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
petCUbiquinol-cytochrome c reductase; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG2857/TC:3.D.3.2.1. (254 aa)    
Predicted Functional Partners:
petB
Ubiquinol-cytochrome c reductase; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 0.999
petA
Ubiquinol-cytochrome c reductase; Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
 
 0.999
pqqL
Zinc protease; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG0612; Belongs to the peptidase M16 family.
   
 0.998
vioB
VioB - polyketide synthase; Catalyzes the hydrogen peroxide-dependent dimerization of two L-tryptophan-derived molecules (imine form of indole 3-pyruvate (IPA)), to form an uncharacterized product suggested to be indole-3-pyruvate imine dimer that can spontaneously convert into dichlorochromopyrrolate (CPA). The uncharacterized product is the substrate of VioE.
  
 0.996
nuoF
NADH-ubiquinone oxidoreductase, chain F; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. Belongs to the complex I 51 kDa subunit family.
   
 
 0.993
nuoE
NADH-ubiquinone oxidoreductase, chain E; Identified by sequence similarity; putative; ORF located using Glimmer/GeneMark/Blastx/COG1905.
   
 
 0.992
nuoG
NADH-ubiquinone oxidoreductase, chain G; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. 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 75 kDa subunit family.
   
 
 0.992
nuoC
NADH-ubiquinone oxidoreductase, chain 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 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; Belongs to the complex I 30 kDa subunit family.
   
 
 0.991
nuoD
NADH-ubiquinone oxidoreductase, chain 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; Belongs to the complex I 49 kDa subunit family.
   
 
 0.991
coxB
Cytochrome-c oxidase, subunit II; 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).
 
 
 0.989
Your Current Organism:
Chromobacterium violaceum
NCBI taxonomy Id: 243365
Other names: C. violaceum ATCC 12472, Chromobacterium violaceum ATCC 12472, Chromobacterium violaceum ATCC12472, Chromobacterium violaceum str. ATCC 12472
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