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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
bkdA12-oxoisovalerate dehydrogenase alpha subunit. (412 aa)    
Predicted Functional Partners:
pdhB
Pyruvate dehydrogenase beta subunit; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2.
 0.999
bkdA2
2-oxoisovalerate dehydrogenase beta subunit.
 0.999
bkdB
Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex E2.
 
 0.998
lpdA
Dihydrolipoamide dehydrogenase.
 
 
 0.970
lpdA-2
Dihydrolipoamide dehydrogenase.
 
 
 0.964
ilvE
Branched-chain-amino-acid aminotransferase.
   
 
 0.911
aceF
Dihydrolipoamide acetyltransferase.
 
 0.901
sucB
Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; E2 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the second step in the conversion of 2- oxoglutarate to succinyl-CoA and CO(2).
 
 0.859
mmgC-2
acyl-CoA dehydrogenase.
  
 
 0.848
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.
     
 0.806
Your Current Organism:
Agrobacterium fabrum
NCBI taxonomy Id: 176299
Other names: A. fabrum str. C58, Agrobacterium fabrum str. C58, Agrobacterium tumefaciens (strain C58 / ATCC 33970), Agrobacterium tumefaciens (strain C58), Agrobacterium tumefaciens str. C58, Agrobacterium tumefaciens str. C58 (Cereon), Agrobacterium tumefaciens str. C58 (Dupont), Agrobacterium tumefaciens str. C58 (U. Washington), Rhizobium radiobacter str. C58 (Cereon), Rhizobium radiobacter str. C58 (Dupont), Rhizobium radiobacter str. C58 (U. Washington)
Server load: medium (62%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.