close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING newly available directed regulatory networks a new typed view showing functional, physical, and regulatory edges in one network new clustering options and cluster-based layouts … and much more!
Explore STRING v12.5 →
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
EH31_04415Acetolactate 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; Belongs to the TPP enzyme family. (552 aa)    
Predicted Functional Partners:
EH31_01175
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.995
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.
 
 0.962
EH31_04410
Aldehyde dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
  0.910
EH31_09785
Threonine dehydratase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.898
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.
 0.862
EH31_06095
Malic enzyme; NADP-dependent; catalyzes the oxidative decarboxylation of malate to form pyruvate; decarboxylates oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.830
EH31_01180
Acetolactate synthase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
  
 
0.809
EH31_00370
Pyridoxal-5'-phosphate-dependent protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.804
EH31_02080
Pyruvate dehydrogenase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
  
 
 0.766
EH31_15305
Aminobenzoate synthetase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.738
Your Current Organism:
Erythrobacter longus
NCBI taxonomy Id: 1044
Other names: ATCC 33941, CIP 104268, DSM 6997, E. longus, IFO 14126, JCM 6170, NBRC 14126, strain OCh101
Server load: medium (58%) [HD]