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
trpDAnthranilate phosphoribosyltransferase; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA). (349 aa)    
Predicted Functional Partners:
trpC
Indole-3-glycerol-phosphate synthase; Involved in tryptophan biosynthesis; amino acid biosynthesis; converts 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate to C(1)-(3-indolyl)-glycerol 3-phosphate and carbon dioxide and water; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpC family.
  
 0.999
AMA44442.1
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.
  
 0.998
trpE
Anthranilate 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.
 
 0.997
trpF
N-(5'-phosphoribosyl)anthranilate isomerase; Catalyzes the formation of 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate from N-(5-phospho-beta-D-ribosyl)-anthranilate in tryptophan biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpF family.
 
 0.993
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
 
  
 0.986
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.
 
  
 0.986
pabB
Para-aminobenzoate synthase component 1; catalyzes the formation of 4-amino-4-deoxychorismate from chorismate and L-glutamine; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.964
aroA
3-phosphoshikimate 1-carboxyvinyltransferase; Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
 
   
 0.823
AMA46835.1
Prephenate dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.790
AMA44445.1
Lipoate--protein ligase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.676
Your Current Organism:
Pseudomonas monteilii
NCBI taxonomy Id: 76759
Other names: ATCC 700476, CCUG 38736, CFML 90-60, CIP 104883, DSM 14164, JCM 21585, NBRC 103158, P. monteilii, Pseudomonas sp. MKP 213, Pseudomonas sp. V7SW2
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