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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
trpATryptophan synthase alpha chain, putative; The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. Belongs to the TrpA family. (259 aa)    
Predicted Functional Partners:
trpB2
Tryptophan synthase beta chain, putative; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
 0.999
trpC
Indole-3-glycerol phosphate synthase, putative; GC: 44.01%; Codon Adaptation Index (CAI): 0.77. Curator(s): P. Xu; Protein involved in tryptophan metabolism; Belongs to the TrpC family.
 
 
 0.999
trpB
Tryptophan synthase beta chain, putative; The beta subunit is responsible for the synthesis of L- tryptophan from indole and L-serine.
 0.999
trpF
N-(5'-phosphoribosyl)anthranilate isomerase, putative; GC: 48.9%; Codon Adaptation Index (CAI): 0.762. Curator(s): P. Xu; Protein involved in isomerase activity; Belongs to the TrpF family.
 
  
 0.997
trpD
Anthranilate phosphoribosyltransferase, putative; Catalyzes the transfer of the phosphoribosyl group of 5- phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield N-(5'- phosphoribosyl)-anthranilate (PRA).
 
  
 0.992
trpE
Anthranilate synthase component I, putative; 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 hig [...]
 
  
 0.990
trpG
Anthranilate synthase component II, putative; GC: 45.21%; Codon Adaptation Index (CAI): 0.783. Curator(s): P. Xu; Protein involved in folic acid biosynthesis.
 
  
 0.989
glyA
Serine hydroxymethyltransferase, putative; Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism.
 
   
 0.977
sdaA
L-serine dehydratase alpha subunit; GC: 45.7%; Codon Adaptation Index (CAI): 0.81; Protein involved in gluconeogenesis; Belongs to the iron-sulfur dependent L-serine dehydratase family.
   
 
 0.952
sdaB
L-serine dehydratase beta subunit; GC: 41.96%; Codon Adaptation Index (CAI): 0.788; Protein involved in amino acid binding; Belongs to the iron-sulfur dependent L-serine dehydratase family.
   
 
 0.949
Your Current Organism:
Streptococcus sanguinis SK36
NCBI taxonomy Id: 388919
Other names: S. sanguinis SK36, Streptococcus sanguinis str. SK36, Streptococcus sanguinis strain SK36
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.