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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
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[Homology]
Score
sucCsuccinyl-CoA synthetase 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. (379 aa)    
Predicted Functional Partners:
sucD
succinyl-CoA synthetase 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.
 0.999
nuoD
NADH-quinone oxidoreductase subunit C; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
  
 0.983
sdhA
Part of four member succinate dehydrogenase enzyme complex that forms a trimeric complex (trimer of tetramers); SdhA/B are the catalytic subcomplex and can exhibit succinate dehydrogenase activity in the absence of SdhC/D which are the membrane components and form cytochrome b556; SdhC binds ubiquinone; oxidizes succinate to fumarate while reducing ubiquinone to ubiquinol; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.975
ALO49709.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.972
ALO48393.1
Pyruvate:ferredoxin (flavodoxin) oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.949
ALO47737.1
MFS transporter; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.941
ALO49954.1
Ferredoxin; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.921
ALO49707.1
Fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.915
ALO47736.1
2-oxoacid:ferredoxin oxidoreductase subunit beta; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.912
ALO49955.1
2-ketoisovalerate ferredoxin oxidoreductase; Catalyzes the coenzyme A-dependent oxidation of 3-methyl-2-oxobutanoate coupled to the reduction of ferredoxin producing S-(2-methylpropanoyl)-CoA; Derived by automated computational analysis using gene prediction method: Protein Homology.
    
 0.912
Your Current Organism:
Prevotella enoeca
NCBI taxonomy Id: 76123
Other names: ATCC 51261, CIP 104472, JCM 12259, NCTC 13068, P. enoeca, VPI D194A-25A
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