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- FUNCTION: 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.
- CATALYTIC ACTIVITY: NADH + quinone = NAD+ + quinol.
- COFACTOR: Binds 1 4Fe-4S cluster (Potential).
- SUBUNIT: NDH-1 is composed of at least 14 different subunits, nqo1 to nqo14. The complex has a L-shaped structure, with the hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in the inner membrane and the hydrophilic peripheral arm (subunits nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The hydrophilic domain contains all the redox centers.
- SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein.
- SIMILARITY: Belongs to the complex I 20 kDa subunit family.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 173 AA [This is the length of the unprocessed precursor] |
Molecular weight: 19117 Da [This is the MW of the unprocessed precursor] |
CRC64: 587B86578797CAEF [This is a checksum on the sequence] |
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10 20 30 40 50 60
MTGLNTAGAD RDLATAELNR ELQDKGFLLT TTEDIINWAR NGSLHWMTFG LACCAVEMMQ
70 80 90 100 110 120
TSMPRYDLER FGTAPRASPR QSDLMIVAGT LTNKMAPALR KVYDQMPEPR YVISMGSCAN
130 140 150 160 170
GGGYYHYSYS VVRGCDRIVP VDIYVPGCPP TAEALLYGIL QLQRRASGAP ARW
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P29918 in FASTA format |
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