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:
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Gene Fusion
Cooccurrence
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[Homology]
Score
NuoENADH dehydrogenase; Derived by automated computational analysis using gene prediction method: Protein Homology. (286 aa)    
Predicted Functional Partners:
nuoA
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 subunit 3 family.
 
 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
nuoD
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 49 kDa subunit family.
 
 0.999
NuoF
NADH dehydrogenase; 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.
 0.999
NuoG
NADH-quinone oxidoreductase subunit 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.
 
 0.999
nuoH
NADH-quinone oxidoreductase subunit H; 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. This subunit may bind ubiquinone.
 
 0.999
nuoI
(4Fe-4S)-binding protein; 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.
 
 0.999
NuoJ_2
NADH:ubiquinone oxidoreductase subunit J; 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.
 
 0.999
nuoK
NADH:ubiquinone oxidoreductase subunit K; 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 subunit 4L family.
 
 0.999
Your Current Organism:
Streptomyces griseorubiginosus
NCBI taxonomy Id: 67304
Other names: ATCC 23627, ATCC 23946 [[Streptomyces phaeopurpureus]], ATCC 23947 [[Streptomyces phaeoviridis]], ATCC 25459, Actinomyces griseorubiginosus, BCRC 12124, BCRC 13754 [[Streptomyces phaeopurpureus]], CBS 692.69, CBS 930.68 [[Streptomyces phaeopurpureus]], CCRC 12124, CCRC 13754 [[Streptomyces phaeopurpureus]], CCRC:12124, CCRC:13754 [[Streptomyces phaeopurpureus]], DSM 40125 [[Streptomyces phaeopurpureus]], DSM 40469, HAMBI 950 [[Streptomyces phaeopurpureus]], IFO 12899 [[Streptomyces phaeopurpureus]], IFO 12900 [[Streptomyces phaeoviridis]], IFO 13047, IFO 3930 [[Streptomyces phaeopurpureus]], INA 7712, ISP 5125 [[Streptomyces phaeopurpureus]], ISP 5469, JCM 4101 [[Streptomyces phaeopurpureus]], JCM 4481, JCM 4660 [[Streptomyces phaeopurpureus]], JCM 4661 [[Streptomyces phaeoviridis]], KCTC 9764 [[Streptomyces phaeopurpureus]], LMG 19941, LMG:19941, NBRC 12899 [[Streptomyces phaeopurpureus]], NBRC 12900 [[Streptomyces phaeoviridis]], NBRC 13047, NBRC 3930 [[Streptomyces phaeopurpureus]], NCIMB 9832 [[Streptomyces phaeoviridis]], NRRL B-12384, NRRL B-2258 [[Streptomyces phaeoviridis]], NRRL B-2260 [[Streptomyces phaeopurpureus]], NRRL-ISP 5125 [[Streptomyces phaeopurpureus]], NRRL-ISP 5469, NRRL:B:2258 [[Streptomyces phaeoviridis]], S. griseorubiginosus, Streptomyces griseirubiginosus, Streptomyces phaeopurpureus, Streptomyces phaeoviridis
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