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
KOH23799.1Dihydroxy-acid dehydratase; Catalyzes the dehydration of 2,3-dihydroxy-3-methylbutanoate to 3-methyl-2-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family. (613 aa)    
Predicted Functional Partners:
KOH23800.1
Branched-chain amino acid aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.997
KOH19265.1
Ketol-acid reductoisomerase; Catalyzes the formation of (R)-2,3-dihydroxy-3-methylbutanoate from (S)-2-hydroxy-2-methyl-3-oxobutanoate in valine and isoleucine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the ketol-acid reductoisomerase family.
 
 
 0.990
ilvA
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.
  
 0.988
KOH19523.1
2-isopropylmalate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the alpha-IPM synthase/homocitrate synthase family.
 
 
 0.983
KOH23802.1
Acetolactate synthase catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate; also known as acetolactate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.982
KOH23801.1
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.964
KOH19521.1
Isopropylmalate isomerase; Dehydratase component, catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.948
KOH19522.1
3-isopropylmalate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.947
leuD
Isopropylmalate isomerase; Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate in leucine biosynthesis; forms a heterodimer of LeuC/D; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.937
KOH19527.1
Acetolactate synthase 3 catalytic subunit; Catalyzes the formation of 2-acetolactate from pyruvate, leucine sensitive; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.936
Your Current Organism:
Vibrio parahaemolyticus
NCBI taxonomy Id: 670
Other names: ATCC 17802, Beneckea parahaemolytica, CAIM 320, CCUG 14474, CCUG 15657, CCUG 4224, CIP 75.2, DSM 10027, IFO 12711, LMG 2850, LMG:2850, NBRC 12711, NCCB 77010, NCCB 77018, NCTC 10903, NRRL B-4167, Oceanomonas parahaemolytica, Pasteurella parahaemolytica, V. parahaemolyticus
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