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
KOH23801.1Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (94 aa)    
Predicted Functional Partners:
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.
  
 0.984
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.
  
 
 0.982
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.
  
 
 0.968
KOH23799.1
Dihydroxy-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.
  
  
 0.964
KOH23800.1
Branched-chain amino acid aminotransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.961
aceE
E1 component; part of pyruvate dehydrogenase; forms a complex with DlaT and LpdC; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.949
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.
  
 0.935
ilvH
Acetolactate synthase 3 regulatory subunit; With IlvI catalyzes the formation of 2-acetolactate from pyruvate, the small subunit is required for full activity and valine sensitivity; E.coli produces 3 isoenzymes of acetolactate synthase which differ in specificity to substrates, valine sensitivity and affinity for cofactors; also known as acetolactate synthase 3 small subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.920
KOH19522.1
3-isopropylmalate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
  0.916
KOH24869.1
Formate acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
  0.900
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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