STRINGSTRING
EIG54382.1 EIG54382.1 trpB-2 trpB-2 EIG53942.1 EIG53942.1 EIG53967.1 EIG53967.1 EIG53071.1 EIG53071.1 glyA glyA EIG52330.1 EIG52330.1 trpA trpA trpB trpB EIG55537.1 EIG55537.1 EIG55312.1 EIG55312.1 EIG55259.1 EIG55259.1 EIG55094.1 EIG55094.1 EIG55089.1 EIG55089.1 EIG54865.1 EIG54865.1 EIG54492.1 EIG54492.1 EIG54488.1 EIG54488.1 EIG54471.1 EIG54471.1 EIG53188.1 EIG53188.1 EIG53189.1 EIG53189.1 dsdA dsdA EIG53344.1 EIG53344.1 EIG53544.1 EIG53544.1 gpmA gpmA gcvH gcvH gcvPA gcvPA EIG54146.1 EIG54146.1 EIG54147.1 EIG54147.1 asd asd EIG54338.1 EIG54338.1 gpmI gpmI EIG53106.1 EIG53106.1
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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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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
Your Input:
EIG54382.1Threonine dehydratase, medium form; 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. (399 aa)
trpB-2Pyridoxal-phosphate dependent TrpB-like enzyme; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (447 aa)
EIG53942.1Threonine synthase; PFAM: Pyridoxal-phosphate dependent enzyme; TIGRFAM: threonine synthase. (483 aa)
EIG53967.1Putative glycerate kinase; PFAM: MOFRL family. (452 aa)
EIG53071.1Glycine cleavage system T protein; PFAM: Aminomethyltransferase folate-binding domain; Glycine cleavage T-protein C-terminal barrel domain. (362 aa)
glyAGlycine/serine 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. (412 aa)
EIG52330.1Fructose-2,6-bisphosphatase; PFAM: Phosphoglycerate mutase family. (205 aa)
trpATryptophan synthase, alpha subunit; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. (256 aa)
trpBTryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (396 aa)
EIG55537.1Hypothetical protein; PFAM: DGC domain. (127 aa)
EIG55312.1Putative deacylase; PFAM: Succinylglutamate desuccinylase / Aspartoacylase family. (463 aa)
EIG55259.1Xaa-Pro aminopeptidase; PFAM: Metallopeptidase family M24; Creatinase/Prolidase N-terminal domain. (360 aa)
EIG55094.1Phosphoserine phosphatase SerB; PFAM: ACT domain; haloacid dehalogenase-like hydrolase; TIGRFAM: Haloacid Dehalogenase superfamily, subfamily IB, phosphoserine phosphatase-like; phosphoserine phosphatase SerB. (406 aa)
EIG55089.1Serine-pyruvate aminotransferase/archaeal aspartate aminotransferase; PFAM: Aminotransferase class-V; TIGRFAM: phosphoserine aminotransferase, putative. (377 aa)
EIG54865.1Cysteine synthase; PFAM: tRNA synthetases class I (C) catalytic domain; Pyridoxal-phosphate dependent enzyme; TIGRFAM: cysteine synthases; cysteine synthase B. (767 aa)
EIG54492.1Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain. (483 aa)
EIG54488.1Fructose-2,6-bisphosphatase; PFAM: Phosphoglycerate mutase family. (201 aa)
EIG54471.1Fructose-2,6-bisphosphatase; PFAM: 6-phosphofructo-2-kinase; Phosphoglycerate mutase family. (405 aa)
EIG53188.1PFAM: Homoserine dehydrogenase, NAD binding domain; Homoserine dehydrogenase; ACT domain. (433 aa)
EIG53189.1PFAM: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Metalloenzyme superfamily; manually curated. (392 aa)
dsdAD-serine ammonia-lyase; PFAM: Pyridoxal-phosphate dependent enzyme; Belongs to the serine/threonine dehydratase family. DsdA subfamily. (444 aa)
EIG53344.1Aspartate kinase, monofunctional class; PFAM: ACT domain; Amino acid kinase family; Belongs to the aspartokinase family. (411 aa)
EIG53544.1Xaa-Pro aminopeptidase; PFAM: Metallopeptidase family M24; Creatinase/Prolidase N-terminal domain. (406 aa)
gpmAPhosphoglycerate mutase, BPG-dependent, family 1; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily. (249 aa)
gcvHGlycine cleavage system H protein; The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein. (124 aa)
gcvPAGlycine cleavage system protein P; The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein. (443 aa)
EIG54146.1PFAM: Glycine cleavage system P-protein; overlaps another CDS with the same product name. (482 aa)
EIG54147.1Pyruvate/2-oxoglutarate dehydrogenase complex, dihydrolipoamide dehydrogenase component; PFAM: Pyridine nucleotide-disulphide oxidoreductase; Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. (461 aa)
asdAspartate-semialdehyde dehydrogenase; Catalyzes the NADPH-dependent formation of L-aspartate- semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl- 4-phosphate; Belongs to the aspartate-semialdehyde dehydrogenase family. (343 aa)
EIG54338.1PFAM: CDP-alcohol phosphatidyltransferase; TIGRFAM: CDP-diacylglycerol--serine O-phosphatidyltransferase; Belongs to the CDP-alcohol phosphatidyltransferase class-I family. (257 aa)
gpmI2,3-bisphosphoglycerate-independent phosphoglycerate mutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (514 aa)
EIG53106.1L-serine dehydratase, iron-sulfur-dependent, single chain form; PFAM: Serine dehydratase alpha chain; Serine dehydratase beta chain; Belongs to the iron-sulfur dependent L-serine dehydratase family. (458 aa)
Your Current Organism:
Desulfovibrio sp. U5L
NCBI taxonomy Id: 596152
Other names: D. sp. U5L
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