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
trpBTryptophan synthase, beta subunit; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine. (404 aa)    
Predicted Functional Partners:
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, putative; Belongs to the TrpC family.
 
 0.999
trpF
N-(5'phosphoribosyl)anthranilate isomerase, putative; Belongs to the TrpF family.
 
 0.999
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
ABD30461.1
Anthranilate synthase component I.
 
  
 0.990
ABD30462.1
Anthranilate synthase component II, putative.
 
 
 0.986
ilvA
Thereonine dehydratase, putative; 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 (By similarity).
   
 0.937
tdcB
Threonine dehydratase; 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 (By similarity). Belongs to the serine/thre [...]
   
 0.919
ABD29855.1
Para-aminobenzoate synthase, glutamine amidotransferase, component II, putative.
 
 
 0.917
ABD29856.1
Conserved hypothetical protein; Annotated as putative para-aminobenzoate synthase, component I containing frameshift in strain Col.
 
  
 0.914
Your Current Organism:
Staphylococcus aureus
NCBI taxonomy Id: 93061
Other names: S. aureus subsp. aureus NCTC 8325, Staphylococcus aureus NCTC 8325, Staphylococcus aureus subsp. aureus NCTC 8325, Staphylococcus aureus subsp. aureus str. NCTC 8325, Staphylococcus aureus subsp. aureus strain NCTC 8325
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