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prs prs cysK cysK cysE cysE ycdF ycdF hxlB hxlB hxlA hxlA gdh gdh acoC acoC acoL acoL katA katA citA citA serC serC yhfS yhfS yjgC yjgC pgl pgl pdhA pdhA pdhB pdhB pdhC pdhC pdhD pdhD pycA pycA rpe rpe sdaAB sdaAB sdaAA sdaAA sucC sucC sucD sucD tkt tkt citB citB yngHA yngHA yoaD yoaD odhB odhB odhA odhA ilvA ilvA kdgA kdgA kdgK kdgK serA serA mleA mleA zwf zwf gndA gndA yqjD yqjD yqjC yqjC lpdV lpdV mmgD mmgD mmgB mmgB mmgA mmgA folD folD accC accC accB accB gcvPB gcvPB gcvPA gcvPA gcvT gcvT glcK glcK yqeC yqeC adhB adhB yrhE yrhE sdhB sdhB sdhA sdhA sdhC sdhC gapB gapB mdh mdh icd icd citZ citZ pyk pyk pfkA pfkA accA accA accD accD ytsJ ytsJ ackA ackA ytcI ytcI acsA acsA malS malS ytkP ytkP pckA pckA pgi pgi gcvH gcvH fadN fadN fumC fumC eno eno pgm pgm tpiA tpiA pgk pgk gapA gapA yvkC yvkC glyA glyA ywlF ywlF maeA maeA ywjI ywjI ywjH ywjH fbaA fbaA pta pta katX katX katE katE mmsA mmsA gntK gntK gntZ gntZ yycR yycR
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proteins of unknown 3D structure
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prsPhosphoribosylpyrophosphate 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)
cysKCysteine synthase; Catalyzes the conversion of O-acetylserine to cysteine. Also acts as a sensor of cysteine availability in the signal transduction pathway modulating CymR activity. When cysteine is present, the pool of O-acetylserine (OAS) is low, which leads to the formation of a CymR- CysK complex and transcriptional repression of the CymR regulon occurs. In the absence of cysteine, the OAS pool is high and the CymR-CysK complex is mostly dissociated, leading to a faster dissociation of CymR from its DNA targets and the lifting of CymR-dependent repression. (308 aa)
cysESerine acetyltransferase; Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS). (217 aa)
ycdFPutative glucose 1-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 short-chain dehydrogenases/reductases (SDR) family. (258 aa)
hxlB6-phospho-3-hexuloisomerase (PHI); Catalyzes the isomerization between 3-hexulose 6-phosphate and fructose 6-phosphate. Together with HxlA, may act as a formaldehyde detoxification system. (185 aa)
hxlA3-hexulose-6-phosphate synthase (HPS); Catalyzes the condensation of ribulose 5-phosphate with formaldehyde to form 3-hexulose 6-phosphate. Together with HxlB, may act as a formaldehyde detoxification system; Belongs to the HPS/KGPDC family. HPS subfamily. (210 aa)
gdhGlucose 1-dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (261 aa)
acoCAcetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (398 aa)
acoLAcetoin 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)
katAVegetative catalase 1; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. (483 aa)
citACitrate 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)
serCPhosphoserine 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)
yhfSPutative acetyl-CoA C-acetyltransferase; May be involved in fatty acid metabolism; Belongs to the thiolase-like superfamily. Thiolase family. (364 aa)
yjgCPutative formate dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (985 aa)
pgl6-phosphogluconolactonase; Catalyzes the hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate. (349 aa)
pdhAPyruvate 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)
pdhBPyruvate 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)
pdhCPyruvate 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)
pdhDDihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (470 aa)
pycAPyruvate 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)
rpeRibulose-5-phosphate 3-epimerase; Catalyzes the reversible epimerization of D-ribulose 5- phosphate to D-xylulose 5-phosphate; Belongs to the ribulose-phosphate 3-epimerase family. (217 aa)
sdaABL-serine dehydratase (beta chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (220 aa)
sdaAAL-serine dehydratase (alpha chain); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the iron-sulfur dependent L-serine dehydratase family. (300 aa)
sucCsuccinyl-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)
sucDsuccinyl-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)
tktTransketolase; 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)
citBAconitate 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)
yngHABiotin carboxylase/methylcrotonoyl-CoA carboxylase subunit; 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. (444 aa)
yoaDPutative 2-hydroxyacid dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (344 aa)
odhB2-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)
odhA2-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)
ilvAThreonine 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)
kdgA2-keto-3-deoxygluconate-6-phosphate aldolase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme. (196 aa)
kdgK2-keto-3-deoxygluconate kinase; Catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). Belongs to the carbohydrate kinase PfkB family. (324 aa)
serA3-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)
mleANAD-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (439 aa)
zwfGlucose-6-phosphate 1-dehydrogenase; Catalyzes the oxidation of glucose 6-phosphate to 6- phosphogluconolactone. (489 aa)
gndANADP+-dependent 6-P-gluconate dehydrogenase; Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH. Is the predominant 6-P-gluconate dehydrogenase isoenzyme in B.subtilis during growth on glucose and gluconate. (469 aa)
yqjDPutative propionyl-CoA carboxylase beta chain; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (507 aa)
yqjCPutative methylmalonyl-CoA epimerase; 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 methylmalonyl-CoA epimerase family. (140 aa)
lpdVBranched-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)
mmgD2-methylcitrate synthase/citrate synthase III; Involved in both the tricarboxylic acid (TCA) and methylcitric acid cycles. Has both 2-methylcitrate synthase and citrate synthase activities. Catalyzes the condensation of propionyl-CoA and oxaloacetate to yield 2-methylcitrate (2-MC) and CoA, and the condensation of acetyl-CoA and oxaloacetate to yield citrate and CoA. Has 2.3-fold higher activity as a 2-methylcitrate synthase. Catalyzes the formation of either (2S,3R)- or (2R,3S)-2-methylcitrate. (372 aa)
mmgB3-hydroxybutyryl-CoA dehydrogenase; Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; Product type e: enzyme; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (287 aa)
mmgADegradative acetoacetyl-CoA thiolase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the thiolase-like superfamily. Thiolase family. (393 aa)
folDMethylenetetrahydrofolate dehydrogenase; Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10- methenyltetrahydrofolate to 10-formyltetrahydrofolate. (283 aa)
accCacetyl-CoA carboxylase subunit (biotin carboxylase subunit); 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. (450 aa)
accBacetyl-CoA carboxylase subunit (biotin carboxyl carrier subunit); 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 (By similarity). Binds biotin. (159 aa)
gcvPBGlycine 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)
gcvPAGlycine 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)
gcvTAminomethyltransferase (glycine cleavage system protein T); The glycine cleavage system catalyzes the degradation of glycine. (362 aa)
glcKGlucose kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the ROK (NagC/XylR) family. (321 aa)
yqeCPutative hydroxyacid dehydrogenase; May act as NAD-dependent 6-P-gluconate dehydrogenase. (297 aa)
adhBPutative 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)
yrhEPutative formate dehydrogenase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme; In the C-terminal section; belongs to the prokaryotic molybdopterin-containing oxidoreductase family. (980 aa)
sdhBSuccinate 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)
sdhASuccinate dehydrogenase (flavoprotein subunit); Evidence 2a: Function of homologous gene experimentally demonstrated in an other organism; enzyme. (586 aa)
sdhCSuccinate dehydrogenase (cytochrome b558 subunit); Di-heme cytochrome of the succinate dehydrogenase complex. (202 aa)
gapBGlyceraldehyde-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)
mdhMalate dehydrogenase; Catalyzes the reversible oxidation of malate to oxaloacetate. (312 aa)
icdIsocitrate dehydrogenase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (423 aa)
citZCitrate 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)
pykPyruvate 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)
pfkA6-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)
accAacetyl-CoA carboxylase (carboxyltransferase alpha subunit); 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. Belongs to the AccA family. (325 aa)
accDacetyl-CoA carboxylase (carboxyltransferase beta subunit); 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. (290 aa)
ytsJNADP-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (410 aa)
ackAAcetate 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)
ytcIPutative 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)
acsAacetyl-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)
malSNAD-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (566 aa)
ytkPPutative cysteine synthase-like protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (311 aa)
pckAPhosphoenolpyruvate 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)
pgiGlucose-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)
gcvHGlycine 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)
fadNenoyl-CoA hydratase / 3-hydroxyacyl-CoA dehydrogenase; Involved in the degradation of long-chain fatty acids; Belongs to the 3-hydroxyacyl-CoA dehydrogenase family. (789 aa)
fumCFumarate 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)
enoEnolase; 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)
pgmPhosphoglycerate mutase; Essential for rapid growth and for sporulation. Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate. (511 aa)
tpiATriose 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)
pgkPhosphoglycerate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the phosphoglycerate kinase family. (394 aa)
gapAGlyceraldehyde-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)
yvkCPutative 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)
glyASerine hydroxymethyltransferase; 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); Belongs to the SHMT family. (415 aa)
ywlFRibose 5-phosphate epimerase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (149 aa)
maeANAD-dependent malic enzyme (conversion of malate into pyruvate); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (582 aa)
ywjIPutative 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)
ywjHPutative transaldolase; Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway. Does not show fructose-6-P aldolase activity. (212 aa)
fbaAFructose-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)
ptaPhosphotransacetylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (323 aa)
katXMajor catalase in spores; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide; Belongs to the catalase family. (547 aa)
katECatalase 2; Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide. Involved in sporulation. (686 aa)
mmsAMethylmalonate-semialdehyde dehydrogenase; Catalyzes the oxidation of malonate semialdehyde (MSA) and methylmalonate semialdehyde (MMSA) into acetyl-CoA and propanoyl-CoA, respectively. (487 aa)
gntKGluconate kinase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (513 aa)
gntZNAD+-6-phosphogluconate dehydrogenase; Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NAD to NADH. Does not contribute to oxidative pentose phosphate (PP) pathway fluxes during growth on glucose. The functional role of GntZ remains obscure. (468 aa)
yycRPutative 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 zinc-containing alcohol dehydrogenase family. (408 aa)
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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