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cydA protein (Synechocystis sp. PCC6803) - STRING interaction network
"cydA" - Cytochrome oxidase d subunit I in Synechocystis sp. PCC6803
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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[Homology]
Score
cydACytochrome oxidase d subunit I (483 aa)    
Predicted Functional Partners:
cydB
Cytochrome oxidase d subunit II (336 aa)
 
  0.999
SYNGTS_1195
Succinate dehydrogenase iron-sulphur protein subunit (331 aa)
         
  0.982
frdA
Succinate dehydrogenase flavoprotein subunit (575 aa)
     
 
  0.980
ndhC
NADH dehydrogenase subunit 3; 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 (By similarity) (120 aa)
     
 
  0.979
ndhK1
NADH dehydrogenase subunit; 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 (248 aa)
     
 
  0.979
ndhA
NADH dehydrogenase subunit 1; 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 (372 aa)
         
  0.979
ndhI
NADH dehydrogenase subunit; 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 (193 aa)
         
  0.979
ndbB
NADH dehydrogenase; Bifunctional oxidoreductase probably ables to act both on prenyl naphthoquinones and on prenyl benzoquinones (PubMed-26023160). Catalyzes the penultimate step in the biosynthesis of vitamin K1 (PubMed-26023160) (404 aa)
 
 
  0.978
SYNGTS_1211
NADH dehydrogenase (445 aa)
   
 
  0.977
ndhD4
NADH dehydrogenase subunit 4 (507 aa)
     
 
  0.977
Your Current Organism:
Synechocystis sp. PCC6803
NCBI taxonomy Id: 1148
Other names: Aphanocapsa sp. (strain N-1), Aphanocapsa sp. N-1, S. sp. PCC 6803, Synechocystis, Synechocystis PCC6803, Synechocystis sp. (ATCC 27184), Synechocystis sp. (PCC 6803), Synechocystis sp. (strain PCC 6803), Synechocystis sp. ATCC 27184, Synechocystis sp. PCC 6803, Synechocystis sp. PCC 6803 A, Synechocystis sp. PCC 6803 B, Synechocystis sp. PCC6803
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