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
ilvCKetol-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. (338 aa)    
Predicted Functional Partners:
ilvH
Acetolactate synthase small 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.
 
 
 0.997
ilvD
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.
 
 
 0.997
AMA44969.1
Homoserine dehydrogenase; Catalyzes the formation of L-aspartate 4-semialdehyde from L-homoserine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.986
AMA47776.1
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.
 
 
 0.974
gltB
Glutamate synthase large subunit; Catalyzes the formation of glutamate from glutamine and alpha-ketoglutarate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.970
AMA46909.1
Acetolactate synthase; Catalyzes the condensation of two pyruvates to form acetolactate, implicated in pH homeostasis via the acetoin-2,3-butanediol pathway or in valine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.969
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.
 
  
 0.934
AMA46676.1
3-isopropylmalate dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.921
AMA46835.1
Prephenate dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.884
AMA44227.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.829
Your Current Organism:
Pseudomonas monteilii
NCBI taxonomy Id: 76759
Other names: ATCC 700476, CCUG 38736, CFML 90-60, CIP 104883, DSM 14164, JCM 21585, NBRC 103158, P. monteilii, Pseudomonas sp. MKP 213, Pseudomonas sp. V7SW2
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