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
acoCAcetoin dehydrogenase E2 component (dihydrolipoamide acetyltransferase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme. (398 aa)    
Predicted Functional Partners:
acoA
Acetoin dehydrogenase E1 component (TPP-dependent alpha subunit); Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage of acetoin into acetate and acetaldehyde. The alpha subunit is probably the catalytic subunit of the enzyme (By similarity).
 0.999
acoB
Acetoin dehydrogenase E1 component (TPP-dependent beta subunit); Catalyzes the 2,6-dichlorophenolindophenol-dependent cleavage of acetoin into acetate and acetaldehyde.
 0.999
acoL
Acetoin dehydrogenase E3 component (dihydrolipoamide dehydrogenase); Evidence 1a: Function experimentally demonstrated in the studied strain; Product type e: enzyme; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
 0.999
pdhD
Dihydrolipoyl dehydrogenase; Catalyzes the oxidation of dihydrolipoamide to lipoamide; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
 0.999
lpdV
Branched-chain alpha-keto acid dehydrogenase E3 subunit (dihydrolipoamide dehydrogenase); The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of 3 enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3); Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family.
 0.998
pdhB
Pyruvate dehydrogenase (E1 beta subunit); 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).
 0.997
odhA
2-oxoglutarate dehydrogenase (E1 subunit); E1 component of the 2-oxoglutarate dehydrogenase (OGDH) complex which catalyzes the decarboxylation of 2-oxoglutarate, the first step in the conversion of 2-oxoglutarate to succinyl-CoA and CO(2).
 0.994
pdhA
Pyruvate dehydrogenase (E1 alpha subunit); 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).
 0.992
bkdAB
Branched-chain alpha-keto acid dehydrogenase E1 subunit; The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3).
 0.974
acoR
Transcriptional regulator; Acts as a transcriptional activator of the acoABCL operon encoding the acetoin dehydrogenase complex.
 
  
 0.961
Your Current Organism:
Bacillus subtilis 168
NCBI taxonomy Id: 224308
Other names: B. subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis 168, Bacillus subtilis subsp. subtilis str. 168, Bacillus subtilis subsp. subtilis str. BGSC 1A700
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