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
AKH89305.1Anthranilate synthase subunit II; Derived by automated computational analysis using gene prediction method: Protein Homology. (210 aa)    
Predicted Functional Partners:
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.
 
 0.999
AKH89304.1
With component II, the glutamine amidotransferase, catalyzes the formation of anthranilate from chorismate and glutamine; 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
trpC
Indole-3-glycerol phosphate synthase; Monomeric bifunctional protein; functions in tryptophan biosynthesis pathway; phosphoribosylanthranilate is rearranged to carboxyphenylaminodeoxyribulosephosphate which is then closed to form indole-3-glycerol phosphate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TrpC family.
  
 0.999
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.
  
 0.999
trpB
Tryptophan synthase subunit beta; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
  
 0.998
hisI
phosphoribosyl-ATP pyrophosphatase; Catalyzes the formation of 1-(5-phosphoribosyl)-AMP from 1-(5-phosphoribosyl)-ATP and the subsequent formation of 1-(5-phosphoribosyl)-5-((5- phosphoribosylamino)methylideneamino)imidazole-4- carboxamide from 1-(5-phosphoribosyl)-AMP in histidine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; In the N-terminal section; belongs to the PRA-CH family.
  
  
 0.920
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.
  
 0.899
pheA
Chorismate mutase; Catalyzing the formation of prephenate from chorismate and the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.895
tyrA
Chorismate mutase; Catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.879
Your Current Organism:
Edwardsiella tarda
NCBI taxonomy Id: 636
Other names: ATCC 15947, ATCC 23656, CIP 78.61, DSM 30052, E. tarda, Edwardsiella anguillimortifera, Edwardsiella sp. HMK1, Edwardsiella sp. PB46, LMG 2793, LMG:2793, NBRC 105688, NCCB 73021, NCTC 10396, Paracolobactrum anguillimortiferum
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