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
ilvEBranched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family. (313 aa)    
Predicted Functional Partners:
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.
  
 0.989
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.
  
 
 0.966
KOO04926.1
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.
 
 0.958
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.
  
 0.957
KOO04925.1
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 0.943
thrA
Aspartate kinase; Multifunctional homotetrameric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.926
pheA
Chorismate mutase; Catalyzing the formation of prephenate from chorismate and the formation of phenylpyruvate from prephenate in phenylalanine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.913
metL
Aspartate kinase; Multifunctional homodimeric enzyme that catalyzes the phosphorylation of aspartate to form aspartyl-4-phosphate as well as conversion of aspartate semialdehyde to homoserine; functions in a number of amino acid biosynthetic pathways; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.913
tyrA
Chorismate mutase; Catalyzes the formation of prephenate from chorismate and the formation of 4-hydroxyphenylpyruvate from prephenate in tyrosine biosynthesis; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  
 0.897
pdhA
Hypothetical protein; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
  
 0.881
Your Current Organism:
Vibrio nereis
NCBI taxonomy Id: 693
Other names: ATCC 25917, Beneckea nereida, Beneckea nereis, CAIM 322, CCUG 28585, CIP 103194, DSM 19584, IFO 15637, JCM 21190, LMG 3895, LMG:3895, NBRC 15637, NCCB 73020, V. nereis, strain 80
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