STRINGSTRING
STRING protein interaction network
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.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
trpEAnthranilate synthase; Part of a heterotetrameric complex that catalyzes the two- step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia. (515 aa)    
Predicted Functional Partners:
AMA50800.1
Anthranilate synthase; TrpG; with TrpE catalyzes the formation of anthranilate and glutamate from chorismate and glutamine; TrpG provides the glutamine amidotransferase activity; Derived by automated computational analysis using gene prediction method: Protein Homology.
 0.999
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).
 
 0.999
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
 
  
 0.998
trpC
Indole-3-glycerol phosphate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpC family.
 0.998
trpA
Tryptophan 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.
 
  
 0.997
aroC
Chorismate synthase; Catalyzes the anti-1,4-elimination of the C-3 phosphate and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate (EPSP) to yield chorismate, which is the branch point compound that serves as the starting substrate for the three terminal pathways of aromatic amino acid biosynthesis. This reaction introduces a second double bond into the aromatic ring system.
 
 
 0.996
trpF
N-(5'-phosphoribosyl)anthranilate isomerase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpF family.
 
 
 0.995
aroH
Chorismate mutase; Catalyzes the Claisen rearrangement of chorismate to prephenate. Probably involved in the aromatic amino acid biosynthesis.
    
 0.986
AMA53498.1
Chorismate mutase; Catalyzes the formation of 3-deoxy-D-aribino-hept-2-ulosonate 7-phosphate from phosphoenolpyruvate and D-erythrose 4-phosphate and the formation of prephenate from chorismate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.985
thrR
ACT domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0735 family.
     
 0.970
Your Current Organism:
Bacillus subtilis inaquosorum
NCBI taxonomy Id: 483913
Other names: B. subtilis subsp. inaquosorum, BGSC 3A28, Bacillus subtilis subsp. inaquosorum, Bacillus subtilis subsp. inaquosorum Rooney et al. 2009, DSM 22148, KCTC 13429, NRRL B-23052
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