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. (333 aa)    
Predicted Functional Partners:
ilvG
Acetolactate synthase 2 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.
 
 
 0.997
leuC
3-isopropylmalate dehydratase large subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate.
  
 0.994
ilvD
Dihydroxy-acid dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the IlvD/Edd family.
 
 
 0.994
APO89472.1
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.986
leuD
3-isopropylmalate dehydratase small subunit; Catalyzes the isomerization between 2-isopropylmalate and 3- isopropylmalate, via the formation of 2-isopropylmaleate. Belongs to the LeuD family. LeuD type 1 subfamily.
 
  
 0.978
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 1 subfamily.
 
  
 0.949
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 1 subfamily.
 
  
 0.939
poxB
Pyruvate oxidase; Catalyzes the formation of acetate from pyruvate; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the TPP enzyme family.
 
  
 0.898
APO89471.1
Serine/threonine dehydratase; Catalyzes the formation of 2-oxobutanoate from L-threonine; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.871
gltB
Glutamate synthase large subunit; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.820
Your Current Organism:
Xanthomonas euvesicatoria
NCBI taxonomy Id: 456327
Other names: ATCC 11633, Bacterium vesicatorium, DSM 19128, ICMP 109, ICMP 98, NCPPB 2968, X. euvesicatoria, Xanthomonas campestris (pv. vesicatoria), Xanthomonas campestris pv. Vesicatoria type A, Xanthomonas campestris pv. vesicatoria, Xanthomonas euvesicatoria Jones et al. 2006 emend. Constantin et al. 2016
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