STRINGSTRING
serA serA thrB thrB hom hom glyA glyA serC serC gpmA gpmA ALE19627.1 ALE19627.1 ALE18872.1 ALE18872.1 trpB trpB trpA trpA ask ask asd asd ALE19248.1 ALE19248.1 serB2 serB2 ilvA ilvA
Nodes:
Network nodes represent proteins
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
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
serA3-phosphoglycerate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family. (531 aa)
thrBSerine kinase; Catalyzes the ATP-dependent phosphorylation of L-homoserine to L-homoserine phosphate; Belongs to the GHMP kinase family. Homoserine kinase subfamily. (301 aa)
homHomoserine dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (453 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. (436 aa)
serCPhosphoserine aminotransferase; Catalyzes the reversible conversion of 3- phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4- phosphonooxybutanoate to phosphohydroxythreonine; Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily. (373 aa)
gpmAPhosphoglyceromutase; Catalyzes the interconversion of 2-phosphoglycerate and 3- phosphoglycerate. (254 aa)
ALE19627.1Dihydrolipoyl dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (492 aa)
ALE18872.1Threonine synthase; Catalyzes the formation of L-threonine from O-phospho-L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology. (488 aa)
trpBPhosphoribosylanthranilate isomerase; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (376 aa)
trpATryptophan synthase subunit alpha; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. (259 aa)
askAspartate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the aspartokinase family. (421 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. (350 aa)
ALE19248.1Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (439 aa)
serB2Phosphoserine phosphatase; Derived by automated computational analysis using gene prediction method: Protein Homology. (401 aa)
ilvAThreonine dehydratase; 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. (428 aa)
Your Current Organism:
Lawsonella clevelandensis
NCBI taxonomy Id: 1528099
Other names: CCUG 66657, Corynebacteriales bacterium CCF1, Corynebacteriales bacterium CCF2, Corynebacteriales bacterium X1036, Corynebacteriales bacterium X1698, Corynebacterineae bacterium NML 120705, Corynebacterineae bacterium X1698, DSM 45743, L. clevelandensis, Lawsonella clevelandensis Bell et al. 2016, bacterium CCF-01, strain X1036
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