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
RPE_3203succinyl-CoA synthetase (ADP-forming) beta subunit; PFAM: ATP-citrate lyase/succinyl-CoA ligase; ATP-grasp domain protein; KEGG: ttj:TTHA0538 succinyl-CoA synthetase beta chain. (375 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
sucD-2
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
RPE_0514
KEGG: rpa:RPA0216 succinate dehydrogenase iron-sulfur protein subunit; TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: ferredoxin; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.990
RPE_0510
PFAM: succinate dehydrogenase, cytochrome b subunit; KEGG: rpb:RPB_0327 succinate dehydrogenase, cytochrome b subunit.
  
 
 0.989
RPE_0511
PFAM: succinate dehydrogenase, cytochrome b subunit; KEGG: rpb:RPB_0326 succinate dehydrogenase, cytochrome b subunit.
  
 
 0.988
RPE_0512
KEGG: rpc:RPC_0070 succinate dehydrogenase, flavoprotein subunit; TIGRFAM: succinate dehydrogenase, flavoprotein subunit; succinate dehydrogenase or fumarate reductase, flavoprotein subunit; PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; FAD dependent oxidoreductase; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 
 0.987
RPE_0296
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).
 
 0.984
RPE_2567
KEGG: rpa:RPA2907 citrate synthase; TIGRFAM: citrate synthase I; PFAM: Citrate synthase; Belongs to the citrate synthase family.
  
 
 0.971
RPE_0297
TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase, E1 component; Transketolase, central region; KEGG: rpc:RPC_0191 2-oxoglutarate dehydrogenase, E1 component.
 
 0.966
RPE_2616
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
  
 0.962
Your Current Organism:
Rhodopseudomonas palustris BisA53
NCBI taxonomy Id: 316055
Other names: R. palustris BisA53, Rhodopseudomonas palustris str. BisA53, Rhodopseudomonas palustris strain BisA53
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.