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gll2083 protein (Gloeobacter violaceus) - STRING interaction network
"gll2083" - NAD(P)H-quinone oxidoreductase subunit F in Gloeobacter violaceus
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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Score
gll2083NAD(P)H-quinone oxidoreductase subunit F (618 aa)    
Predicted Functional Partners:
gll2082
NAD(P)H-quinone oxidoreductase subunit D4 (510 aa)
0.999
ndhA
NADH dehydrogenase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient (407 aa)
 
  0.998
ndhH2
NAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon- concentration (394 aa)
 
  0.998
ndhH1
NAD(P)H-quinone oxidoreductase subunit H; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon- concentration (393 aa)
 
  0.998
glr0219
NAD(P)H-quinone oxidoreductase subunit 4; NDH-1 shuttles electrons from NAD(P)H, 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 plastoquinone. 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 (526 aa)
 
0.997
glr1004
NAD(P)H-quinone oxidoreductase subunit M (504 aa)
0.997
glr0750
NADH dehydrogenase subunit J; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon- concentration (176 aa)
 
  0.997
gll2536
NADH dehydrogenase subunit 4 (498 aa)
 
0.996
ndhC
NADH dehydrogenase subunit A; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon- concentration (120 aa)
 
  0.996
ndhB
NAD(P)H-quinone oxidoreductase subunit 2; NDH-1 shuttles electrons from an unknown electron donor, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory and/or the photosynthetic chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient. Cyanobacterial NDH-1 also plays a role in inorganic carbon- concentration (513 aa)
 
  0.996
Your Current Organism:
Gloeobacter violaceus
NCBI taxonomy Id: 251221
Other names: G. violaceus, G. violaceus PCC 7421, Gloeobacter, Gloeobacter violaceus, Gloeobacter violaceus ATCC 29082, Gloeobacter violaceus PCC 7421, Gloeobacter violaceus str. PCC 7421, Gloeobacter violaceus strain PCC 7421, Gloeobacterales, Gloeobacterales Cavalier-Smith 2002, Gloeobacteria, Gloeobacteria Cavalier-Smith 2002
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