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
sucCsuccinyl-CoA synthetase (ADP-forming) beta 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 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. (388 aa)    
Predicted Functional Partners:
sucD
succinyl-CoA synthetase (ADP-forming) 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.
 0.999
ABK47939.1
PFAM: succinate dehydrogenase, cytochrome b subunit; KEGG: son:SO1927 succinate dehydrogenase, cytochrome b556 subunit.
  
 
 0.990
ABK47940.1
Succinate dehydrogenase subunit D; Membrane-anchoring subunit of succinate dehydrogenase (SDH).
  
 
 0.990
ABK47944.1
2-oxoglutarate dehydrogenase E2 component; 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).
 
 0.989
ABK47942.1
TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; KEGG: son:SO1929 succinate dehydrogenase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.983
ABK47943.1
TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase, E1 component; Transketolase, central region; KEGG: son:SO1930 2-oxoglutarate dehydrogenase E1 component.
 
 0.982
ABK46647.1
Succinate dehydrogenase subunit B; KEGG: son:SO0399 fumarate reductase iron-sulfur protein; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: 4Fe-4S ferredoxin, iron-sulfur binding domain protein.
 
 0.980
ABK47941.1
TIGRFAM: succinate dehydrogenase, flavoprotein subunit; succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: son:SO1928 succinate dehydrogenase flavoprotein subunit; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 
 0.980
ABK46646.1
TIGRFAM: succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; KEGG: son:SO0398 fumarate reductase flavoprotein subunit.
 
 0.972
ABK46644.1
PFAM: fumarate reductase respiratory complex, transmembrane subunit; KEGG: son:SO0396 fumarate reductase cytochrome B subunit.
  
 
 0.968
Your Current Organism:
Shewanella sp. ANA3
NCBI taxonomy Id: 94122
Other names: S. sp. ANA-3, Shewanella sp. ANA-3, Shewanella sp. arsenana, Shewanella trabarsenatis
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.