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
sucDsuccinyl-CoA synthetase, alpha subunit; 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. (709 aa)    
Predicted Functional Partners:
DvMF_1127
TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: ferredoxin; 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: tpe:Tpen_1126 succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.999
DvMF_2460
TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: dde:Dde_1256 fumarate reductase iron-sulfur subunit; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.999
DvMF_2459
KEGG: dde:Dde_1257 fumarate reductase flavoprotein subunit; TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein.
 
 0.998
DvMF_2458
PFAM: fumarate reductase respiratory complex transmembrane subunit; KEGG: dde:Dde_1258 fumarate reductase, cytochrome b subunit.
 
 
 0.997
DvMF_1860
PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; pyruvate:ferredoxin (flavodoxin) oxidoreductase; KEGG: dde:Dde_3237 pyruvate:ferredoxin (flavodoxin) oxidoreductase; Belongs to the pyruvate:ferredoxin/flavodoxin oxidoreductase family.
  
 0.988
DvMF_0184
PFAM: pyruvate ferredoxin/flavodoxin oxidoreductase; pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: dde:Dde_1792 pyruvate ferredoxin oxidoreductase, alpha subunit.
  
 
 0.978
DvMF_2322
PFAM: iron-containing alcohol dehydrogenase; Aldehyde Dehydrogenase_; KEGG: emi:Emin_0772 iron-containing alcohol dehydrogenase; In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.
  
 0.975
DvMF_0602
PFAM: 4Fe-4S ferredoxin iron-sulfur binding domain protein; KEGG: sat:SYN_02497 ferridoxin.
 
 
 0.974
DvMF_1710
PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: dau:Daud_0788 fumarate reductase/succinate dehydrogenase flavoprotein domain protein.
  
 
 0.974
atpA
ATP synthase F1, alpha subunit; Produces ATP from ADP in the presence of a proton gradient across the membrane. The alpha chain is a regulatory subunit. Belongs to the ATPase alpha/beta chains family.
  
 
 0.974
Your Current Organism:
Desulfovibrio vulgaris Miyazaki
NCBI taxonomy Id: 883
Other names: D. vulgaris str. 'Miyazaki F', Desulfovibrio vulgaris (strain Miyazaki), Desulfovibrio vulgaris str. 'Miyazaki F'
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.