FUNCTION: Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA 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 (By similarity). Has a role in growth and sporulation on acetate. {ECO:0000250, ECO:0000269|PubMed:7934817}.

FUNCTION: Provides the ATPase subunit for at least 2 ABC transporter complexes; YfiYZ/YfhA/YusV involved in import of the iron-hydroxamate siderophores schizokinen, arthrobactin and corprogen (Probable), and FeuABC/YusV involved in import of the catecholate siderophores bacillibactin and enterobactin (Probable). Probably responsible for energy coupling to the transport system (By similarity). {ECO:0000250, ECO:0000269|PubMed:16672620, ECO:0000305}.

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 LevDE PTS system is involved in fructose transport. {ECO:0000269|PubMed:9033408, ECO:0000305|PubMed:2117666}.; FUNCTION: LevD and LevE act as negative regulators of the levanase operon. They may be involved in a PTS-mediated phosphorylation of a regulator. {ECO:0000269|PubMed:2117666}.

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 GmuABC PTS system is involved in the transport of oligo-glucomannans such as cellobiose or mannobiose. {ECO:0000305|PubMed:18177310}.

FUNCTION: Involved in the gluconeogenesis. Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NADP. 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 NADP to NADPH. The reduced NADPH is then exchanged with the second NADP, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG. {ECO:0000269|PubMed:10799476}.

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 (By similarity). {ECO:0000250}.

FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity). {ECO:0000250}.

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. {ECO:0000255|HAMAP-Rule:MF_01988}.

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}.

FUNCTION: Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. RocG is unable to utilize glutamate or glutamine as sole carbon source and to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars. {ECO:0000269|PubMed:17183217, ECO:0000269|PubMed:18326565, ECO:0000269|PubMed:9829940}.

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex (EC 2.3.1.168) (Branched-chain alpha-keto acid dehydrogenase complex component E2) (BCKAD-E2) (BCKADE2) (Dihydrolipoamide acetyltransferase component of branched-chain alpha-keto acid dehydrogenase complex) (Dihydrolipoamide branched chain transacylase) (Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase)

FUNCTION: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+). {ECO:0000269|PubMed:10198001, ECO:0000269|PubMed:10648512, ECO:0000269|PubMed:17293423, ECO:0000269|PubMed:9878723}.

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). {ECO:0000250|UniProtKB:P08839}.

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. {ECO:0000255|HAMAP-Rule:MF_00435}.

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 (By similarity). {ECO:0000250}.

Putative PTS system glucosamine-specific EIICBA component [Includes: Glucosamine permease IIC component (PTS system glucosamine-specific EIIC component); Glucosamine-specific phosphotransferase enzyme IIB component (EC 2.7.1.193) (PTS system glucosamine-specific EIIB component); Glucosamine-specific phosphotransferase enzyme IIA component (EC 2.7.1.193) (PTS system glucosamine-specific EIIA component)

FUNCTION: Mediates uptake of riboflavin and roseoflavin, a toxic riboflavin analog; may also transport FMN. Probably a riboflavin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins (By similarity). {ECO:0000250, ECO:0000269|PubMed:17693491}.

FUNCTION: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+). {ECO:0000269|PubMed:10198001, ECO:0000269|PubMed:17293423}.

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 (GTP, UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:12897004}.

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_01396}.; FUNCTION: Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits. {ECO:0000255|HAMAP-Rule:MF_01396}.

FUNCTION: Catalyzes the formation of pyridoxal 5-phosphate from ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The ammonia is provided by the PdxT subunit. Can also use ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, resulting from enzyme-catalyzed isomerization of RBP and G3P, respectively. {ECO:0000255|HAMAP-Rule:MF_01824, ECO:0000269|PubMed:16030023, ECO:0000269|PubMed:18271580}.

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. Also involved in the biosynthesis of anthranilate. {ECO:0000269|PubMed:2123867}.

FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme a of subunit 1 to the bimetallic center formed by heme a3 and copper B. This cytochrome c oxidase shows proton pump activity across the membrane in addition to the electron transfer.

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 LevDE PTS system is involved in fructose transport. {ECO:0000269|PubMed:9033408, ECO:0000305|PubMed:2117666, ECO:0000305|PubMed:9551099}.; FUNCTION: LevD and LevE act as negative regulators of the levanase operon. They may be involved in a PTS-mediated phosphorylation of a regulator. {ECO:0000269|PubMed:2117666}.

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}.

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). The misacylated Cys-tRNA(Pro) is not edited by ProRS. {ECO:0000255|HAMAP-Rule:MF_01569}.

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 sucrose transport. {ECO:0000250}.; FUNCTION: Acts as both a kinase and a phosphatase on SacT. {ECO:0000250}.

PTS system fructose-specific EIIABC component (EIIABC-Fru) [Includes: PTS system fructose-specific EIIA component (EC 2.7.1.202) (EII-Fru) (Fructose-specific phosphotransferase enzyme IIA component); 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)

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 branched chain acyl-CoA, determining the biosynthesis of branched-chain of fatty acids instead of straight-chain. {ECO:0000269|PubMed:10629181}.

Processive diacylglycerol beta-glucosyltransferase (EC 2.4.1.315) (Beta-diglucosyldiacylglycerol synthase) (Beta-DGS) (DGlcDAG synthase) (Glc2-DAG synthase) (Beta-gentiobiosyldiacylglycerol synthase) (Beta-monoglucosyldiacylglycerol synthase) (Beta-MGS) (MGlcDAG synthase) (Beta-triglucosyldiacylglycerol synthase) (TGlcDAG synthase) (Diglucosyl diacylglycerol synthase (1,6-linking)) (Glucosyl-beta-1,6-glucosyldiacylglycerol synthase) (UDP glucosyltransferase) (UDP-glucose:1,2-diacylglycerol-3-beta-D-glucosyltransferase)

FUNCTION: Processive glucosyltransferase involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. Is able to successively transfer up to three glucosyl residues to diacylglycerol (DAG), thereby catalyzing the formation of beta-monoglucosyl-DAG (3-O-(beta-D-glucopyranosyl)-1,2-diacyl-sn-glycerol), beta-diglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol) and beta-triglucosyl-DAG (3-O-(beta-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl-beta-(1->6)-D-glucopyranosyl)-1,2-diacyl-sn-glycerol). Beta-diglucosyl-DAG is the predominant glycolipid found in Bacillales and is also used as a membrane anchor for lipoteichoic acid (LTA). Also seems to be able to form beta-tetraglucosyl-DAG, although this glycolipid has not been found in B.subtilis membrane. UgtP can only use UDP-glucose as sugar donor. {ECO:0000255|HAMAP-Rule:MF_01280, ECO:0000269|PubMed:9720862}.

PTS system glucose-specific EIICBA component (EC 2.7.1.199) (EII-Glc/EIII-Glc) (EIICBA-Glc) (EIICBA-Glc 1) [Includes: Glucose permease IIC component (PTS system glucose-specific EIIC component); Glucose-specific phosphotransferase enzyme IIB component (PTS system glucose-specific EIIB component); Glucose-specific phosphotransferase enzyme IIA component (PTS system glucose-specific EIIA component)

FUNCTION: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+). {ECO:0000269|PubMed:10198001, ECO:0000269|PubMed:17293423}.

FUNCTION: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).; FUNCTION: Involved in cholate and Na(+) efflux activities, which may be mechanistically coupled. Does not require other Mrp proteins for its own function.

FUNCTION: Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP-Rule:MF_00421, ECO:0000269|PubMed:15301530}.

FUNCTION: Catalyzes the FAD-dependent oxidative deamination of various amines and D-amino acids to yield the corresponding alpha-keto acids, ammonia/amine, and hydrogen peroxide. Oxidizes sarcosine (N-methylglycine), N-ethylglycine and glycine (PubMed:9827558, PubMed:11744710, PubMed:19864430). Can also oxidize the herbicide glyphosate (N-phosphonomethylglycine) (PubMed:19864430). Displays lower activities on D-alanine, D-valine, D-proline and D-methionine (PubMed:9827558, PubMed:11744710). Does not act on L-amino acids and other D-amino acids (PubMed:9827558). Is essential for thiamine biosynthesis since the oxidation of glycine catalyzed by ThiO generates the glycine imine intermediate (dehydroglycine) required for the biosynthesis of the thiazole ring of thiamine pyrophosphate (PubMed:12627963). {ECO:0000269|PubMed:11744710, ECO:0000269|PubMed:12627963, ECO:0000269|PubMed:19864430, ECO:0000269|PubMed:9827558}.

Es14_enzyme
Es16_enzyme
Es18_enzyme
Ee14_enzyme
Ee16_enzyme
Eo15_enzyme
Eo17_enzyme
Ea15_enzyme
Ea17_enzyme

Es14_enzyme
Es16_enzyme
Es18_enzyme
Ee14_enzyme
Ee16_enzyme
Eo15_enzyme
Eo17_enzyme
Ea15_enzyme
Ea17_enzyme

Es14_enzyme
Es16_enzyme
Es18_enzyme
Ee14_enzyme
Ee16_enzyme
Eo15_enzyme
Eo17_enzyme
Ea15_enzyme
Ea17_enzyme

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). {ECO:0000269|PubMed:17458547}.