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
sucCPutative succinyl-CoA synthetase beta chain; 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. (389 aa)    
Predicted Functional Partners:
sucD
succinyl-CoA ligase, 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
sucB
2-oxoglutarate dehydrogenase, E2 component, dihydrolipoyllysine-residue 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).
 
 0.991
sdhC
Succinate dehydrogenase, cytochrome b556 subunit; Identified by match to protein family HMM PF01127; match to protein family HMM TIGR02970.
  
 
 0.990
sdhD
Succinate dehydrogenase, hydrophobic membrane anchor protein; Membrane-anchoring subunit of succinate dehydrogenase (SDH).
  
 
 0.989
sdhA
Succinate dehydrogenase, flavoprotein subunit; Identified by match to protein family HMM PF00890; match to protein family HMM PF02910; match to protein family HMM TIGR01812; match to protein family HMM TIGR01816; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 
 0.987
ACR13668.1
Succinate dehydrogenase / fumarate reductase family protein, iron-sulfur subunit; Identified by similarity to SP:P07014; match to protein family HMM TIGR00384.
 
 0.985
ACR14577.1
Succinate dehydrogenase / fumarate reductase family protein, flavoprotein subunit; Identified by similarity to SP:P0AC41; match to protein family HMM PF00890; match to protein family HMM PF01266; match to protein family HMM PF02910; match to protein family HMM PF07992; match to protein family HMM TIGR01812.
 
 0.984
ACR11710.1
Fumarate reductase / succinate dehydrogenase family protein, iron-sulfur subunit; Identified by similarity to SP:P17596; match to protein family HMM PF00111; match to protein family HMM TIGR00384; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.983
ACR12761.1
2-oxo acid dehydrogenases acyltransferase; Identified by match to protein family HMM PF00198.
  
 0.980
ACR11129.1
Fumarate reductase respiratory complex, transmembrane subunit; Identified by match to protein family HMM PF02967.
  
 
 0.980
Your Current Organism:
Teredinibacter turnerae T7901
NCBI taxonomy Id: 377629
Other names: T. turnerae T7901, Teredinibacter turnerae str. T7901, Teredinibacter turnerae strain T7901
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.