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
APH00530.1NADH-quinone oxidoreductase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology. (175 aa)    
Predicted Functional Partners:
APH00463.1
Subunit A of antiporter complex involved in resistance to high concentrations of Na+, K+, Li+ and/or alkali; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.999
APH00502.1
NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
 
 0.999
nuoB
NADH dehydrogenase; 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 a menaquinone. 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.
 
 0.999
nuoC
NADH dehydrogenase; 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 a menaquinone. 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.
 
 0.999
APH00504.1
NADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
APH00507.1
NADH-quinone oxidoreductase subunit G; Catalyzes the transfer of electrons from NADH to quinone; Derived by automated computational analysis using gene prediction method: Protein Homology.
  
 0.999
APH00508.1
NADH:ubiquinone oxidoreductase subunit H; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
APH00513.1
NADH:ubiquinone oxidoreductase subunit M; Derived by automated computational analysis using gene prediction method: Protein Homology.
 
 0.999
APH00525.1
NADH-ubiquinone oxidoreductase subunit 3; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain.
 
 0.999
nuoB-2
Hydroxyacid dehydrogenase; 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 a menaquinone. 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.
 
 0.999
Your Current Organism:
Janibacter terrae
NCBI taxonomy Id: 103817
Other names: ATCC BAA-130, CCUG 45369, CIP 107018, DSM 13876, DSM 13953 [[Janibacter brevis Imamura et al. 2000]], J. terrae, JCM 10705, JCM 12887 [[Janibacter brevis Imamura et al. 2000]], Janibacter brevis, Janibacter brevis Imamura et al. 2000, Janibacter terrae Yoon et al. 2000 emend. Lang et al. 2003, KCCM 80001, KCTC 19953, NBRC 107853, strain 10N [[Janibacter brevis Imamura et al. 2000]], strain CS12
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