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
OEF99305.1Succinate dehydrogenase flavoprotein subunit; Derived by automated computational analysis using gene prediction method: Protein Homology. (586 aa)    
Predicted Functional Partners:
BHF71_01545
Integrase; Incomplete; too short partial abutting assembly gap; missing start; Derived by automated computational analysis using gene prediction method: GeneMarkS+.
 
 0.999
OEF99306.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
OEG00226.1
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.999
OEG00154.1
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.999
OEF99276.1
Electron transfer flavoprotein subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.991
nuoD
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be a menaquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family.
  
 0.988
sucC
succinate--CoA ligase subunit beta; 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.
 0.971
sucD
succinate--CoA ligase subunit alpha; 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.
 0.969
OEG00081.1
Citrate synthase; Catalyzes the formation of citrate from acetyl-CoA and oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.951
nuoI
NADH-quinone oxidoreductase subunit I; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
  
 0.948
Your Current Organism:
Vulcanibacillus modesticaldus
NCBI taxonomy Id: 337097
Other names: Bacillus sp. BR, DSM 14931, JCM 12998, V. modesticaldus, strain Br
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