STRINGSTRING
AGI23344.1 AGI23344.1 AGI23345.1 AGI23345.1 AGI23346.1 AGI23346.1 AGI23347.1 AGI23347.1 AGI23348.1 AGI23348.1 AGI23349.1 AGI23349.1 nuoC nuoC AGI22207.1 AGI22207.1 nuoI nuoI nuoB nuoB nuoN nuoN
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
AGI23344.1Monovalent cation/H+ antiporter subunit A; COG1009 NADH:ubiquinone oxidoreductase subunit 5 (chain L)/Multisubunit Na+/H+ antiporter, MnhA subunit. (933 aa)    
Predicted Functional Partners:
AGI23345.1
COG1006 Multisubunit Na+/H+ antiporter, MnhC subunit.
 
 
 0.999
AGI23346.1
COG0651 Formate hydrogenlyase subunit 3/Multisubunit Na+/H+ antiporter, MnhD subunit.
 
 
0.999
AGI23347.1
Cation antiporter; COG1863 Multisubunit Na+/H+ antiporter, MnhE subunit.
 
 
 0.999
AGI23348.1
COG2212 Multisubunit Na+/H+ antiporter, MnhF subunit.
 
 
 0.999
AGI23349.1
COG1320 Multisubunit Na+/H+ antiporter, MnhG subunit.
 
 
 0.999
nuoC
Bifunctional NADH:ubiquinone oxidoreductase subunit C/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.
  
 
 0.999
AGI22207.1
COG1145 Ferredoxin.
  
 
 0.996
nuoI
NADH dehydrogenase 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.
  
 
 0.996
nuoB
NADH dehydrogenase subunit B; 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.
  
 
 0.985
nuoN
NADH:ubiquinone oxidoreductase subunit N; 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 subunit 2 family.
 
 
0.970
Your Current Organism:
Pseudomonas sp. ATCC 13867
NCBI taxonomy Id: 1294143
Other names: P. sp. ATCC 13867, Pseudomonas denitrificans ATCC 13867
Server load: low (30%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.