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.
Node Color
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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
trpBTryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (396 aa)    
Predicted Functional Partners:
trpA
Tryptophan 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.
 0.999
trpC
Indole-3-glycerol-phosphate synthase., Phosphoribosylanthranilate isomerase; PFAM: Indole-3-glycerol phosphate synthase; N-(5'phosphoribosyl)anthranilate isomerase (PRAI); KEGG: eca:ECA2299 bifunctional indole-3-glycerol phosphate synthase/phosphoribosylanthranilate isomerase; Belongs to the TrpC family.
 
 0.999
PC1_2006
TIGRFAM: glutamine amidotransferase of anthranilate synthase; PFAM: glutamine amidotransferase class-I; KEGG: eca:ECA2297 anthranilate synthase component II.
 
  
 0.998
trpD
Anthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA).
 
  
 0.992
PC1_2007
KEGG: eca:ECA2296 anthranilate synthase component I; TIGRFAM: anthranilate synthase component I; PFAM: Chorismate binding-like; Anthranilate synthase component I domain protein.
 
  
 0.982
ilvA
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.
  
 0.931
PC1_1930
TIGRFAM: para-aminobenzoate synthase, subunit I; PFAM: Chorismate binding-like; Anthranilate synthase component I domain protein; KEGG: eca:ECA2378 para-aminobenzoate synthase component I.
 
  
 0.929
PC1_3855
TIGRFAM: glutamine amidotransferase of anthranilate synthase; PFAM: glutamine amidotransferase class-I; KEGG: eca:ECA4066 para-aminobenzoate synthase component II.
 
  
 0.928
PC1_0450
KEGG: eca:ECA0465 phosphoserine phosphatase; TIGRFAM: phosphoserine phosphatase SerB; HAD-superfamily hydrolase, subfamily IB (PSPase-like); PFAM: Haloacid dehalogenase domain protein hydrolase; Haloacid dehalogenase domain protein hydrolase type 3.
  
 
 0.917
glyA
Glycine 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.
     
 0.912
Your Current Organism:
Pectobacterium carotovorum
NCBI taxonomy Id: 561230
Other names: P. carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum PC1, Pectobacterium carotovorum subsp. carotovorum str. PC1, Pectobacterium carotovorum subsp. carotovorum strain PC1
Server load: low (12%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.