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
ARP43697.1Succinate dehydrogenasecytochrome b556 subunit. (202 aa)    
Predicted Functional Partners:
frdB
Fumarate reductase iron-sulfur subunit.
 
 0.999
frdA
Fumarate reductase flavoprotein subunit.
 
 0.999
sucC
Succinyl-CoA ligase [ADP-forming]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.
  
 
 0.989
sucD
Succinyl-CoA ligase [ADP-forming]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.
  
 
 0.983
ARP41472.1
Putative fumarate hydratase subunit beta; Catalyzes the reversible hydration of fumarate to (S)-malate. Belongs to the class-I fumarase family.
  
 
 0.980
ctaC
Cytochrome c oxidase subunit 2; 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).
  
 
 0.975
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.
  
 
 0.969
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.
   
  
 0.949
ordL
Putative oxidoreductase OrdL.
  
  
 0.929
ach1
Acetyl-CoA hydrolase.
   
 
 0.909
Your Current Organism:
Geobacillus thermodenitrificans
NCBI taxonomy Id: 33940
Other names: ATCC 29492, BGSC 94A1, Bacillus sp. BGSC W9A21, Bacillus sp. BGSC W9A45, Bacillus sp. BGSC W9A5, Bacillus sp. BGSC W9A54, Bacillus sp. BGSC W9A65, Bacillus sp. BGSC W9A66, Bacillus sp. BGSC W9A67, Bacillus sp. BGSC W9A69, Bacillus sp. BGSC W9A71, Bacillus sp. BGSC W9A73, Bacillus sp. BGSC W9A74, Bacillus sp. BGSC W9A86, Bacillus sp. BGSC W9A87, Bacillus sp. BGSC W9A91, Bacillus thermodenitrificans, DSM 465, G. thermodenitrificans, Geobacillus sp. A333, Geobacillus sp. F84a, Geobacillus sp. G11MC16, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Cihan et al. 2011, Geobacillus thermodenitrificans (Manachini et al. 2000) Nazina et al. 2001 emend. Coorevits et al. 2012, LMG 17532, LMG:17532, strain R-35647
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