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. (392 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
Acel_0586
TIGRFAM: 2-oxoglutarate dehydrogenase, E1 subunit; PFAM: dehydrogenase, E1 component; catalytic domain of components of various dehydrogenase complexes; Transketolase, central region; KEGG: tfu:Tfu_0566 2-oxoglutarate dehydrogenase, E1 component.
 
 0.999
Acel_1865
PFAM: fumarate reductase/succinate dehydrogenase flavoprotein domain protein; FAD dependent oxidoreductase; KEGG: sco:SCO5107 putative succinate dehydrogenase flavoprotein subunit.
 0.990
Acel_1864
TIGRFAM: succinate dehydrogenase and fumarate reductase iron-sulfur protein; PFAM: ferredoxin; KEGG: nfa:nfa56030 putative succinate dehydrogenase iron-sulfur subunit.
 
 0.987
Acel_0935
2-oxoglutarate dehydrogenase E2 component; PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: fra:Francci3_3135 dehydrogenase subunit.
 
 0.977
Acel_0284
PFAM: pyruvate flavodoxin/ferredoxin oxidoreductase domain protein; KEGG: tfu:Tfu_2674 2-oxoglutarate ferredoxin oxidoreductase, alpha subunit.
  
 
 0.957
Acel_1658
KEGG: mbo:Mb1162 citrate synthase; TIGRFAM: 2-methylcitrate synthase/citrate synthase II; PFAM: Citrate synthase; Belongs to the citrate synthase family.
  
 
 0.945
Acel_0588
Catalytic domain of components of various dehydrogenase complexes; The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
 
 0.931
Acel_0031
PFAM: biotin/lipoyl attachment domain-containing protein; catalytic domain of components of various dehydrogenase complexes; E3 binding domain protein; KEGG: sco:SCO3815 putative dihydrolipoamide acyltransferase component.
 
 0.928
Acel_0377
TIGRFAM: Methylmalonyl-CoA mutase-like; PFAM: cobalamin B12-binding domain protein; KEGG: ade:Adeh_1832 methylmalonyl-CoA mutase.
  
 
 0.925
Your Current Organism:
Acidothermus cellulolyticus
NCBI taxonomy Id: 351607
Other names: A. cellulolyticus 11B, Acidothermus cellulolyticus 11B, Acidothermus cellulolyticus str. 11B, Acidothermus cellulolyticus strain 11B
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.