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
sdhBPart 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; the catalytic subunits are similar to fumarate reductase; Derived by automated computational analysis using gene prediction method: Protein Homology. (258 aa)    
Predicted Functional Partners:
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.
 
 0.999
KOO52396.1
Succinate dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
KOO49406.1
Cytochrome B; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B).
  
 
 0.995
KOO47952.1
Fumarate hydratase; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
 
 0.992
sucC
succinyl-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.
 
 0.979
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.
 
 0.969
KOO49046.1
Menaquinol-cytochrome C reductase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.944
KOO52447.1
Citrate synthase; Catalyzes the formation of citrate from acetyl-CoA and oxaloacetate; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.943
KOO49221.1
2-oxoglutarate ferredoxin oxidoreductase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 
 0.903
icmF
methylmalonyl-CoA mutase; Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly.
  
 
 0.899
Your Current Organism:
Viridibacillus arvi
NCBI taxonomy Id: 263475
Other names: Bacillus arvi, Bacillus arvi Heyrman et al. 2005, Bacillus sp. 433-D9, DSM 16317, LMG 22165, LMG:22165, V. arvi, Viridibacillus arvi (Heyrman et al. 2005) Albert et al. 2007
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