTD7pp_enzyme R_NTD8pp_enzyme R_NTD9pp_enzyme R_UACGALPpp_enzyme R_UACGAMPpp_enzyme R_UDPGALPpp_enzyme R_UDPGPpp_enzyme R_UGLCURPpp_enzyme	R_NTD10pp R_NTD11pp R_NTD12pp R_NTD1pp R_NTD2pp R_NTD3pp R_NTD4pp R_NTD5pp R_NTD6pp R_NTD7pp R_NTD8pp R_NTD9pp R_UACGALPpp R_UACGAMPpp R_UDPGALPpp R_UDPGPpp R_UGLCURPpp	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		R_3HAD100_enzyme R_3HAD120_duplicate_2_enzyme R_3HAD121_duplicate_2_enzyme R_3HAD140_enzyme R_3HAD141_enzyme R_3HAD160_enzyme R_3HAD161_duplicate_2_enzyme R_3HAD180_enzyme R_3HAD181_enzyme R_3HAD40_enzyme R_3HAD60_enzyme R_3HAD80_enzyme R_T2DECAI_enzyme	R_3HAD100 R_3HAD120_duplicate_2 R_3HAD121_duplicate_2 R_3HAD140 R_3HAD141 R_3HAD160 R_3HAD161_duplicate_2 R_3HAD180 R_3HAD181 R_3HAD40 R_3HAD60 R_3HAD80 R_T2DECAI	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}.
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
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}.
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}.
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
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.
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		R_FACOAE100_enzyme R_FACOAE120_enzyme R_FACOAE140_enzyme R_FACOAE141_enzyme R_FACOAE160_enzyme R_FACOAE161_enzyme R_FACOAE180_enzyme R_FACOAE181_enzyme R_FACOAE60_enzyme R_FACOAE80_enzyme	R_FACOAE100 R_FACOAE120 R_FACOAE140 R_FACOAE141 R_FACOAE160 R_FACOAE161 R_FACOAE180 R_FACOAE181 R_FACOAE60 R_FACOAE80	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
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}.
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}.
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
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}.
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}.
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
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}.
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}.
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}.
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
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}.
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}.
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
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}.
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.
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
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
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.
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}.
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
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.-.-.-
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}.
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}.
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}.
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.
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}.
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
b4262	b4262	Lipopolysaccharide export system permease protein LptG	Cell_inner_membrane		R_ACOLIPAabctex_enzyme R_CLIPAabctex_enzyme R_COLIPAPabctex_enzyme R_COLIPAabctex_enzyme R_ECA4COLIPAabctex_enzyme R_ENLIPAabctex_enzyme R_K2L4Aabctex_enzyme R_LIPAabctex_enzyme R_O16A4COLIPAabctex_enzyme	R_ACOLIPAabctex R_CLIPAabctex R_COLIPAPabctex R_COLIPAabctex R_ECA4COLIPAabctex R_ENLIPAabctex R_K2L4Aabctex R_LIPAabctex R_O16A4COLIPAabctex	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		R_ACOLIPAabctex_enzyme R_CLIPAabctex_enzyme R_COLIPAPabctex_enzyme R_COLIPAabctex_enzyme R_ECA4COLIPAabctex_enzyme R_ENLIPAabctex_enzyme R_K2L4Aabctex_enzyme R_LIPAabctex_enzyme R_O16A4COLIPAabctex_enzyme	R_ACOLIPAabctex R_CLIPAabctex R_COLIPAPabctex R_COLIPAabctex R_ECA4COLIPAabctex R_ENLIPAabctex R_K2L4Aabctex R_LIPAabctex R_O16A4COLIPAabctex	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}.
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
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_enzyme R_MDDCP2pp_duplicate_2_enzyme R_MDDCP3pp_duplicate_2_enzyme R_MDDCP4pp_duplicate_2_enzyme R_MDDCP5pp_duplicate_2_enzyme	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	R_ACGAptspp R_ACGAptspp_duplicate_2 R_ACMANAptspp R_ACMUMptspp R_ARBTptspp R_ARBTptspp_duplicate_2 R_ASCBptspp R_DHAPT R_FRUpts2pp R_FRUptspp R_GALTptspp R_GAMptspp R_GLCptspp R_GLCptspp_duplicate_2 R_GLCptspp_duplicate_3 R_MALTptspp R_MANGLYCptspp R_MANptspp R_MNLptspp R_SBTptspp R_SUCptspp R_TREptspp	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.
b4042	b4042	Diacylglycerol kinase (DAGK) (EC 2.7.1.107) (Diglyceride kinase) (DGK)	Cell_inner_membrane		R_DAGK120_enzyme R_DAGK140_enzyme R_DAGK141_enzyme R_DAGK160_enzyme R_DAGK161_enzyme R_DAGK180_enzyme R_DAGK181_enzyme	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_enzyme R_G3PAT140_enzyme R_G3PAT141_enzyme R_G3PAT160_enzyme R_G3PAT161_enzyme R_G3PAT180_enzyme R_G3PAT181_enzyme	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}.
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}.
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
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}.
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
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}.
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}.
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}.
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		R_RNDR1_enzyme R_RNDR1_duplicate_2_enzyme R_RNDR2_enzyme R_RNDR2_duplicate_2_enzyme R_RNDR3_enzyme R_RNDR3_duplicate_2_enzyme R_RNDR4_enzyme R_RNDR4_duplicate_2_enzyme	R_RNDR1 R_RNDR1_duplicate_2 R_RNDR2 R_RNDR2_duplicate_2 R_RNDR3 R_RNDR3_duplicate_2 R_RNDR4 R_RNDR4_duplicate_2	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}.
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}.
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}.
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}.
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	R_G2PPpp R_NTD10pp_duplicate_2 R_NTD11pp_duplicate_2 R_NTD12pp_duplicate_2 R_NTD1pp_duplicate_2 R_NTD2pp_duplicate_2 R_NTD3pp_duplicate_2 R_NTD4pp_duplicate_2 R_NTD5pp_duplicate_2 R_NTD6pp_duplicate_2 R_NTD7pp_duplicate_2 R_NTD8pp_duplicate_2 R_NTD9pp_duplicate_2 R_PSP_Lpp R_PTHRpp R_R5PPpp R_TYRPpp	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
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
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		R_2DGULRGx_enzyme R_2DGULRGy_enzyme R_2DGULRx_enzyme R_2DGULRy_enzyme R_DKGLCNR2x_enzyme R_DKGLCNR2y_enzyme R_GLYCLTDx_enzyme R_GLYCLTDy_duplicate_2_enzyme R_HPYRRx_duplicate_2_enzyme R_HPYRRy_duplicate_2_enzyme	R_2DGULRGx R_2DGULRGy R_2DGULRx R_2DGULRy R_DKGLCNR2x R_DKGLCNR2y R_GLYCLTDx R_GLYCLTDy_duplicate_2 R_HPYRRx_duplicate_2 R_HPYRRy_duplicate_2	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.
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
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
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
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
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
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
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}.
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}.
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}.
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
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}.
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
b0968	b0968	Acylphosphatase (EC 3.6.1.7) (Acylphosphate phosphohydrolase)	Cytoplasm		R_APH120_enzyme R_APH140_enzyme R_APH141_enzyme R_APH160_enzyme R_APH161_enzyme R_APH180_enzyme R_APH181_enzyme	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
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
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		R_MDDCP1pp_duplicate_3_enzyme R_MDDCP2pp_duplicate_3_enzyme R_MDDCP3pp_duplicate_3_enzyme R_MDDCP4pp_duplicate_3_enzyme R_MDDCP5pp_duplicate_3_enzyme R_MDDEP1pp_duplicate_2_enzyme R_MDDEP2pp_duplicate_2_enzyme R_MDDEP3pp_duplicate_2_enzyme R_MDDEP4pp_duplicate_2_enzyme	R_MDDCP1pp_duplicate_3 R_MDDCP2pp_duplicate_3 R_MDDCP3pp_duplicate_3 R_MDDCP4pp_duplicate_3 R_MDDCP5pp_duplicate_3 R_MDDEP1pp_duplicate_2 R_MDDEP2pp_duplicate_2 R_MDDEP3pp_duplicate_2 R_MDDEP4pp_duplicate_2	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		R_3OAS100_enzyme R_3OAS120_duplicate_2_enzyme R_3OAS121_enzyme R_3OAS140_enzyme R_3OAS141_enzyme R_3OAS160_enzyme R_3OAS161_enzyme R_3OAS180_duplicate_2_enzyme R_3OAS60_duplicate_2_enzyme R_3OAS80_enzyme R_KAS14_enzyme R_MACPD_enzyme R_OPMEACPS_enzyme	R_3OAS100 R_3OAS120_duplicate_2 R_3OAS121 R_3OAS140 R_3OAS141 R_3OAS160 R_3OAS161 R_3OAS180_duplicate_2 R_3OAS60_duplicate_2 R_3OAS80 R_KAS14 R_MACPD R_OPMEACPS	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_enzyme R_FUMt2_2pp_enzyme R_MALDt2_2pp_enzyme R_MALt2_2pp_enzyme R_OROTt2_2pp_enzyme R_SUCCt2_2pp_enzyme	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}.
b3451	b3451	sn-glycerol-3-phosphate transport system permease protein UgpE	Cell_inner_membrane		R_G3PCabcpp_enzyme R_G3PEabcpp_enzyme R_G3PGabcpp_enzyme R_G3PIabcpp_enzyme R_G3PSabcpp_enzyme R_GLYC2Pabcpp_enzyme R_GLYC3Pabcpp_enzyme	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_enzyme R_G3PEabcpp_enzyme R_G3PGabcpp_enzyme R_G3PIabcpp_enzyme R_G3PSabcpp_enzyme R_GLYC2Pabcpp_enzyme R_GLYC3Pabcpp_enzyme	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}.
b3453	b3453	sn-glycerol-3-phosphate-binding periplasmic protein UgpB	Periplasm		R_G3PCabcpp_enzyme R_G3PEabcpp_enzyme R_G3PGabcpp_enzyme R_G3PIabcpp_enzyme R_G3PSabcpp_enzyme R_GLYC2Pabcpp_enzyme R_GLYC3Pabcpp_enzyme	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_enzyme R_G3PEabcpp_enzyme R_G3PGabcpp_enzyme R_G3PIabcpp_enzyme R_G3PSabcpp_enzyme R_GLYC2Pabcpp_enzyme R_GLYC3Pabcpp_enzyme	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_enzyme R_ILEabcpp_enzyme R_LEUabcpp_enzyme R_LEUabcpp_duplicate_2_enzyme R_THRabcpp_enzyme R_VALabcpp_enzyme	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_enzyme R_ILEabcpp_enzyme R_LEUabcpp_enzyme R_LEUabcpp_duplicate_2_enzyme R_THRabcpp_enzyme R_VALabcpp_enzyme	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_enzyme R_ILEabcpp_enzyme R_LEUabcpp_enzyme R_LEUabcpp_duplicate_2_enzyme R_THRabcpp_enzyme R_VALabcpp_enzyme	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_enzyme R_ILEabcpp_enzyme R_LEUabcpp_enzyme R_LEUabcpp_duplicate_2_enzyme R_THRabcpp_enzyme R_VALabcpp_enzyme	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
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		R_BMOGDS1_enzyme R_BMOGDS1_duplicate_2_enzyme R_BMOGDS2_enzyme R_BMOGDS2_duplicate_2_enzyme R_BWCOGDS1_enzyme R_BWCOGDS1_duplicate_2_enzyme R_BWCOGDS2_enzyme R_BWCOGDS2_duplicate_2_enzyme R_MOGDS_enzyme R_MOGDS_duplicate_2_enzyme	R_BMOGDS1 R_BMOGDS1_duplicate_2 R_BMOGDS2 R_BMOGDS2_duplicate_2 R_BWCOGDS1 R_BWCOGDS1_duplicate_2 R_BWCOGDS2 R_BWCOGDS2_duplicate_2 R_MOGDS R_MOGDS_duplicate_2	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}.
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_enzyme R_BMOGDS2_duplicate_2_enzyme R_BWCOGDS1_duplicate_2_enzyme R_BWCOGDS2_duplicate_2_enzyme R_MOGDS_duplicate_2_enzyme	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}.
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_enzyme R_PSSA140_enzyme R_PSSA141_enzyme R_PSSA160_enzyme R_PSSA161_enzyme R_PSSA180_enzyme R_PSSA181_enzyme	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
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		R_DSBDR_enzyme R_METSOXR1_enzyme R_METSOXR1_duplicate_2_enzyme R_METSOXR2_enzyme R_PAPSR_enzyme R_RNDR1_enzyme R_RNDR2_duplicate_2_enzyme R_RNDR3_duplicate_2_enzyme R_RNDR4_duplicate_2_enzyme R_THIORDXi_enzyme R_TRDR_duplicate_2_enzyme	R_DSBDR R_METSOXR1 R_METSOXR1_duplicate_2 R_METSOXR2 R_PAPSR R_RNDR1 R_RNDR2_duplicate_2 R_RNDR3_duplicate_2 R_RNDR4_duplicate_2 R_THIORDXi R_TRDR_duplicate_2	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}.
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		R_FACOAL100t2pp_enzyme R_FACOAL120t2pp_duplicate_2_enzyme R_FACOAL140t2pp_duplicate_2_enzyme R_FACOAL141t2pp_duplicate_2_enzyme R_FACOAL160t2pp_duplicate_2_enzyme R_FACOAL161t2pp_enzyme R_FACOAL180t2pp_duplicate_2_enzyme R_FACOAL181t2pp_enzyme R_FACOAL60t2pp_enzyme R_FACOAL80t2pp_enzyme	R_FACOAL100t2pp R_FACOAL120t2pp_duplicate_2 R_FACOAL140t2pp_duplicate_2 R_FACOAL141t2pp_duplicate_2 R_FACOAL160t2pp_duplicate_2 R_FACOAL161t2pp R_FACOAL180t2pp_duplicate_2 R_FACOAL181t2pp R_FACOAL60t2pp R_FACOAL80t2pp	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}.
b4213	b4213	2,3-cyclic-nucleotide 2-phosphodiesterase/3-nucleotidase (EC 3.1.3.6) (EC 3.1.4.16)	Periplasm		R_23PDE2pp_enzyme R_23PDE4pp_enzyme R_23PDE7pp_enzyme R_23PDE9pp_enzyme R_3NTD2pp_enzyme R_3NTD4pp_enzyme R_3NTD7pp_enzyme R_3NTD9pp_enzyme	R_23PDE2pp R_23PDE4pp R_23PDE7pp R_23PDE9pp R_3NTD2pp R_3NTD4pp R_3NTD7pp R_3NTD9pp	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}.
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}.
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
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}.
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
b0684	b0684	Flavodoxin 1	Cytoplasm		R_FLDR2_enzyme R_MECDPDH5_duplicate_2_enzyme R_POR5_enzyme R_RNTR1c2_enzyme R_RNTR1c2_duplicate_2_enzyme R_RNTR2c2_enzyme R_RNTR2c2_duplicate_2_enzyme R_RNTR3c2_enzyme R_RNTR3c2_duplicate_2_enzyme R_RNTR4c2_enzyme R_RNTR4c2_duplicate_2_enzyme	R_FLDR2 R_MECDPDH5_duplicate_2 R_POR5 R_RNTR1c2 R_RNTR1c2_duplicate_2 R_RNTR2c2 R_RNTR2c2_duplicate_2 R_RNTR3c2 R_RNTR3c2_duplicate_2 R_RNTR4c2 R_RNTR4c2_duplicate_2	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
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}.
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.
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_enzyme R_DASYN140_enzyme R_DASYN141_enzyme R_DASYN160_enzyme R_DASYN161_enzyme R_DASYN180_enzyme R_DASYN181_enzyme	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
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
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.
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		R_ACOAD1f_enzyme R_ACOAD2f_enzyme R_ACOAD3f_enzyme R_ACOAD4f_enzyme R_ACOAD5f_enzyme R_ACOAD6f_enzyme R_ACOAD7f_enzyme R_ACOAD8f_enzyme	R_ACOAD1f R_ACOAD2f R_ACOAD3f R_ACOAD4f R_ACOAD5f R_ACOAD6f R_ACOAD7f R_ACOAD8f	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		R_ACOLIPAabctex_enzyme R_CLIPAabctex_enzyme R_COLIPAPabctex_enzyme R_COLIPAabctex_enzyme R_ECA4COLIPAabctex_enzyme R_ENLIPAabctex_enzyme R_K2L4Aabctex_enzyme R_LIPAabctex_enzyme R_O16A4COLIPAabctex_enzyme	R_ACOLIPAabctex R_CLIPAabctex R_COLIPAPabctex R_COLIPAabctex R_ECA4COLIPAabctex R_ENLIPAabctex R_K2L4Aabctex R_LIPAabctex R_O16A4COLIPAabctex	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}.
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
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}.
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.-.-.-
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		R_CTECOAI6_enzyme R_CTECOAI7_enzyme R_CTECOAI8_enzyme R_ECOAH1_enzyme R_ECOAH2_enzyme R_ECOAH3_enzyme R_ECOAH4_enzyme R_ECOAH5_enzyme R_ECOAH6_enzyme R_ECOAH7_enzyme R_ECOAH8_enzyme R_HACD1_enzyme R_HACD2_enzyme R_HACD3_enzyme R_HACD4_enzyme R_HACD5_enzyme R_HACD6_enzyme R_HACD7_enzyme R_HACD8_enzyme	R_CTECOAI6 R_CTECOAI7 R_CTECOAI8 R_ECOAH1 R_ECOAH2 R_ECOAH3 R_ECOAH4 R_ECOAH5 R_ECOAH6 R_ECOAH7 R_ECOAH8 R_HACD1 R_HACD2 R_HACD3 R_HACD4 R_HACD5 R_HACD6 R_HACD7 R_HACD8	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}.
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_enzyme R_FE3Ri_enzyme R_FLVR_enzyme R_FLVRx_enzyme R_FMNRx_duplicate_2_enzyme R_FMNRx2_duplicate_2_enzyme	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		R_ACACT1r_duplicate_3_enzyme R_ACACT2r_duplicate_2_enzyme R_ACACT3r_duplicate_2_enzyme R_ACACT4r_duplicate_2_enzyme R_ACACT5r_duplicate_2_enzyme R_ACACT6r_duplicate_2_enzyme R_ACACT7r_duplicate_2_enzyme R_ACACT8r_duplicate_2_enzyme	R_ACACT1r_duplicate_3 R_ACACT2r_duplicate_2 R_ACACT3r_duplicate_2 R_ACACT4r_duplicate_2 R_ACACT5r_duplicate_2 R_ACACT6r_duplicate_2 R_ACACT7r_duplicate_2 R_ACACT8r_duplicate_2	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
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.
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
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}.
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}.
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}.
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
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}.
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}.
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
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
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
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	R_3HAD100_duplicate_2 R_3HAD120 R_3HAD121 R_3HAD140_duplicate_2 R_3HAD141_duplicate_2 R_3HAD160_duplicate_2 R_3HAD161 R_3HAD180_duplicate_2 R_3HAD181_duplicate_2 R_3HAD40_duplicate_2 R_3HAD60_duplicate_2 R_3HAD80_duplicate_2 R_OGMEACPD R_OPMEACPD	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		R_GRXR_duplicate_3_enzyme R_PAPSR2_duplicate_4_enzyme R_RNDR1b_duplicate_3_enzyme R_RNDR2b_duplicate_3_enzyme R_RNDR3b_duplicate_3_enzyme R_RNDR4b_enzyme	R_GRXR_duplicate_3 R_PAPSR2_duplicate_4 R_RNDR1b_duplicate_3 R_RNDR2b_duplicate_3 R_RNDR3b_duplicate_3 R_RNDR4b	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		R_APG3PAT120_enzyme R_APG3PAT140_enzyme R_APG3PAT141_enzyme R_APG3PAT160_enzyme R_APG3PAT161_enzyme R_APG3PAT180_enzyme R_APG3PAT181_enzyme	R_APG3PAT120 R_APG3PAT140 R_APG3PAT141 R_APG3PAT160 R_APG3PAT161 R_APG3PAT180 R_APG3PAT181	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	R_RNDR1b R_RNDR1b_duplicate_2 R_RNDR1b_duplicate_3 R_RNDR1b_duplicate_4 R_RNDR2b R_RNDR2b_duplicate_2 R_RNDR2b_duplicate_3 R_RNDR2b_duplicate_4 R_RNDR3b R_RNDR3b_duplicate_2 R_RNDR3b_duplicate_3 R_RNDR3b_duplicate_4 R_RNDR4b R_RNDR4b_duplicate_2 R_RNDR4b_duplicate_3 R_RNDR4b_duplicate_4	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	R_RNDR1b R_RNDR1b_duplicate_2 R_RNDR1b_duplicate_3 R_RNDR1b_duplicate_4 R_RNDR2b R_RNDR2b_duplicate_2 R_RNDR2b_duplicate_3 R_RNDR2b_duplicate_4 R_RNDR3b R_RNDR3b_duplicate_2 R_RNDR3b_duplicate_3 R_RNDR3b_duplicate_4 R_RNDR4b R_RNDR4b_duplicate_2 R_RNDR4b_duplicate_3 R_RNDR4b_duplicate_4	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}.
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_enzyme R_MDDCP2pp_duplicate_4_enzyme R_MDDCP3pp_duplicate_4_enzyme R_MDDCP4pp_duplicate_4_enzyme R_MDDCP5pp_duplicate_4_enzyme	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		R_CMtpp_duplicate_2_enzyme R_DOXRBCNtpp_duplicate_2_enzyme R_FUSAtpp_duplicate_2_enzyme R_MINCYCtpp_duplicate_2_enzyme R_NOVBCNtpp_duplicate_2_enzyme R_RFAMPtpp_duplicate_2_enzyme R_TTRCYCtpp_duplicate_2_enzyme	R_CMtpp_duplicate_2 R_DOXRBCNtpp_duplicate_2 R_FUSAtpp_duplicate_2 R_MINCYCtpp_duplicate_2 R_NOVBCNtpp_duplicate_2 R_RFAMPtpp_duplicate_2 R_TTRCYCtpp_duplicate_2	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
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
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
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	R_RNTR1c2 R_RNTR1c2_duplicate_2 R_RNTR1c2_duplicate_3 R_RNTR1c2_duplicate_4 R_RNTR2c2 R_RNTR2c2_duplicate_2 R_RNTR2c2_duplicate_3 R_RNTR2c2_duplicate_4 R_RNTR3c2 R_RNTR3c2_duplicate_2 R_RNTR3c2_duplicate_3 R_RNTR3c2_duplicate_4 R_RNTR4c2 R_RNTR4c2_duplicate_2 R_RNTR4c2_duplicate_3 R_RNTR4c2_duplicate_4	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
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_enzyme R_COBALT2t3pp_enzyme R_MN2t3pp_duplicate_2_enzyme R_NI2t3pp_duplicate_2_enzyme R_ZN2t3pp_duplicate_2_enzyme	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
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}.
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_enzyme R_PGSA140_enzyme R_PGSA141_enzyme R_PGSA160_enzyme R_PGSA161_enzyme R_PGSA180_enzyme R_PGSA181_enzyme	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_enzyme R_FA120ACPHi_enzyme R_FA140ACPHi_enzyme R_FA141ACPHi_enzyme R_FA160ACPHi_enzyme R_FA161ACPHi_enzyme R_FA80ACPHi_enzyme	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		R_CLPNS120pp_enzyme R_CLPNS140pp_duplicate_2_enzyme R_CLPNS141pp_enzyme R_CLPNS160pp_enzyme R_CLPNS161pp_duplicate_2_enzyme R_CLPNS180pp_enzyme R_CLPNS181pp_enzyme	R_CLPNS120pp R_CLPNS140pp_duplicate_2 R_CLPNS141pp R_CLPNS160pp R_CLPNS161pp_duplicate_2 R_CLPNS180pp R_CLPNS181pp	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}.
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}.
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		R_ADNt2pp_copy1_duplicate_2_enzyme R_CYTDt2pp_copy1_enzyme R_DADNt2pp_duplicate_2_enzyme R_DCYTt2pp_enzyme R_DURIt2pp_duplicate_2_enzyme R_THMDt2pp_copy1_enzyme R_URIt2pp_copy1_enzyme	R_ADNt2pp_copy1_duplicate_2 R_CYTDt2pp_copy1 R_DADNt2pp_duplicate_2 R_DCYTt2pp R_DURIt2pp_duplicate_2 R_THMDt2pp_copy1 R_URIt2pp_copy1	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
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
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
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}.
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}.
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.
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_enzyme R_COBALT2abcpp_enzyme R_CU2abcpp_enzyme R_HG2abcpp_enzyme R_NI2abcpp_enzyme R_ZN2abcpp_enzyme	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}.
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
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
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
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
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
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}.
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}.
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}.
b2423	b2423	Sulfate transport system permease protein CysW	Cell_inner_membrane		R_MOBDabcpp_enzyme R_MOBDabcpp_duplicate_3_enzyme R_SELtpp_enzyme R_SLNTtpp_enzyme R_SULabcpp_duplicate_2_enzyme R_SULabcpp_duplicate_3_enzyme R_TSULabcpp_enzyme R_TSULabcpp_duplicate_2_enzyme	R_MOBDabcpp R_MOBDabcpp_duplicate_3 R_SELtpp R_SLNTtpp R_SULabcpp_duplicate_2 R_SULabcpp_duplicate_3 R_TSULabcpp R_TSULabcpp_duplicate_2	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		R_MOBDabcpp_enzyme R_MOBDabcpp_duplicate_3_enzyme R_SELtpp_enzyme R_SLNTtpp_enzyme R_SULabcpp_duplicate_2_enzyme R_SULabcpp_duplicate_3_enzyme R_TSULabcpp_enzyme R_TSULabcpp_duplicate_2_enzyme	R_MOBDabcpp R_MOBDabcpp_duplicate_3 R_SELtpp R_SLNTtpp R_SULabcpp_duplicate_2 R_SULabcpp_duplicate_3 R_TSULabcpp R_TSULabcpp_duplicate_2	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.-
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}.
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}.
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		R_MOBDabcpp_enzyme R_MOBDabcpp_duplicate_3_enzyme R_SELtpp_enzyme R_SLNTtpp_enzyme R_SULabcpp_duplicate_2_enzyme R_SULabcpp_duplicate_3_enzyme R_TSULabcpp_enzyme R_TSULabcpp_duplicate_2_enzyme	R_MOBDabcpp R_MOBDabcpp_duplicate_3 R_SELtpp R_SLNTtpp R_SULabcpp_duplicate_2 R_SULabcpp_duplicate_3 R_TSULabcpp R_TSULabcpp_duplicate_2	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		R_PGPP120_duplicate_2_enzyme R_PGPP120pp_enzyme R_PGPP140_duplicate_2_enzyme R_PGPP140pp_enzyme R_PGPP141_duplicate_2_enzyme R_PGPP141pp_enzyme R_PGPP160_enzyme R_PGPP160pp_enzyme R_PGPP161_duplicate_2_enzyme R_PGPP161pp_enzyme R_PGPP180_enzyme R_PGPP180pp_enzyme R_PGPP181_duplicate_2_enzyme R_PGPP181pp_enzyme	R_PGPP120_duplicate_2 R_PGPP120pp R_PGPP140_duplicate_2 R_PGPP140pp R_PGPP141_duplicate_2 R_PGPP141pp R_PGPP160 R_PGPP160pp R_PGPP161_duplicate_2 R_PGPP161pp R_PGPP180 R_PGPP180pp R_PGPP181_duplicate_2 R_PGPP181pp	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_enzyme R_DADNtex_enzyme R_DCYTtex_enzyme R_DURItex_enzyme R_GUAtex_enzyme R_INStex_enzyme R_URItex_enzyme	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}.
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
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}.
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
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}.
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
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
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
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
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}.
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
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		R_FLDR2_enzyme R_FLDR2_duplicate_2_enzyme R_RNTR1c2_duplicate_2_enzyme R_RNTR1c2_duplicate_3_enzyme R_RNTR2c2_duplicate_2_enzyme R_RNTR2c2_duplicate_3_enzyme R_RNTR3c2_duplicate_2_enzyme R_RNTR3c2_duplicate_3_enzyme R_RNTR4c2_duplicate_2_enzyme R_RNTR4c2_duplicate_3_enzyme	R_FLDR2 R_FLDR2_duplicate_2 R_RNTR1c2_duplicate_2 R_RNTR1c2_duplicate_3 R_RNTR2c2_duplicate_2 R_RNTR2c2_duplicate_3 R_RNTR3c2_duplicate_2 R_RNTR3c2_duplicate_3 R_RNTR4c2_duplicate_2 R_RNTR4c2_duplicate_3	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}.
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	R_EAR100x R_EAR100y R_EAR120x R_EAR120y R_EAR121x R_EAR121y R_EAR140x R_EAR140y R_EAR141x R_EAR141y R_EAR160x R_EAR160y R_EAR161x R_EAR161y R_EAR180x R_EAR180y R_EAR181x R_EAR181y R_EAR40x R_EAR40y R_EAR60x R_EAR60y R_EAR80x R_EAR80y R_EGMEACPR R_EPMEACPR	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	R_2AGPA120tipp R_2AGPA140tipp R_2AGPA141tipp R_2AGPA160tipp R_2AGPA161tipp R_2AGPA180tipp R_2AGPA181tipp R_2AGPE120tipp R_2AGPE140tipp R_2AGPE141tipp R_2AGPE160tipp R_2AGPE161tipp R_2AGPE180tipp R_2AGPE181tipp R_2AGPG120tipp R_2AGPG140tipp R_2AGPG141tipp R_2AGPG160tipp R_2AGPG161tipp R_2AGPG180tipp R_2AGPG181tipp	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
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		R_DURIPP_duplicate_2_enzyme R_PUNP1_enzyme R_PUNP2_enzyme R_PUNP3_duplicate_2_enzyme R_PUNP4_duplicate_2_enzyme R_PUNP5_duplicate_2_enzyme R_PUNP6_duplicate_2_enzyme	R_DURIPP_duplicate_2 R_PUNP1 R_PUNP2 R_PUNP3_duplicate_2 R_PUNP4_duplicate_2 R_PUNP5_duplicate_2 R_PUNP6_duplicate_2	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}.
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}.
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
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	R_CMtpp R_CMtpp_duplicate_2 R_DOXRBCNtpp R_DOXRBCNtpp_duplicate_2 R_FUSAtpp R_FUSAtpp_duplicate_2 R_MINCYCtpp R_MINCYCtpp_duplicate_2 R_NOVBCNtpp R_NOVBCNtpp_duplicate_2 R_RFAMPtpp R_RFAMPtpp_duplicate_2 R_TTRCYCtpp R_TTRCYCtpp_duplicate_2	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_enzyme R_DOXRBCNtpp_enzyme R_FUSAtpp_enzyme R_MINCYCtpp_enzyme R_NOVBCNtpp_enzyme R_RFAMPtpp_enzyme R_TTRCYCtpp_enzyme	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}.
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_enzyme R_PSD140_enzyme R_PSD141_enzyme R_PSD160_enzyme R_PSD161_enzyme R_PSD180_enzyme R_PSD181_enzyme	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}.
b4035	b4035	Maltose/maltodextrin import ATP-binding protein MalK (EC 3.6.3.19)	Cell_inner_membrane		R_14GLUCANabcpp_enzyme R_MALTHXabcpp_enzyme R_MALTPTabcpp_enzyme R_MALTTRabcpp_enzyme R_MALTTTRabcpp_enzyme R_MALTabcpp_enzyme	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
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
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
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
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}.
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_enzyme R_MCTP1Bpp_duplicate_2_enzyme R_MCTP2App_enzyme R_MPTG_duplicate_2_enzyme R_MPTG2_duplicate_2_enzyme	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
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.
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.
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.
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}.
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.
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}.
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
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}.
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
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
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}.
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}.
b3200	b3200	Lipopolysaccharide export system protein LptA	Periplasm		R_ACOLIPAabctex_enzyme R_CLIPAabctex_enzyme R_COLIPAPabctex_enzyme R_COLIPAabctex_enzyme R_ECA4COLIPAabctex_enzyme R_ENLIPAabctex_enzyme R_K2L4Aabctex_enzyme R_LIPAabctex_enzyme R_O16A4COLIPAabctex_enzyme	R_ACOLIPAabctex R_CLIPAabctex R_COLIPAPabctex R_COLIPAabctex R_ECA4COLIPAabctex R_ENLIPAabctex R_K2L4Aabctex R_LIPAabctex R_O16A4COLIPAabctex	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}.
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		R_FACOAL100t2pp_duplicate_2_enzyme R_FACOAL120t2pp_enzyme R_FACOAL140t2pp_enzyme R_FACOAL141t2pp_enzyme R_FACOAL160t2pp_enzyme R_FACOAL161t2pp_duplicate_2_enzyme R_FACOAL180t2pp_enzyme R_FACOAL181t2pp_duplicate_2_enzyme R_FACOAL60t2pp_duplicate_2_enzyme R_FACOAL80t2pp_duplicate_2_enzyme	R_FACOAL100t2pp_duplicate_2 R_FACOAL120t2pp R_FACOAL140t2pp R_FACOAL141t2pp R_FACOAL160t2pp R_FACOAL161t2pp_duplicate_2 R_FACOAL180t2pp R_FACOAL181t2pp_duplicate_2 R_FACOAL60t2pp_duplicate_2 R_FACOAL80t2pp_duplicate_2	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}.
b1252	b1252	Protein TonB	Cell_inner_membrane		R_ADOCBLtonex_enzyme R_CBItonex_enzyme R_CBL1tonex_enzyme R_CPGNtonex_enzyme R_FE3DCITtonex_enzyme R_FE3DHBZStonex_enzyme R_FE3DHBZStonex_duplicate_2_enzyme R_FE3HOXtonex_enzyme R_FECRMtonex_enzyme R_FEENTERtonex_enzyme R_FEOXAMtonex_enzyme	R_ADOCBLtonex R_CBItonex R_CBL1tonex R_CPGNtonex R_FE3DCITtonex R_FE3DHBZStonex R_FE3DHBZStonex_duplicate_2 R_FE3HOXtonex R_FECRMtonex R_FEENTERtonex R_FEOXAMtonex	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}.
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}.
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
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
b0474	b0474	Adenylate kinase (AK) (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate monophosphate kinase)	Cytoplasm		R_ADK1_enzyme R_ADK3_enzyme R_ADK4_enzyme R_ADNK1_enzyme R_DADK_enzyme R_NDPK1_enzyme R_NDPK2_enzyme R_NDPK3_duplicate_2_enzyme R_NDPK4_enzyme R_NDPK5_enzyme R_NDPK6_duplicate_2_enzyme R_NDPK7_enzyme R_NDPK8_enzyme	R_ADK1 R_ADK3 R_ADK4 R_ADNK1 R_DADK R_NDPK1 R_NDPK2 R_NDPK3_duplicate_2 R_NDPK4 R_NDPK5 R_NDPK6_duplicate_2 R_NDPK7 R_NDPK8	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
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).
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
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
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
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
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}.
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_enzyme R_AGPAT140_enzyme R_AGPAT141_enzyme R_AGPAT160_enzyme R_AGPAT161_enzyme R_AGPAT180_enzyme R_AGPAT181_enzyme	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
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
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
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}.
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}.
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_enzyme R_NTD12_enzyme R_NTD3_duplicate_2_enzyme R_NTD5_duplicate_2_enzyme R_NTD6_enzyme R_NTD8_enzyme	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}.
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	R_2AGPEAT120 R_2AGPEAT140 R_2AGPEAT141 R_2AGPEAT160 R_2AGPEAT161 R_2AGPEAT180 R_2AGPEAT181 R_2AGPGAT120 R_2AGPGAT140 R_2AGPGAT141 R_2AGPGAT160 R_2AGPGAT161 R_2AGPGAT180 R_2AGPGAT181 R_AACPS1 R_AACPS2 R_AACPS3 R_AACPS4 R_AACPS5 R_AACPS6 R_AACPS7 R_AACPS8 R_AACPS9	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}.
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}.
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		R_NTD1_enzyme R_NTD10_enzyme R_NTD11_enzyme R_NTD12_duplicate_2_enzyme R_NTD2_enzyme R_NTD3_enzyme R_NTD4_enzyme R_NTD5_enzyme R_NTD6_duplicate_2_enzyme R_NTD7_enzyme R_NTD8_duplicate_2_enzyme R_NTD9_enzyme R_PPA_duplicate_2_enzyme R_PPA2_duplicate_2_enzyme	R_NTD1 R_NTD10 R_NTD11 R_NTD12_duplicate_2 R_NTD2 R_NTD3 R_NTD4 R_NTD5 R_NTD6_duplicate_2 R_NTD7 R_NTD8_duplicate_2 R_NTD9 R_PPA_duplicate_2 R_PPA2_duplicate_2	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}.
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
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}.
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
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}.
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
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
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
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}.
b1249	b1249	Cardiolipin synthase A (CL synthase) (EC 2.7.8.-)	Cell_inner_membrane		R_CLPNS120pp_duplicate_2_enzyme R_CLPNS140pp_enzyme R_CLPNS141pp_duplicate_2_enzyme R_CLPNS160pp_duplicate_2_enzyme R_CLPNS161pp_enzyme R_CLPNS180pp_duplicate_2_enzyme R_CLPNS181pp_duplicate_2_enzyme	R_CLPNS120pp_duplicate_2 R_CLPNS140pp R_CLPNS141pp_duplicate_2 R_CLPNS160pp_duplicate_2 R_CLPNS161pp R_CLPNS180pp_duplicate_2 R_CLPNS181pp_duplicate_2	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}.
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}.
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}.
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
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		R_14GLUCANtexi_enzyme R_GLCtex_copy2_enzyme R_MALTHXtexi_enzyme R_MALTPTtexi_enzyme R_MALTTRtexi_enzyme R_MALTTTRtexi_enzyme R_MALTtexi_enzyme	R_14GLUCANtexi R_GLCtex_copy2 R_MALTHXtexi R_MALTPTtexi R_MALTTRtexi R_MALTTTRtexi R_MALTtexi	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_enzyme R_MALTHXabcpp_enzyme R_MALTPTabcpp_enzyme R_MALTTRabcpp_enzyme R_MALTTTRabcpp_enzyme R_MALTabcpp_enzyme	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_enzyme R_MALTHXabcpp_enzyme R_MALTPTabcpp_enzyme R_MALTTRabcpp_enzyme R_MALTTTRabcpp_enzyme R_MALTabcpp_enzyme	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		R_ADOCBLtonex_enzyme R_CBItonex_enzyme R_CBL1tonex_enzyme R_CPGNtonex_enzyme R_FE3DCITtonex_enzyme R_FE3DHBZStonex_enzyme R_FE3DHBZStonex_duplicate_2_enzyme R_FE3HOXtonex_enzyme R_FECRMtonex_enzyme R_FEENTERtonex_enzyme R_FEOXAMtonex_enzyme	R_ADOCBLtonex R_CBItonex R_CBL1tonex R_CPGNtonex R_FE3DCITtonex R_FE3DHBZStonex R_FE3DHBZStonex_duplicate_2 R_FE3HOXtonex R_FECRMtonex R_FEENTERtonex R_FEOXAMtonex	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		R_ADOCBLtonex_enzyme R_CBItonex_enzyme R_CBL1tonex_enzyme R_CPGNtonex_enzyme R_FE3DCITtonex_enzyme R_FE3DHBZStonex_enzyme R_FE3DHBZStonex_duplicate_2_enzyme R_FE3HOXtonex_enzyme R_FECRMtonex_enzyme R_FEENTERtonex_enzyme R_FEOXAMtonex_enzyme	R_ADOCBLtonex R_CBItonex R_CBL1tonex R_CPGNtonex R_FE3DCITtonex R_FE3DHBZStonex R_FE3DHBZStonex_duplicate_2 R_FE3HOXtonex R_FECRMtonex R_FEENTERtonex R_FEOXAMtonex	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		R_RNTR1c2_duplicate_2_enzyme R_RNTR1c2_duplicate_3_enzyme R_RNTR2c2_duplicate_2_enzyme R_RNTR2c2_duplicate_3_enzyme R_RNTR3c2_duplicate_2_enzyme R_RNTR3c2_duplicate_3_enzyme R_RNTR4c2_duplicate_2_enzyme R_RNTR4c2_duplicate_3_enzyme	R_RNTR1c2_duplicate_2 R_RNTR1c2_duplicate_3 R_RNTR2c2_duplicate_2 R_RNTR2c2_duplicate_3 R_RNTR3c2_duplicate_2 R_RNTR3c2_duplicate_3 R_RNTR4c2_duplicate_2 R_RNTR4c2_duplicate_3	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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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.
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.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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}.
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.
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}.
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}.
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}.
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.
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}.
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}.

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