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
acoATPP-dependent pyruvate or acetoin dehydrogenase subunit alpha [Energy production and conversion]; High confidence in function and specificity. (330 aa)    
Predicted Functional Partners:
pdhB
Pyruvate dehydrogenase E1 component subunit beta; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO2. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3); High confidence in function and specificity.
 0.999
PSM36_2445
This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...]
 0.999
PSM36_2447
Pyruvate dehydrogenase (acetyl-transferring); Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine <=> [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO(2); High confidence in function and specificity.
 0.999
acoC
Dihydrolipoamide acetyltransferase; High confidence in function and specificity.
 0.997
PSM36_1042
Branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed; High confidence in function and specificity.
 0.992
PSM36_2183
This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide; High confidenc [...]
 
 0.981
maeB
Bifunctional malic enzyme oxidoreductase/phosphotransacetylase; (S)-malate + NADP(+) <=> pyruvate + CO(2) + NADPH, Oxaloacetate <=> pyruvate + CO(2); High confidence in function and specificity.
  
 
 0.945
PSM36_2185
Branched-chain alpha-keto acid dehydrogenase subunit E2; Reviewed; High confidence in function and specificity.
 0.940
nifJ
Pyruvate dehydrogenase (NADP(+)); Pyruvate + CoA + NADP(+) <=> acetyl-CoA + CO(2) + NADPH; High confidence in function and specificity.
  
 0.937
pdhA
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).
  
  
 
0.924
Your Current Organism:
Proteiniphilum saccharofermentans
NCBI taxonomy Id: 1642647
Other names: CECT 8610, DSM 28694, LMG 28299, LMG:28299, P. saccharofermentans, Proteiniphilum saccharofermentans Hahnke et al. 2016, Proteiniphilum sp. M3/6, strain M3/6
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