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
pdhB_2Pyruvate dehydrogenase E1 component subunit beta. (332 aa)    
Predicted Functional Partners:
pdhA_1
Pyruvate dehydrogenase E1 component subunit alpha; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
 0.999
pdhA_2
Pyruvate dehydrogenase E1 component subunit alpha; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
 0.999
pdhA_3
Pyruvate dehydrogenase E1 component subunit alpha; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
 0.999
acoA
Acetoin:2,6-dichlorophenolindophenol oxidoreductase subunit alpha.
 0.996
ARP43395.1
2-oxoisovalerate dehydrogenase subunit alpha.
 0.996
pdhC_1
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex.
 0.994
pdhC_2
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex.
 0.994
pdhC_4
Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex.
 0.994
pdhD
Dihydrolipoyl dehydrogenase.
 0.990
lpdA
Dihydrolipoyl dehydrogenase.
 
 0.987
Your Current Organism:
Geobacillus thermodenitrificans
NCBI taxonomy Id: 33940
Other names: ATCC 29492, BGSC 94A1, Bacillus sp. BGSC W9A21, Bacillus sp. BGSC W9A45, Bacillus sp. BGSC W9A5, Bacillus sp. BGSC W9A54, Bacillus sp. BGSC W9A65, Bacillus sp. BGSC W9A66, Bacillus sp. BGSC W9A67, Bacillus sp. BGSC W9A69, Bacillus sp. BGSC W9A71, Bacillus sp. BGSC W9A73, Bacillus sp. BGSC W9A74, Bacillus sp. BGSC W9A86, Bacillus sp. BGSC W9A87, Bacillus sp. BGSC W9A91, Bacillus thermodenitrificans, DSM 465, G. thermodenitrificans, Geobacillus sp. A333, Geobacillus sp. F84a, Geobacillus sp. G11MC16, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Cihan et al. 2011, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Coorevits et al. 2012, LMG 17532, LMG:17532, strain R-35647
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