STRINGSTRING
AEF20576.1 AEF20576.1 trpE trpE trpD trpD trpC trpC AEF22663.1 AEF22663.1 trpF trpF trpB trpB AEF21989.1 AEF21989.1 trpA trpA aroC aroC AEF22468.1 AEF22468.1
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
AEF20576.1TIGRFAM: Anthranilate synthase, glutamine amidotransferase domain; KEGG: pmy:Pmen_3946 anthranilate synthase component II; PFAM: Glutamine amidotransferase class-I, C-terminal. (198 aa)    
Predicted Functional Partners:
trpE
Anthranilate synthase component I; 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 concentr [...]
 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
KEGG: psb:Psyr_4579 indole-3-glycerol-phosphate synthase; PFAM: Indole-3-glycerol phosphate synthase; Belongs to the TrpC family.
  
 0.999
AEF22663.1
TIGRFAM: Para-aminobenzoate synthase, component I; KEGG: pmy:Pmen_2540 aminodeoxychorismate synthase, subunit I; PFAM: Chorismate binding, C-terminal; Anthranilate synthase component I, N-terminal.
 0.999
trpF
PFAM: N-(5'phosphoribosyl)anthranilate isomerase (PRAI); KEGG: pmy:Pmen_2716 N-(5'-phosphoribosyl)anthranilate isomerase; Belongs to the TrpF family.
  
 0.997
trpB
Tryptophan synthase beta chain; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
 
  
 0.976
AEF21989.1
Chorismate mutase; TIGRFAM: Gamma/beta/epsilon proteobacterial P-protein, chorismate mutase domain; PFAM: Prephenate dehydratase; Chorismate mutase, type II; Amino acid-binding ACT; KEGG: pmy:Pmen_1850 prephenate dehydratase; SMART: Chorismate mutase.
 
 
 0.973
trpA
Tryptophan synthase alpha chain; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family.
 
  
 0.972
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.
 
 
 0.966
AEF22468.1
PFAM: Glycosyl transferase, family 3, N-terminal; KEGG: pmy:Pmen_2381 hypothetical protein.
 
  
 0.887
Your Current Organism:
Pseudomonas fulva
NCBI taxonomy Id: 743720
Other names: P. fulva 12-X, Pseudomonas fulva 12-X, Pseudomonas fulva str. 12-X, Pseudomonas fulva strain 12-X
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.