ID   NQO10_PARDE             Reviewed;         200 AA.
AC   P29922;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-NOV-2008, entry version 49.
DE   RecName: Full=NADH-quinone oxidoreductase chain 10;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I, chain 10;
DE   AltName: Full=NDH-1, chain 10;
GN   Name=nqo10;
OS   Paracoccus denitrificans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=266;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13543 / NRRL B-3784;
RX   MEDLINE=93136200; PubMed=8422400; DOI=10.1021/bi00054a030;
RA   Xu X., Matsuno-Yagi A., Yagi T.;
RT   "DNA sequencing of the seven remaining structural genes of the gene
RT   cluster encoding the energy-transducing NADH-quinone oxidoreductase of
RT   Paracoccus denitrificans.";
RL   Biochemistry 32:968-981(1993).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-
CC       sulfur (Fe-S) centers, to quinones in the respiratory chain. The
CC       immediate electron acceptor for the enzyme in this species is
CC       believed to be ubiquinone. Couples the redox reaction to proton
CC       translocation (for every two electrons transferred, four hydrogen
CC       ions are translocated across the cytoplasmic membrane), and thus
CC       conserves the redox energy in a proton gradient.
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- SUBUNIT: NDH-1 is composed of at least 14 different subunits, nqo1
CC       to nqo14. The complex has a L-shaped structure, with the
CC       hydrophobic arm (subunits nqo7, nqo8, nqo10 to nqo14) embedded in
CC       the inner membrane and the hydrophilic peripheral arm (subunits
CC       nqo1 to nqo6, nqo9) protruding into the bacterial cytoplasm. The
CC       hydrophilic domain contains all the redox centers.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein.
CC   -!- SIMILARITY: Belongs to the complex I subunit 6 family.
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DR   EMBL; L02354; AAA25596.1; -; Genomic_DNA.
DR   PIR; F45456; F45456.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to u...; IEA:InterPro.
DR   InterPro; IPR001457; OxRdtase_q3.
DR   Pfam; PF00499; Oxidored_q3; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Oxidoreductase;
KW   Quinone; Transmembrane; Ubiquinone.
FT   CHAIN         1    200       NADH-quinone oxidoreductase chain 10.
FT                                /FTId=PRO_0000118368.
FT   TRANSMEM      2     22       Potential.
FT   TRANSMEM     26     46       Potential.
FT   TRANSMEM     51     71       Potential.
FT   TRANSMEM     90    110       Potential.
FT   TRANSMEM    144    164       Potential.
SQ   SEQUENCE   200 AA;  21819 MW;  9D3B421C33F4ACAE CRC64;
     MMTFAFYLFA ISACVAGFMV VIGRNPVHSV LWLILAFLSA AGLFVLQGAE FVAMLLVVVY
     VGAVAVLFLF VVMMLDVDFA ELKGELARYL PLALVIGVVL LAQLGIAFSG WTPSDQAESL
     RAAPVDAAVE NTLGLGLVLY DRYVLMFQLA GLVLLVAMIG AIVLTMRHRK DVKRQNVLEQ
     MWRDPAKTME LKDVKPGQGL
//