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
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Textmining
[Homology]
Score
sdhASuccinate dehydrogenase, flavoprotein subunit; COG: COG1053; Pfam: PF00890,PF02910; InterPro: IPR011281; Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily. (588 aa)    
Predicted Functional Partners:
sdhB
Succinate dehydrogenase iron-sulfur subunit; COG: COG0479; Pfam: PF00111; InterPro: IPR004489; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.999
sdhC
Succinate dehydrogenase, cytochrome b556 subunit; COG: COG2009; Pfam: PF01127; InterPro: IPR014314; overlaps another CDS with the same product name.
 
 0.999
frdB
Succinate dehydrogenase and fumarate reductase iron-sulfur protein; COG: COG0479; Pfam: PF00111,PF00037; InterPro: IPR004489; Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
 
 0.998
sdhD
Succinate dehydrogenase, hydrophobic membrane anchor protein; Membrane-anchoring subunit of succinate dehydrogenase (SDH).
 
 0.997
fumB
Hydrolyase, tartrate beta subunit/fumarate domain protein, Fe-S type; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
 
 0.991
nifJ
Pyruvate synthase; COG: COG0674; Pfam: PF01855,PF01558,PF00037,PF02775; InterPro: IPR011895.
  
 
 0.989
sucC
succinate-CoA ligase, 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.
 
 0.988
fumC
Fumarate hydratase, class II; Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate; Belongs to the class-II fumarase/aspartase family. Fumarase subfamily.
 
 0.987
nuoD
NADH dehydrogenase subunit D; 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; In the C-terminal section; belongs to the complex I 49 kDa subunit family.
  
 
 0.986
sucD
succinyl-CoA synthetase, 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.
 
 0.985
Your Current Organism:
Serratia odorifera
NCBI taxonomy Id: 667129
Other names: S. odorifera DSM 4582, Serratia odorifera DSM 4582, Serratia odorifera str. DSM 4582, Serratia odorifera strain DSM 4582
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