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
KUN48973.1Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family. (561 aa)    
Predicted Functional Partners:
ilvH
Acetolactate synthase small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.998
ilvC1
Ketol-acid reductoisomerase; Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.
 
 
 0.991
frc
Formyl-coenzyme A transferase; Involved in the catabolism of oxalate and in the adapatation to low pH via the induction of the oxalate-dependent acid tolerance response (ATR). Catalyzes the transfer of the CoA moiety from formyl- CoA to oxalate; Belongs to the CoA-transferase III family. Frc subfamily.
 
 
 0.965
KUN46117.1
Threonine dehydratase; Catalyzes the formation of 2-oxobutanoate from L-threonine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.965
KUN49082.1
CoA-binding protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
  0.961
leuB
3-isopropylmalate dehydrogenase; Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate. Belongs to the isocitrate and isopropylmalate dehydrogenases family. LeuB type 2 subfamily.
 
 0.958
KUN46674.1
2-oxoacid:ferredoxin oxidoreductase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.947
leuA
2-isopropylmalate synthase; Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3- hydroxy-4-methylpentanoate (2-isopropylmalate); Belongs to the alpha-IPM synthase/homocitrate synthase family. LeuA type 2 subfamily.
  
 
 0.936
cimA
Transferase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.930
KUN46673.1
2-oxoglutarate ferredoxin oxidoreductase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.923
Your Current Organism:
Streptomyces olivochromogenes
NCBI taxonomy Id: 1963
Other names: ATCC 25479, ATCC 3336, Actinomyces olivochromogenus, CBS 889.69, DSM 40451, IFO 13067, IFO 3178, IMET 40352, ISP 5451, JCM 4163, JCM 4500, KCTC 9064, NBRC 13067, NBRC 3178, NRRL-ISP 5451, S. olivochromogenes, Streptomyces olivichromogenes, Streptomyces olivochromogenus
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.