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
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
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[Homology]
Score
sucDsuccinyl-CoA synthetase 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. (291 aa)    
Predicted Functional Partners:
sucC
succinyl-CoA synthetase 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
AHY59441.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.993
AHY59442.1
Part of four member fumarate reductase enzyme complex FrdABCD which catalyzes the reduction of fumarate to succinate during anaerobic respiration; FrdAB are the catalytic subcomplex consisting of a flavoprotein subunit and an iron-sulfur subunit, respectively; FrdCD are the membrane components which interact with quinone and are involved in electron transfer; the catalytic subunits are similar to succinate dehydrogenase SdhAB; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 
 0.993
sdhC
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.984
sucA
SucA; E1 component of the oxoglutarate dehydrogenase complex which catalyzes the formation of succinyl-CoA from 2-oxoglutarate; SucA catalyzes the reaction of 2-oxoglutarate with dihydrolipoamide succinyltransferase-lipoate to form dihydrolipoamide succinyltransferase-succinyldihydrolipoate and carbon dioxide; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.981
AHY58522.1
Dihydrolipoamide succinyltransferase; 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).
 
 0.973
AHY57594.1
E3 component of pyruvate and 2-oxoglutarate dehydrogenase complex; catalyzes the oxidation of dihydrolipoamide to lipoamide; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.949
AHY60543.1
acetyl-CoA hydrolase; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 0.946
sdhD
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.941
AHY57592.1
Dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
  
 0.940
Your Current Organism:
Stenotrophomonas rhizophila
NCBI taxonomy Id: 216778
Other names: ATCC BAA-473, CCUG 47042, DSM 14405, JCM 13333, S. rhizophila, Stenotrophomonas rhizophila Wolf et al. 2002, strain e-p10
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