| Protein name |
NAD(P)H-quinone oxidoreductase subunit O (EC 7.1.1.-) (NAD(P)H dehydrogenase I subunit O) (NDH-1 subunit O) (NDH-O) |
| NCBI Accession ID |
CP000553.1 |
| Organism |
Prochlorococcus marinus (strain NATL1A) |
| Left |
180277 |
| Right |
180540 |
| Strand |
+ |
| Nucleotide Sequence |
ATGTCTGAACAAACCGGAAAAGTAGATGATTCACAATCACCTCCAAAGGTACAAAAGAAACTCAGAAAAGGAGATCTTGTAAAAGTTGATCGTGAAAAATATTCTAATAGCTTAGAATCTAAGGCAAGTGATACTAATCTACCTGAATATATTTTTCAAGGGCCTGGCGAAGTATTATTGATTAAAGGTGATTACTGTCAAGTTAGATGGAGGAGACCAGTCCCTGATGTTTGGATGAATTCTGATCATATAGTCTCATATTAA |
| Sequence |
MSEQTGKVDDSQSPPKVQKKLRKGDLVKVDREKYSNSLESKASDTNLPEYIFQGPGEVLLIKGDYCQVRWRRPVPDVWMNSDHIVSY |
| Source of smORF |
Swiss-Prot |
| Function |
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. {ECO:0000255|HAMAP-Rule:MF_01354}. |
| Pubmed ID |
18159947
|
| Domain |
CDD:403201 |
| Functional Category |
Others |
| Uniprot ID |
A2BZU7
|
| ORF Length (Amino Acid) |
87 |