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| | pdxS | Glutamine amidotransferase for pyridoxal phosphate synthesis; 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. (294 aa) |
| | pdxT | Glutamine amidotransferase for pyridoxal phosphate synthesis; Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS. (196 aa) |
| | prs | Phosphoribosylpyrophosphate synthetase; 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). (317 aa) |
| | ilvE | Ketomethiobutyrate-branched-chain/aromatic amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Involved in the final step of the methionine regeneration pathway, where ketomethiobutyrate (KMTB) is converted to methionine via a transamination. The amino donor preference is isoleucine, leucine, valine, phenylalanine, and tyrosine; Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (356 aa) |
| | ansZ | L-asparaginase 2 (putative lipoprotein); Catalyzes the conversion of L-asparagine to L-aspartate and ammonium. (375 aa) |
| | ldh | L-lactate dehydrogenase; Catalyzes the conversion of lactate to pyruvate. (321 aa) |
| | yclM | Aspartate kinase III; Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. (454 aa) |
| | gabR | Transcriptional regulator (GntR/MocR family) with PLP binding site; Activates the transcription of the gabTD operon. Is also a repressor of its own expression, both in the presence and absence of GABA. Binds specifically to the DNA region overlapping the -35 region of the gabT promoter and the -10 and +1 regions of the gabR promoter. Principally regulates the utilization of gamma-aminobutyrate. In the C-terminal section; belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (479 aa) |
| | gabT | 4-aminobutyrate aminotransferase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. (436 aa) |
| | gabD | Succinate-semialdehyde dehydrogenase; Catalyzes the NADP(+) dependent oxidation of succinate semialdehyde to succinate. (462 aa) |
| | ydaP | Putative enzyme with pyruvate as substrate; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (574 aa) |
| | bdhA | Acetoin reductase/2,3-butanediol dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (346 aa) |
| | yerD | Putative flavoenzyme; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (525 aa) |
| | cypD | Putative bifunctional P-450/NADPH-P450 reductase 1; Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS). (1061 aa) |
| | yflL | Putative acylphosphatase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the acylphosphatase family. (91 aa) |
| | acoA | Acetoin dehydrogenase E1 component (TPP-dependent alpha subunit); Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage of acetoin into acetate and acetaldehyde. The alpha subunit is probably the catalytic subunit of the enzyme (By similarity). (333 aa) |
| | acoB | Acetoin dehydrogenase E1 component (TPP-dependent beta subunit); Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage of acetoin into acetate and acetaldehyde. (342 aa) |
| | acoC | Acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (398 aa) |
| | acoL | Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (458 aa) |
| | acoR | Transcriptional regulator; Acts as a transcriptional activator of the acoABCL operon encoding the acetoin dehydrogenase complex. (605 aa) |
| | citA | Citrate synthase I; Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect; Belongs to the citrate synthase family. (366 aa) |
| | yhdR | Putative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (393 aa) |
| | serC | Phosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (359 aa) |
| | lplJ | Lipoate-protein ligase; 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 use octanoate as substrate. (331 aa) |
| | asnO | Asparagine synthetase; Asparagine synthetase involved in sporulation. (614 aa) |
| | tnrA | Nitrogen sensing transcriptional regulator; Transcription regulator that actives the transcription of genes required for nitrogen assimilation such as nrgAB (ammonium transport), nasABCDEF (nitrate/nitrite assimilation), ureABC (urea degradation) and gabP (GABA transport), during nitrogen limitation. Also represses glnRA and gltAB in the absence of ammonium. On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, TnrA requires a DNA sequence of 17 nucleotides as minimal binding site. (110 aa) |
| | dapX | N-acetyl-L,L-diaminopimelate aminotransferase; Essential for murein biosynthesis. Probably catalyzes the conversion of L-2-acetamido-6-oxopimelate to N-acetyl-LL- 2,6-diaminopimelate (Probable); Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (393 aa) |
| | dapH | Tetrahydrodipicolinate N-acetyltransferase; Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate. (236 aa) |
| | dapL | N-acetyl-diaminopimelate deacetylase; Catalyzes the conversion of N-acetyl-diaminopimelate to diaminopimelate and acetate. (374 aa) |
| | pdhA | Pyruvate dehydrogenase (E1 alpha subunit); 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). (371 aa) |
| | pdhB | Pyruvate dehydrogenase (E1 beta subunit); 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). (325 aa) |
| | pdhC | Pyruvate dehydrogenase (dihydrolipoamide acetyltransferase E2 subunit); 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). (442 aa) |
| | pdhD | Dihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (470 aa) |
| | glsB | Glutaminase; Evidence 2b: Function of strongly homologous gene; Product type e: enzyme. (309 aa) |
| | pycA | Pyruvate carboxylase; Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second, leading to oxaloacetate production. Fulfills an anaplerotic function in B.subtilis as it is necessary for growth on glucose, but is not required for sporulation. (1148 aa) |
| | sucC | succinyl-CoA synthetase (beta subunit); 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. (385 aa) |
| | sucD | succinyl-CoA synthetase (alpha subunit); 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. (300 aa) |
| | codY | Transcriptional regulator, GTP and BCAA-dependent; DNA-binding protein that represses the expression of many genes that are induced as cells make the transition from rapid exponential growth to stationary phase and sporulation. It is a GTP- binding protein that senses the intracellular GTP concentration as an indicator of nutritional limitations. At low GTP concentration it no longer binds GTP and stop to act as a transcriptional repressor. (259 aa) |
| | asd | Aspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (346 aa) |
| | dapG | Aspartokinase I (alpha and beta subunits); Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. Belongs to the aspartokinase family. (404 aa) |
| | dapA | Dihydrodipicolinate synthase; Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA). (290 aa) |
| | glnR | Transcriptional regulator (nitrogen metabolism); Transcription repressor that represses many genes including ureABC and tnrA, during nitrogen excess. On the contrary of the MerR members, which require longer DNA sites for high-affinity binding, GlnR requires a DNA sequence of 17 nucleotides as minimal binding site. (135 aa) |
| | glnA | Glutamine synthetase; Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA- binding active state and turns on the transcription of genes required for nitrogen assimilation. Under condi [...] (444 aa) |
| | tkt | Transketolase; 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. (667 aa) |
| | citB | Aconitate hydratase (aconitase); Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Also catalyzes the rehydration of 2- methyl-cis-aconitate to produce 2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein which plays a role in the regulation of citrate concentration and in the sporulation. To prevent the accumulation of excessive levels of citrate, it binds near the 5' end of the citZ mRNA, decreasing its stability and thereby limiting the conce [...] (909 aa) |
| | yoeD | Putative excisionase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (76 aa) |
| | gltB | Glutamate synthase (small subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (493 aa) |
| | gltA | Glutamate synthase (large subunit); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the glutamate synthase family. (1520 aa) |
| | gltC | Transcriptional regulator (LysR family); Positive regulator of glutamate biosynthesis (gltAB genes). Negatively regulates its own expression. (300 aa) |
| | dhaS | Putative aldehyde dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the aldehyde dehydrogenase family. (495 aa) |
| | odhB | 2-oxoglutarate dehydrogenase complex (dihydrolipoamide transsuccinylase, E2 subunit); E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2). (417 aa) |
| | odhA | 2-oxoglutarate dehydrogenase (E1 subunit); E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2). (944 aa) |
| | ilvA | Threonine dehydratase; 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). (422 aa) |
| | ilvD | Dihydroxy-acid dehydratase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the IlvD/Edd family. (558 aa) |
| | aspB | Putative aspartate aminotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (393 aa) |
| | dapB | (4S)-4-hydroxy-2,3,4, 5-tetrahydro-(2S)-dipicolinic acid (HTPA) dehydratase reductase; Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. (267 aa) |
| | gudB | Cryptic glutamate dehydrogenase; GudB seems to be intrinsically inactive, however spontaneous mutations removing a 9-bp direct repeat within the wild-type gudB sequence activated the GudB protein and allowed more-efficient utilization of amino acids of the glutamate family. This insertion presumably causes severe destabilization of the fold of the protein, leading to an inactive enzyme that is very quickly degraded. The cryptic GudB serves as a buffer that may compensate for mutations in the rocG gene and that can also be decryptified for the utilization of glutamate as a single carbon [...] (427 aa) |
| | serA | 3-phosphoglycerate dehydrogenase; 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. (525 aa) |
| | lysA | Diaminopimelate decarboxylase; Specifically catalyzes the decarboxylation of meso- diaminopimelate (meso-DAP) to L-lysine. (439 aa) |
| | drm | Phosphopentomutase; Phosphotransfer between the C1 and C5 carbon atoms of pentose; Belongs to the phosphopentomutase family. (394 aa) |
| | mleA | NAD-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (439 aa) |
| | mleN | malate-H+/Na+-lactate antiporter; Couples proton uptake and Na(+) efflux to the substrate- product malate/lactate antiport, in an electroneutral malate- 2H(+)/Na(+)-lactate exchange. Plays a role in supporting growth to high density on malate at reduced protonmotive force; Belongs to the NhaC Na(+)/H(+) (TC 2.A.35) antiporter family. (468 aa) |
| | ansB | L-aspartase (aspartate ammonia lyase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-II fumarase/aspartase family. Aspartase subfamily. (475 aa) |
| | ansA | Exported L-asparaginase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the asparaginase 1 family. (329 aa) |
| | nudF | ADP-ribose pyrophosphatase; 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 (By similarity). (185 aa) |
| | bkdB | Branched-chain alpha-keto acid dehydrogenase E2 subunit (lipoamide acyltransferase); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). (424 aa) |
| | bkdAB | Branched-chain alpha-keto acid dehydrogenase E1 subunit; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). (327 aa) |
| | bkdAA | Branched-chain alpha-keto acid dehydrogenase E1 subunit; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the BCKDHA family. (330 aa) |
| | lpdV | Branched-chain alpha-keto acid dehydrogenase E3 subunit (dihydrolipoamide dehydrogenase); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (474 aa) |
| | buk | Branched-chain fatty-acid kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the acetokinase family. (363 aa) |
| | bcd | Branched-chain amino acid dehydrogenase; Catalyzes the reversible deamination of L-leucine to 4- methyl-2-oxopentanoate. (364 aa) |
| | ptb | Phosphate butyryl coenzyme A transferase; Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate; Belongs to the phosphate acetyltransferase and butyryltransferase family. (299 aa) |
| | lipM | Protein octanoyltransferase; Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domain of GcvH, an intermediate carrier during protein lipoylation. Is also able to catalyze the reverse reaction. Octanoyl-CoA can also act as a substrate although very poorly. Does not display lipoate protein ligase activity, despite its sequence similarity to LplA; Belongs to the octanoyltransferase LipM family. (278 aa) |
| | gcvPB | Glycine decarboxylase (subunit 2) (glycine cleavage system protein P); 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 (By similarity); Belongs to the GcvP family. C-terminal subunit subfamily. (488 aa) |
| | gcvPA | Glycine decarboxylase (subunit 1) (glycine cleavage system protein P); 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 (By similarity). (448 aa) |
| | gcvT | Aminomethyltransferase (glycine cleavage system protein T); The glycine cleavage system catalyzes the degradation of glycine. (362 aa) |
| | adhB | Putative oxidoreductase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the zinc-containing alcohol dehydrogenase family. Class-III subfamily. (378 aa) |
| | adhA | Putative dehydrogenase; Functions in the protection against aldehyde-stress. Belongs to the zinc-containing alcohol dehydrogenase family. (349 aa) |
| | leuD | 3-isopropylmalate dehydratase (small subunit); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily. (199 aa) |
| | leuC | 3-isopropylmalate dehydratase (large subunit); Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate; Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily. (472 aa) |
| | leuB | 3-isopropylmalate dehydrogenase; 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; Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 1 subfamily. (365 aa) |
| | leuA | 2-isopropylmalate synthase; 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); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 1 subfamily. (518 aa) |
| | ilvC | Acetohydroxy-acid isomeroreductase; 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. (342 aa) |
| | ilvH | Acetolactate synthase (acetohydroxy-acid synthase) (small subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the acetolactate synthase small subunit family. (172 aa) |
| | ilvB | Acetolactate synthase (acetohydroxy-acid synthase) (large subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (574 aa) |
| | sdhB | Succinate dehydrogenase (iron-sulfur protein); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family. (253 aa) |
| | sdhA | Succinate dehydrogenase (flavoprotein subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (586 aa) |
| | sdhC | Succinate dehydrogenase (cytochrome b558 subunit); Di-heme cytochrome of the succinate dehydrogenase complex. (202 aa) |
| | lysC | Aspartokinase II alpha subunit (aa 1->408) and beta subunit (aa 246->408); Catalyzes the phosphorylation of the beta-carboxyl group of aspartic acid with ATP to yield 4-phospho-L-aspartate, which is involved in the branched biosynthetic pathway leading to the biosynthesis of amino acids threonine, isoleucine and methionine. (408 aa) |
| | ysaA | Putative phosphatase; Catalyzes the last step of the phosphorylated serine biosynthetic pathway, i.e. dephosphorylation of O-phospho-L-serine to form L-serine. To a lesser extent, is also able to dephosphorylate phosphothreonine, phosphoethanolamine, and histidinol phosphate in vitro; Belongs to the HAD-like hydrolase superfamily. (260 aa) |
| | gapB | Glyceraldehyde-3-phosphate dehydrogenase; 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; Belongs to the gl [...] (340 aa) |
| | mdh | Malate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa) |
| | icd | Isocitrate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (423 aa) |
| | citZ | Citrate synthase II; Might regulate the synthesis and function of enzymes involved in later enzymatic steps of Krebs cycle. Loss in activity results in sporulation defect; Belongs to the citrate synthase family. (372 aa) |
| | pyk | Pyruvate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; In the C-terminal section; belongs to the PEP-utilizing enzyme family. (585 aa) |
| | pfkA | 6-phosphofructokinase; Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis; Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub- subfamily. (319 aa) |
| | ytsJ | NADP-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (410 aa) |
| | ackA | Acetate kinase; Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction. Appears to favor the formation of acetate. Involved in the secretion of excess carbohydrate. (395 aa) |
| | ytcI | Putative acyl-coenzyme A synthetase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the ATP-dependent AMP-binding enzyme family. (529 aa) |
| | acsA | acetyl-CoA synthetase; 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. (572 aa) |
| | ccpA | Transcriptional regulator (Lacl family); Global transcriptional regulator of carbon catabolite repression (CCR) and carbon catabolite activation (CCA), which ensures optimal energy usage under diverse conditions. Interacts with either P- Ser-HPr or P-Ser-Crh, leading to the formation of a complex that binds to DNA at the catabolite-response elements (cre). Binding to DNA allows activation or repression of many different genes and operons. (334 aa) |
| | malS | NAD-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (566 aa) |
| | ytjP | Putative dipeptidase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (463 aa) |
| | asnB | Asparagine synthetase; Main asparagine synthetase in vegetative cells. (632 aa) |
| | pckA | Phosphoenolpyruvate carboxykinase; Involved in the gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA. (527 aa) |
| | pgi | Glucose-6-phosphate isomerase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the GPI family. (450 aa) |
| | dapF | Diaminopimelate epimerase; Catalyzes the stereoinversion of LL-2,6-diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso-DAP), a precursor of L- lysine and an essential component of the bacterial peptidoglycan. (284 aa) |
| | thrB | Homoserine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (309 aa) |
| | thrC | Threonine synthase; Catalyzes the gamma-elimination of phosphate from L- phosphohomoserine and the beta-addition of water to produce L- threonine. (352 aa) |
| | hom | Homoserine dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (433 aa) |
| | lipA | Lipoyl synthase (lipoic acid synthetase); 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; Belongs to the radical SAM superfamily. Lipoyl synthase family. (298 aa) |
| | gcvH | Glycine cleavage system protein H; 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. (127 aa) |
| | fumC | Fumarate hydratase; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. (462 aa) |
| | eno | Enolase; Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis; Belongs to the enolase family. (430 aa) |
| | pgm | Phosphoglycerate mutase; Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (511 aa) |
| | tpiA | Triose phosphate isomerase; Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D- glyceraldehyde-3-phosphate (G3P); Belongs to the triosephosphate isomerase family. (253 aa) |
| | pgk | Phosphoglycerate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the phosphoglycerate kinase family. (394 aa) |
| | gapA | Glyceraldehyde-3-phosphate dehydrogenase; Involved in the glycolysis. 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. (335 aa) |
| | yvkC | Putative phosphotransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the PEP-utilizing enzyme family. (831 aa) |
| | yvyI | Putative phosphohexomutase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type e: enzyme; Belongs to the mannose-6-phosphate isomerase type 1 family. (316 aa) |
| | alsD | Alpha-acetolactate decarboxylase; Converts acetolactate into acetoin, which can be excreted by the cells. This may be a mechanism for controlling the internal pH of cells in the stationary stage; Belongs to the alpha-acetolactate decarboxylase family. (255 aa) |
| | alsS | Alpha-acetolactate synthase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (570 aa) |
| | alsR | Transcriptional regulator controlling alsSD and ictEP expression (LysR family); Regulates the expression of the alsSD operon for acetoin biosynthesis. (302 aa) |
| | ywlG | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; PubMedId: 15995210. (180 aa) |
| | ywlF | Ribose 5-phosphate epimerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (149 aa) |
| | ywjI | Putative fructose 1,6-bisphosphatase class II; Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Can functionally substitute for the FBPase class 3 (Fbp) of B.subtilis. (321 aa) |
| | ywjH | Putative transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. Does not show fructose-6-P aldolase activity. (212 aa) |
| | fbaA | Fructose-1,6-bisphosphate aldolase; 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. (285 aa) |
| | lipL | Octanoyl-[GcvH]:protein N-octanoyltransferase; Catalyzes the amidotransfer (transamidation) of the octanoyl moiety from octanoyl-GcvH to the lipoyl domain of the E2 subunit of lipoate-dependent enzymes. (281 aa) |
| | pta | Phosphotransacetylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (323 aa) |
| | rocA | Delta-1-pyrroline-5 carboxylate dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (515 aa) |
| | rocG | Glutamate dehydrogenase; 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 [...] (424 aa) |
| | ywdH | Putative aldehyde dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (456 aa) |
| | ilvK | Branched-chain amino acid aminotransferase; Transaminates branched-chain amino acids and ketoglutarate. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (363 aa) |
| | aldY | Putative aldehyde dehydrogenase; May contribute to protect cells against stress due to ethanol and related compounds; Belongs to the aldehyde dehydrogenase family. (485 aa) |
| | deoC | Deoxyribose-phosphate aldolase; Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5- phosphate. (223 aa) |
| | aldX | Putative aldehyde dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; Belongs to the aldehyde dehydrogenase family. (445 aa) |
| | glxK | Glycerate kinase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (382 aa) |
| | fbp | Fructose-1,6-bisphosphatase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (641 aa) |
