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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13543 / NRRL B-3784;
DOI=10.1021/bi00054a030; PubMed=8422400 [NCBI, ExPASy, EBI, Israel, Japan]
Xu X.,
Matsuno-Yagi A.,
Yagi T.;
"DNA sequencing of the seven remaining structural genes of the gene cluster encoding the energy-transducing NADH-quinone oxidoreductase of Paracoccus denitrificans.";
Biochemistry 32:968-981(1993).
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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.
- 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; Multi-pass membrane protein.
- SIMILARITY: Belongs to the complex I subunit 6 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: 200 AA [This is the length of the unprocessed precursor] |
Molecular weight: 21819 Da [This is the MW of the unprocessed precursor] |
CRC64: 9D3B421C33F4ACAE [This is a checksum on the sequence] |
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10 20 30 40 50 60
MMTFAFYLFA ISACVAGFMV VIGRNPVHSV LWLILAFLSA AGLFVLQGAE FVAMLLVVVY
70 80 90 100 110 120
VGAVAVLFLF VVMMLDVDFA ELKGELARYL PLALVIGVVL LAQLGIAFSG WTPSDQAESL
130 140 150 160 170 180
RAAPVDAAVE NTLGLGLVLY DRYVLMFQLA GLVLLVAMIG AIVLTMRHRK DVKRQNVLEQ
190 200
MWRDPAKTME LKDVKPGQGL
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P29922 in FASTA format |
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