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| | gcaD | Bifunctional glucosamine-1-phosphate N-acetyltransferase/UDP-N-acetylglucosamine pyrophosphorylase; 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. In the C-terminal section; belon [...] (456 aa) |
| | cysE | Serine acetyltransferase; Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS). (217 aa) |
| | ybbJ | Putative acyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (160 aa) |
| | ybfA | Conserved hypothetical protein; Putative DNA-binding acetyltransferase. (305 aa) |
| | ydaF | Putative ribosomal protein N-acetyltransferase; Putative N-acetyltransferase. May act on ribosomal proteins (Potential); Belongs to the acetyltransferase family. (183 aa) |
| | ydfB | Conserved hypothetical protein; Evidence 7: Gene remnant; Belongs to the acetyltransferase family. (261 aa) |
| | ydgE | Putative N-acetyltransferase; 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 acetyltransferase family. (157 aa) |
| | ydhI | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (160 aa) |
| | rimI | Ribosomal protein S18 alanine N-acetyltransferase; Acetylates the N-terminal alanine of ribosomal protein S18. (151 aa) |
| | tsaD | tRNA(NNU) t(6)A37 threonylcarbamoyladenosine modification; Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaE and TsaB; this reaction does not require ATP in vitro. TsaD likely plays a direct catalytic role in this reaction. Belongs to the KAE1 / TsaD family. (346 aa) |
| | yesJ | Putative acetyltransferase; 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 acetyltransferase family. (180 aa) |
| | yfmK | Putative acetyltransferase; 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 acetyltransferase family. (148 aa) |
| | acoC | Acetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (398 aa) |
| | yfiQ | Putative membrane component involved in biofilm formation; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (362 aa) |
| | fabL | Enoyl-acyl carrier protein reductase III; Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). It confers resistance to triclosan. Belongs to the short-chain dehydrogenases/reductases (SDR) family. (250 aa) |
| | yhcX | Putative amidohydrolase; 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 carbon-nitrogen hydrolase superfamily. NIT1/NIT2 family. (513 aa) |
| | yhdJ | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the acetyltransferase family. (142 aa) |
| | plsC | 1-acylglycerol-phosphate (1-acyl-G3P) acyltransferase; Converts lysophosphatidic acid (LPA) into phosphatidic acid (PA) by incorporating an acyl moiety at the 2 position. This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA. Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family. (199 aa) |
| | fabHB | Beta-ketoacyl-acyl carrier protein synthase III 2; 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. (325 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) |
| | yhfO | Putative N-acetyltransferase; 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 acetyltransferase family. (149 aa) |
| | yhfS | Putative acetyl-CoA C-acetyltransferase; May be involved in fatty acid metabolism; Belongs to the thiolase-like superfamily. Thiolase family. (364 aa) |
| | yitH | Putative N-acetyltransferase; 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 acetyltransferase family. (282 aa) |
| | yitI | Putative N-acetyltransferase; 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 acetyltransferase family. (149 aa) |
| | argJ | Ornithine acetyltransferase; Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate. (406 aa) |
| | fabHA | Beta-ketoacyl-acyl carrier protein synthase III 1; 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. (312 aa) |
| | fabF | Beta-ketoacyl-acyl carrier protein synthase II; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (413 aa) |
| | yjbC | Putative thiol oxidation management factor; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (192 aa) |
| | fabI | Enoyl-acyl carrier protein reductase; 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. (258 aa) |
| | yjcF | Putative acetyltransferase; 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 acetyltransferase family. (140 aa) |
| | yjcK | Putative ribosomal-protein-alanine N-acetyltransferase; Acetylates the N-terminal alanine of ribosomal protein S5. (181 aa) |
| | yjdG | Putative acetyltransferase; 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 acetyltransferase family. (168 aa) |
| | ykkB | Putative N-acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (172 aa) |
| | ykrP | Putative integral inner membrane protein; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (340 aa) |
| | ykwB | Putative acetyltransferase; 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 acetyltransferase family. (226 aa) |
| | dapH | Tetrahydrodipicolinate N-acetyltransferase; Catalyzes the transfer of an acetyl group from acetyl-CoA to tetrahydrodipicolinate. (236 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) |
| | ykzC | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function. (142 aa) |
| | ylbP | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (160 aa) |
| | plsX | phosphate:acyl-ACP acyltransferase; 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. (333 aa) |
| | fabD | Malonyl CoA:acyl carrier protein transacylase; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the FabD family. (317 aa) |
| | fabG | Beta-ketoacyl-acyl carrier protein reductase; 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; Belongs to the short-chain dehydrogenases/reductases (SDR) family. (246 aa) |
| | kbl | 2-amino-3-ketobutyrate CoA ligase (glycine acetyl transferase); 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. (392 aa) |
| | pksC | malonyl-CoA-acyltransferase involved in polyketide synthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It catalyzes the transfer of the malonyl-CoA group to the acyl-carrier-protein AcpK (Mal-AcpK); Belongs to the FabD family. (288 aa) |
| | pksE | Enzyme involved in polyketide synthesis; Probably involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. Probably has an acyl transferase activity and could also have a flavin mononucleotide-dependent oxidoreductase activity; In the N-terminal section; belongs to the FabD family. (767 aa) |
| | pksF | Decarboxylase converting malonyl-S-AcpK to acetyl-S-AcpK for polyketide synthesis; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. It decarboxylates selectively the malonyl group attached on the acyl-carrier-protein AcpK (Mal-AcpK); Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP synthases family. (415 aa) |
| | pksJ | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (5043 aa) |
| | pksL | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (4538 aa) |
| | pksM | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (4262 aa) |
| | pksN | Polyketide synthase of type I; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (5488 aa) |
| | pksR | Polyketide synthase; Involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is involved in secondary metabolism. (2543 aa) |
| | ynaD | Putative N-acetyltransferase; 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 acetyltransferase family. (170 aa) |
| | plsY | Acylphosphate:glycerol-3-phosphate acyltransferase; Catalyzes the transfer of an acyl group from acyl-phosphate (acyl-PO(4)) to glycerol-3-phosphate (G3P) to form lysophosphatidic acid (LPA). This enzyme utilizes acyl-phosphate as fatty acyl donor, but not acyl-CoA or acyl-ACP; Belongs to the PlsY family. (193 aa) |
| | yoaA | Putative N-acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the acetyltransferase family. (177 aa) |
| | yoaP | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; Belongs to the acetyltransferase family. (251 aa) |
| | yobR | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the acetyltransferase family. (247 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) |
| | kamB | Epsilon-amino-beta-lysine acetyl transferase; In vitro, is able to catalyze the acetylation of beta-lysine to N6-acetyl-beta-lysine, an archaeal osmolyte produced by methanogenic archaea. Its physiological function has not yet been elucidated. (275 aa) |
| | cgeE | Protein involved in maturation of the outermost layer of the spore; May be involved in maturation of the outermost layer of the spore. (259 aa) |
| | yokL | Putative acetyltransferase; 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 acetyltransferase family. (177 aa) |
| | yokD | Aminoglycoside N3'-acetyltransferase; May contribute to antibiotic resistance; Belongs to the antibiotic N-acetyltransferase family. (272 aa) |
| | metA | Putative homoserine O-acetyltransferase; Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine; Belongs to the MetA family. (301 aa) |
| | bpsA | Promiscuous alkylpyrone synthase BpsA; Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (365 aa) |
| | ypzK | Putative acetyltransferase; Involved in riboflavin biosynthesis. (124 aa) |
| | yqkA | Conserved hypothetical protein; Evidence 4: Homologs of previously reported genes of unknown function; In the C-terminal section; belongs to the UPF0157 (GrpB) family. (343 aa) |
| | yqjY | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (156 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) |
| | 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) |
| | mmgA | Degradative 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) |
| | 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) |
| | yrkN | Putative N-acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (185 aa) |
| | bltD | Spermine/spermidine acetyltransferase; Acetylates both spermidine and spermine at primary propyl amine moieties, with spermine being the preferred substrate. (152 aa) |
| | oatA | Peptidoglycan O-acetyltransferase; Evidence 1a: Function experimentally demonstrated in the studied strain; enzyme. (634 aa) |
| | ysnE | Putative indole acetic acid acetyltransferase; 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 acetyltransferase family. (151 aa) |
| | ytmI | Putative N-acetyltransferase; 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 acetyltransferase family. (178 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) |
| | acuA | Protein acetyltransferase; Part of the acuABC operon, which is possibly involved in the breakdown of acetoin and butanediol. Acts as an acetyltransferase inactivating acetyl-CoA synthetase AcsA via acetylation at a Lys residue. (210 aa) |
| | bioF | 8-amino-7-oxononanoate synthase; 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. (389 aa) |
| | yuaI | Putative acetyl-transferase; 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 acetyltransferase family. (173 aa) |
| | paiA | Polyamine N-acetyltransferase; Involved in the protection against polyamine toxicity by regulating their concentration. Also could be involved in the negative control of sporulation as well as production of degradative enzymes such as alpha-amylase, levansucrase and alkaline phosphatase. Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It possesses N1-acetyltransferase activity toward polyamine substrates including spermidine, spermine, aminopropylcadaverine, norspermidine, homospermidine [...] (172 aa) |
| | fadA | acetyl-CoA C-acyltransferase; Involved in the degradation of long-chain fatty acids; Belongs to the thiolase-like superfamily. Thiolase family. (391 aa) |
| | yvbK | Putative acyltransferase; Probable N-acetyltransferase. (155 aa) |
| | yvcN | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme; Belongs to the arylamine N-acetyltransferase family. (254 aa) |
| | fabZ | (3R)-hydroxymyristoyl-[acyl carrier protein] dehydratase; Involved in unsaturated fatty acids biosynthesis. Catalyzes the dehydration of short chain beta-hydroxyacyl-ACPs and long chain saturated and unsaturated beta-hydroxyacyl-ACPs. (141 aa) |
| | ywnH | Putative phosphinothricin acetyltransferase; This enzyme is an effector of phosphinothricin tripeptide (PTT or bialaphos) resistance. Inactivates PTT by transfer of an acetyl group (By similarity); Belongs to the acetyltransferase family. PAT/BAR subfamily. (163 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) |
| | spsD | Putative TDP-glycosamine N-acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (289 aa) |
| | yxeL | Putative acetyltransferase; Catalyzes the N-acetylation of S-(2-succino)cysteine. Is involved in a S-(2-succino)cysteine (2SC) degradation pathway that allows B.subtilis to grow on 2SC as a sole sulfur source, via its metabolization to cysteine. Moreover, 2SC is a toxic compound in B.subtilis at high exogenous concentrations, and this enzyme relieves 2SC toxicity via N-acetylation; Belongs to the acetyltransferase family. (165 aa) |
| | yxbD | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (159 aa) |
| | yycN | Putative N-acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; putative enzyme. (156 aa) |
| | yybD | Putative acetyltransferase; Could catalyze the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and release both CoA and the acetylated product. (147 aa) |
| | yyaT | Putative acetyltransferase; Evidence 3: Function proposed based on presence of conserved amino acid motif, structural feature or limited homology; Product type pe: putative enzyme. (148 aa) |
| | yyaR | Putative acetyl-transferase; Involved in resistance to streptothricin, a broad-spectrum antibiotic produced by streptomycetes. Detoxifies streptothricin via acetylation of the beta amino group of the first beta-lysyl moiety of streptothricin; Belongs to the acetyltransferase family. GNAT subfamily. (173 aa) |
| | maa | Maltose O-acetyltransferase; Catalyzes the CoA-dependent transfer of an acetyl group to maltose and other sugars. Acetylates glucose exclusively at the C6 position and maltose at the C6 position of the non-reducing end glucosyl moiety. Is able to acetylate maltooligosaccharides. (184 aa) |
