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yoaB yoaB adhE adhE dadX dadX pyrD pyrD aspC aspC ybcF ybcF yahI yahI carB carB ridA ridA alr alr ilvA ilvA argI argI tnaA tnaA argR argR tdcB tdcB tdcF tdcF yqeA yqeA glyA glyA cdd cdd dcyD dcyD
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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experimentally determined
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gene neighborhood
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gene co-occurrence
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yoaBPutative reactive intermediate deaminase; Belongs to the RutC family. (114 aa)
adhEAcetaldehyde dehydrogenase [acetylating]; This enzyme has three activities: ADH, ACDH, and PFL- deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction; In the N-terminal section; belongs to the aldehyde dehydrogenase family. (891 aa)
dadXAlanine racemase, catabolic, PLP-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. (356 aa)
pyrDDihydro-orotate oxidase, FMN-linked; Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. (336 aa)
aspCAspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. (396 aa)
ybcFPutative carbamate kinase; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process. (297 aa)
yahICarbamate kinase-like protein; Putative kinase; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the carbamate kinase family. (316 aa)
carBCarbamoyl-phosphate synthase large subunit; Protein involved in arginine biosynthetic process and pyrimidine nucleotide biosynthetic process; Belongs to the CarB family. (1073 aa)
ridAEnamine/imine deaminase, reaction intermediate detoxification; Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity); Belongs to the RutC family. (128 aa)
alrAlanine racemase, biosynthetic, PLP-binding; Catalyzes the interconversion of L-alanine and D-alanine. Provides the D-alanine required for cell wall biosynthesis. (359 aa)
ilvAL-threonine dehydratase, biosynthetic; 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. (514 aa)
argIOrnithine carbamoyltransferase 1; Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. (334 aa)
tnaAtryptophanase/L-cysteine desulfhydrase, PLP-dependent; Tryptophanase; Protein involved in cellular amino acid catabolic process; Belongs to the beta-eliminating lyase family. (471 aa)
argRL-arginine-responsive arginine metabolism regulon transcriptional regulator; Negatively controls the expression of the four operons of arginine biosynthesis in addition to the carAB operon. Predominantly interacts with A/T residues in ARG boxes. It also binds to a specific site in cer locus. Thus it is essential for cer-mediated site-specific recombination in ColE1. It is necessary for monomerization of the plasmid ColE1; Belongs to the ArgR family. (156 aa)
tdcBL-threonine dehydratase, catabolic; 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. TdcB also dehydrates serine t [...] (329 aa)
tdcFPutative reactive intermediate deaminase; May be a post-translational regulator that controls the metabolic fate of L-threonine or the potentially toxic intermediate 2- ketobutyrate. (129 aa)
yqeAPutative kinase; Belongs to the carbamate kinase family. (310 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. Thus, is able to catalyze the cleavage of allothreonine and 3-phenylserine. Also catalyzes the irreversible conversion of 5,10-m [...] (417 aa)
cddCytidine/deoxycytidine deaminase; This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. (294 aa)
dcyDD-cysteine desulfhydrase, PLP-dependent; Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D- alanine. (328 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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