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glyA glyA patA patA tdh tdh glnA glnA alr alr tyrB tyrB aspA aspA dadX dadX dadA dadA ghrA ghrA putA putA aspC aspC gltA gltA ybdL ybdL gdhA gdhA alaA alaA alaC alaC
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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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colored nodes:
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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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
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Your Input:
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)
patAPutrescine:2-oxoglutaric acid aminotransferase, PLP-dependent; Catalyzes the aminotransferase reaction from putrescine to 2- oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4- aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cad [...] (459 aa)
tdhL-threonine 3-dehydrogenase, NAD(P)-binding; Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2- amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+). Belongs to the zinc-containing alcohol dehydrogenase family. (341 aa)
glnAGlutamine synthetase; Catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. (469 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)
tyrBTyrosine aminotransferase, tyrosine-repressible, PLP-dependent; Broad-specificity enzyme that catalyzes the transamination of 2-ketoisocaproate, p-hydroxyphenylpyruvate, and phenylpyruvate to yield leucine, tyrosine, and phenylalanine, respectively. In vitro, is able to catalyze the conversion of beta-methyl phenylpyruvate to the nonproteinogenic amino acid (2S,3S)-beta-methyl-phenylalanine, a building block of the antibiotic mannopeptimycin produced by Streptomyces hygroscopicus NRRL3085; Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (397 aa)
aspAAspartate ammonia-lyase (aspartase); Protein involved in cellular amino acid metabolic process, asparagine biosynthetic process and lysine biosynthetic process via diaminopimelate. (478 aa)
dadXAlanine racemase, catabolic, PLP-binding; Isomerizes L-alanine to D-alanine which is then oxidized to pyruvate by DadA. (356 aa)
dadAD-amino acid dehydrogenase; Catalyzes the oxidative deamination of D-amino acids. Has broad substrate specificity; is mostly active on D-alanine, and to a lesser extent, on several other D-amino acids such as D-methionine, D- serine and D-proline, but not on L-alanine. Participates in the utilization of L-alanine and D-alanine as the sole source of carbon, nitrogen and energy for growth. Is also able to oxidize D-amino acid analogs such as 3,4-dehydro-D-proline, D-2-aminobutyrate, D-norvaline, D-norleucine, cis-4-hydroxy-D-proline, and DL-ethionine. (432 aa)
ghrAGlyoxylate/hydroxypyruvate reductase A; Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low. (312 aa)
putADelta-1-pyrroline-5-carboxylate dehydrogenase; Oxidizes proline to glutamate for use as a carbon and nitrogen source and also function as a transcriptional repressor of the put operon; In the C-terminal section; belongs to the aldehyde dehydrogenase family. (1320 aa)
aspCAspartate aminotransferase, PLP-dependent; Aspartate aminotransferase; Protein involved in cellular amino acid catabolic process and aspartate biosynthetic process. (396 aa)
gltACitrate synthase; Protein involved in tricarboxylic acid cycle and anaerobic respiration; Belongs to the citrate synthase family. (427 aa)
ybdLMethionine aminotransferase, PLP-dependent; Shows aminotransferase activity with methionine and histidine as substrates, and to a lesser extent also with phenylalanine. Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family. (386 aa)
gdhAGlutamate dehydrogenase, NADP-specific; Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia; Belongs to the Glu/Leu/Phe/Val dehydrogenases family. (447 aa)
alaAGlutamate-pyruvate aminotransferase; Involved in the biosynthesis of alanine. (405 aa)
alaCGlutamate-pyruvate aminotransferase; Involved in the biosynthesis of alanine. (412 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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