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galE galE thiL thiL dxs dxs thiI thiI galK galK galT galT bioA bioA bioF bioF bioC bioC bioD bioD galU galU ydiU ydiU thiD thiD thiG thiG thiF thiF thiE thiE thiC thiC
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galEUDP-galactose-4-epimerase; Involved in the metabolism of galactose. Catalyzes the conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) through a mechanism involving the transient reduction of NAD. It is only active on UDP-galactose and UDP-glucose. (338 aa)
thiLThiamine monophosphate kinase; Catalyzes the ATP-dependent phosphorylation of thiamine- monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1. Cannot use thiamine as substrate. Is highly specific for ATP as phosphate donor; Belongs to the thiamine-monophosphate kinase family. (325 aa)
dxs1-deoxyxylulose-5-phosphate synthase, thiamine triphosphate-binding, FAD-requiring; Catalyzes the acyloin condensation reaction between C atoms 2 and 3 of pyruvate and glyceraldehyde 3-phosphate to yield 1-deoxy-D- xylulose-5-phosphate (DXP). (620 aa)
thiItRNA s(4)U8 sulfurtransferase; Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS. Belongs to the ThiI family. (482 aa)
galKGalactokinase; Catalyzes the transfer of the gamma-phosphate of ATP to D- galactose to form alpha-D-galactose-1-phosphate (Gal-1-P). To a lesser extent, is also able to phosphorylate 2-deoxy-D-galactose and D- galactosamine. Is not able to use D-galacturonic acid, D-talose, L- altrose, and L-glucose as substrates. (382 aa)
galTGalactose-1-phosphate uridylyltransferase; Protein involved in cell surface antigen activity, host-interacting, galactose metabolic process, colanic acid biosynthetic process, carbohydrate catabolic process and response to desiccation; Belongs to the galactose-1-phosphate uridylyltransferase type 1 family. (348 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)
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)
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)
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)
galUGlucose-1-phosphate uridylyltransferase; May play a role in stationary phase survival; Belongs to the UDPGP type 2 family. (302 aa)
ydiUUPF0061 family protein; Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr and Tyr residues of target proteins (AMPylation). Cannot use GTP, CTP or UTP as cosubstrate. AMPylates SucA at 'Thr-405' and GrxA on 'Tyr-13'. Regulates protein S-glutathionylation levels probably by AMPylation of deglutathionylation enzymes such as GrxA. Probably involved in redox homeostasis. (478 aa)
thiDHydroxy-methylpyrimidine kinase and hydroxy-phosphomethylpyrimidine kinase; Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. Belongs to the ThiD family. (266 aa)
thiGThiamine biosynthesis ThiGH complex subunit; Catalyzes the rearrangement of 1-deoxy-D-xylulose 5-phosphate (DXP) to produce the thiazole phosphate moiety of thiamine. Sulfur is provided by the thiocarboxylate moiety of the carrier protein ThiS. In vitro, sulfur can be provided by H(2)S; Belongs to the ThiG family. (256 aa)
thiFAdenylyltransferase, modifies ThiS C-terminus; Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein ThiS; Belongs to the HesA/MoeB/ThiF family. (251 aa)
thiEThiamine phosphate synthase (thiamine phosphate pyrophosphorylase); Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). Belongs to the thiamine-phosphate synthase family. (211 aa)
thiCPhosphomethylpyrimidine synthase; Catalyzes the synthesis of the hydroxymethylpyrimidine phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent reaction. (631 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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