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. (386 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
Pnap_3035
TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; KEGG: pol:Bpro_3603 succinate dehydrogenase and fumarate reductase iron-sulfur protein; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 0.990
Pnap_3032
PFAM: succinate dehydrogenase, cytochrome b subunit; KEGG: pol:Bpro_3600 succinate dehydrogenase, cytochrome b subunit.
  
 
 0.988
Pnap_3033
KEGG: pol:Bpro_3601 succinate dehydrogenase, cytochrome b subunit.
  
 
 0.987
Pnap_1857
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).
 0.983
Pnap_3034
KEGG: pol:Bpro_3602 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 pyridine nucleotide-disulphide oxidoreductase; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily.
 0.969
Pnap_1782
Pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.949
Pnap_2383
KEGG: pol:Bpro_2161 methylmalonyl-CoA mutase; TIGRFAM: methylmalonyl-CoA mutase, large subunit; PFAM: methylmalonyl-CoA mutase; cobalamin B12-binding domain protein.
  
 
 0.943
Pnap_0073
PFAM: acetyl-CoA hydrolase/transferase; KEGG: dar:Daro_2807 acetyl-CoA hydrolase/transferase.
   
 0.933
Pnap_1856
KEGG: pol:Bpro_2624 2-oxoglutarate dehydrogenase, E1 component; TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase, E1 component; Transketolase, central region.
 
 0.931
Your Current Organism:
Polaromonas naphthalenivorans
NCBI taxonomy Id: 365044
Other names: P. naphthalenivorans CJ2, Polaromonas naphthalenivorans CJ2, Polaromonas naphthalenivorans str. CJ2, Polaromonas naphthalenivorans strain CJ2
Server load: medium (42%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.