ID   NQO8_PARDE              Reviewed;         345 AA.
AC   P29920;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   04-NOV-2008, entry version 51.
DE   RecName: Full=NADH-quinone oxidoreductase subunit 8;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit H;
DE   AltName: Full=NDH-1 subunit 8;
GN   Name=nqo8;
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 1 family.
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DR   EMBL; L02354; AAA25592.1; -; Genomic_DNA.
DR   PIR; C45456; C45456.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:EC.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:HAMAP.
DR   HAMAP; MF_01350; -; 1.
DR   InterPro; IPR001694; Resp_NADH_DHase_1.
DR   PANTHER; PTHR11432; Resp_NADH_DH_1; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00667; COMPLEX1_ND1_1; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Oxidoreductase;
KW   Quinone; Transmembrane; Ubiquinone.
FT   CHAIN         1    345       NADH-quinone oxidoreductase subunit 8.
FT                                /FTId=PRO_0000117521.
FT   TRANSMEM     15     35       Potential.
FT   TRANSMEM     82    102       Potential.
FT   TRANSMEM    115    135       Potential.
FT   TRANSMEM    161    181       Potential.
FT   TRANSMEM    190    210       Potential.
FT   TRANSMEM    240    262       Potential.
FT   TRANSMEM    278    298       Potential.
FT   TRANSMEM    309    329       Potential.
SQ   SEQUENCE   345 AA;  38751 MW;  E33B667E569506B4 CRC64;
     MAEFWASPYG FALSMLLQGL AVIAFVMGSL IFMVYGDRKI WAAVQMRRGP NVVGPWGLLQ
     TFADALKYIV KEIVIPAGAD KFVYFLAPFL SMMLALFAFV VIPFDEGWVM ANINVGILFI
     FAASSLEVYG VIMGGWASNS KYPFLASLRS AAQMISYEVS LGLIIIGIII STGSMNLTAI
     VEAHGGDYGL LNWYWLPHLP MVVLFFVSAL AECNRPPFDL VEAESELVAG FMTEYSSTPY
     LLFMAGEYIA MYLMCALLSL LFFGGWLSPV PFIADGWWWM VIKMWFWFYM FAMVKAIVPR
     YRYDQLMRIG WKVFLPLSLG WVVLVAILAR YEILGGFWAR FAVGG
//