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fadD fadD birA birA bioH bioH accB accB fadH fadH ttdR ttdR aas aas ftnA ftnA fadK fadK fabI fabI acpP acpP fabG fabG fabD fabD fabH fabH fabA fabA bioD bioD bioC bioC bioF bioF bioB bioB bioA bioA lacZ lacZ fabZ fabZ
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fadDacyl-CoA synthetase (long-chain-fatty-acid--CoA ligase); Catalyzes the esterification, concomitant with transport, of exogenous long-chain fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Activity is the highest with fatty acid substrates of > 10 carbon atoms. Is involved in the aerobic beta- oxidative degradation of fatty acids, which allows aerobic growth of E.coli on fatty acids as a sole carbon and energy source. (561 aa)
birABifunctional ligase/repressor BirA; Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon. (321 aa)
bioHpimeloyl-ACP methyl ester carboxylesterase; The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain [...] (256 aa)
accBBiotin carboxyl carrier protein of acetyl-CoA carboxylase; 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. (156 aa)
fadH2,4-dienoyl-CoA reductase, NADH and FMN-linked; Functions as an auxiliary enzyme in the beta-oxidation of unsaturated fatty acids with double bonds at even carbon positions. Catalyzes the NADPH-dependent reduction of the C4-C5 double bond of the acyl chain of 2,4-dienoyl-CoA to yield 2-trans-enoyl-CoA. Acts on both isomers, 2-trans,4- cis- and 2-trans,4-trans-decadienoyl-CoA, with almost equal efficiency. Is not active with NADH instead of NADPH. Does not show cis->trans isomerase activity. (672 aa)
ttdRTranscriptional activator of ttdABT; Positive regulator required for L-tartrate-dependent anaerobic growth on glycerol. Induces expression of the ttdA-ttdB-ygjE operon. (310 aa)
aasFused 2-acylglycerophospho-ethanolamine acyl transferase/acyl-acyl carrier protein synthetase; Plays a role in lysophospholipid acylation. Transfers fatty acids to the 1-position via an enzyme-bound acyl-ACP intermediate in the presence of ATP and magnesium. Its physiological function is to regenerate phosphatidylethanolamine from 2-acyl-glycero-3- phosphoethanolamine (2-acyl-GPE) formed by transacylation reactions or degradation by phospholipase A1. (719 aa)
ftnAFerritin iron storage protein (cytoplasmic); Iron-storage protein; Belongs to the ferritin family. Prokaryotic subfamily. (165 aa)
fadKShort chain acyl-CoA synthetase, anaerobic; Catalyzes the esterification, concomitant with transport, of exogenous fatty acids into metabolically active CoA thioesters for subsequent degradation or incorporation into phospholipids. Is maximally active on C6:0, C8:0 and C12:0 fatty acids, while has a low activity on C14-C18 chain length fatty acids. Is involved in the anaerobic beta-oxidative degradation of fatty acids, which allows anaerobic growth of E.coli on fatty acids as a sole carbon and energy source in the presence of nitrate or fumarate as a terminal electron acceptor. Can fun [...] (548 aa)
fabIEnoyl-[acyl-carrier-protein] reductase, NADH-dependent; Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism and in the biotin biosynthesis. (262 aa)
acpPAcyl carrier protein (ACP); Carrier of the growing fatty acid chain in fatty acid biosynthesis; Belongs to the acyl carrier protein (ACP) family. (78 aa)
fabG3-oxoacyl-[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. (244 aa)
fabDmalonyl-CoA-[acyl-carrier-protein] transacylase; Belongs to the FabD family. (309 aa)
fabH3-oxoacyl-[acyl-carrier-protein] synthase III; Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain; Belongs to the t [...] (317 aa)
fabABeta-hydroxydecanoyl thioester dehydrase; Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E- (2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length. Is inactive in the dehydration of long chain unsaturated beta-hydroxyacyl-ACP. (172 aa)
bioDDethiobiotin synthetase; Catalyzes a mechanistically unusual reaction, the ATP- dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8- diaminopelargonic acid (DAPA) to form an ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminopelargonic acid; Belongs to the dethiobiotin synthetase family. (225 aa)
bioCmalonyl-ACP O-methyltransferase, SAM-dependent; Converts the free carboxyl group of a malonyl-thioester to its methyl ester by transfer of a methyl group from S-adenosyl-L- methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. (251 aa)
bioF8-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. Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate, but it is believed that pimeloyl- ACP rather than pimeloyl-CoA is the physiological substrate of BioF. Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family. BioF subfamily. (384 aa)
bioBBiotin synthase; Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. (346 aa)
bioA7,8-diaminopelargonic acid synthase, PLP-dependent; Catalyzes the transfer of the alpha-amino group from S- adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only animotransferase known to utilize SAM as an amino donor; Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. BioA subfamily. (429 aa)
lacZbeta-D-galactosidase; Protein involved in carbohydrate catabolic process; Belongs to the glycosyl hydrolase 2 family. (1024 aa)
fabZ(3R)-hydroxymyristol 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. (151 aa)
Your Current Organism:
Escherichia coli K12
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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