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ndhL ndhL ndhH ndhH ndhN ndhN ndhO ndhO ABM71845.1 ABM71845.1 secE secE hli3 hli3 ABM72128.1 ABM72128.1 ABM72999.1 ABM72999.1 ABM71714.1 ABM71714.1 ndhA ndhA
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
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a 3D structure is known or predicted
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Known Interactions
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experimentally determined
Predicted Interactions
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textmining
co-expression
protein homology
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ndhLNADH dehydrogenase subunit NdhL (ndhL); 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. (77 aa)    
Predicted Functional Partners:
ndhH
Putative 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.
    
 
 0.949
ndhN
NADH dehydrogenase I subunit N; 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.
  
 
 
 0.885
ndhO
Conserved hypothetical protein; 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.
  
 
 
 0.880
ABM71845.1
Conserved hypothetical protein.
     
 0.834
secE
Putative preprotein translocase, SecE subunit; Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
  
   
 0.772
hli3
Possible high light inducible protein.
  
     0.772
ABM72128.1
Hypothetical protein.
  
 
   0.769
ABM72999.1
Conserved hypothetical protein.
  
 
 
 0.769
ABM71714.1
Conserved hypothetical protein.
  
     0.766
ndhA
Putative respiratory-chain 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.
    
 
 0.759
Your Current Organism:
Prochlorococcus marinus MIT9515
NCBI taxonomy Id: 167542
Other names: P. marinus str. MIT 9515, Prochlorococcus marinus str. MIT 9515
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