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.
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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
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[Homology]
Score
sucDsuccinate--CoA ligase subunit alpha; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while succinate binding and nucleotide specificity is provided by the beta subunit. (300 aa)    
Predicted Functional Partners:
sucC
succinate--CoA ligase subunit beta; Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit.
 0.999
sdhB
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.998
sdhA
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.998
sdhC
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 
 0.995
acoC
Branched-chain alpha-keto acid dehydrogenase subunit E2; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.972
aceF
2-oxoglutarate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.971
KZE52005.1
methylmalonyl-CoA mutase; MDM; functions in conversion of succinate to propionate; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.968
KZE52006.1
methylmalonyl-CoA mutase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.968
KZE51465.1
Dienelactone hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.967
KZE48290.1
acetyl-CoA hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.964
Your Current Organism:
Brevibacillus parabrevis
NCBI taxonomy Id: 54914
Other names: ATCC 10027, B. parabrevis, Bacillus parabrevis, CIP 103840, DSM 8376, IFO 12334, JCM 8506, LMG 15971, LMG:15971, NBRC 12334, NCIMB 13346, NRRL NRS-605, NRRL NRS-815
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