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
KOO04925.1Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology. (94 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.
  
  
 0.959
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.
  
 0.944
ilvE
Branched-chain amino acid aminotransferase; Acts on leucine, isoleucine and valine. Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family.
  
  
 0.943
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.
  
 
 0.936
ilvC
Ketol-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.
  
 
 0.848
KOO02341.1
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.
  
 0.748
oadG
Oxaloacetate decarboxylase subunit gamma; Catalyzes the decarboxylation of oxaloacetate coupled to Na(+) translocation.
  
  
  0.741
priB
Primosomal replication protein N; Binds single-stranded DNA at the primosome assembly site (PAS); Belongs to the PriB family.
  
     0.732
KOO02291.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
     0.708
zapC
Cell division protein ZapC; Contributes to the efficiency of the cell division process by stabilizing the polymeric form of the cell division protein FtsZ. Acts by promoting interactions between FtsZ protofilaments and suppressing the GTPase activity of FtsZ.
  
     0.702
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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