ID   NQO8_RHOMR              Reviewed;         341 AA.
AC   Q4QSC6;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=NADH-quinone oxidoreductase subunit 8;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I subunit 8;
DE   AltName: Full=NDH-1 subunit 8;
GN   Name=nqo8;
OS   Rhodothermus marinus (Rhodothermus obamensis).
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=29549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PRQ-62B;
RX   PubMed=16023073; DOI=10.1016/j.bbabio.2005.06.003;
RA   Melo A.M.P., Lobo S.A.L., Sousa F.L., Fernandes A.S., Pereira M.M.,
RA   Hreggvidsson G.O., Kristjansson J.K., Saraiva L.M., Teixeira M.;
RT   "A nhaD Na+/H+ antiporter and a pcd homologues are among the
RT   Rhodothermus marinus complex I genes.";
RL   Biochim. Biophys. Acta 1709:95-103(2005).
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 menaquinone. 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 (By similarity).
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits
CC       NQO7-14 constitute the membrane sector of the complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC       protein (Potential).
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family.
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DR   EMBL; AY972098; AAY42992.1; -; Genomic_DNA.
DR   BRENDA; 1.6.99.5; 1132.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; NADH_UbQ_OxRdtase_su1.
DR   InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR   PANTHER; PTHR11432; Resp_NADH_DH_1; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00667; COMPLEX1_ND1_1; FALSE_NEG.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Oxidoreductase;
KW   Quinone; Transmembrane.
FT   CHAIN         1    341       NADH-quinone oxidoreductase subunit 8.
FT                                /FTId=PRO_0000240051.
FT   TRANSMEM      9     29       Potential.
FT   TRANSMEM     75     95       Potential.
FT   TRANSMEM    108    128       Potential.
FT   TRANSMEM    154    174       Potential.
FT   TRANSMEM    180    200       Potential.
FT   TRANSMEM    244    264       Potential.
FT   TRANSMEM    278    298       Potential.
FT   TRANSMEM    321    341       Potential.
SQ   SEQUENCE   341 AA;  37374 MW;  546A00803E4605A9 CRC64;
     MDLPLYWTAL IAFLIINAML LTASVLVYAE RKISGFIQHR LGPNRVGPAG FLQPFADVVK
     LLFKEDIIPA QANRFIHALA PTIMVTIAMT VPALIPFARG VVIADIDVGV LAILALTSIS
     VYGITLAGWS SNSKYSLLGG LRSSAQMISY ELAMGTAVLS VILQAGSLNV SAIVEAQRDG
     WAILGWHVFT NPIGALIFIV TAFAETNRLP FDLPEAEQEL VGGYHTEYSG MKFGMFFLAE
     YVNLFVASFV IATLFFGGYL VPFEPLLLKA FPALEGSVLL GLLQFLSLLA KTCFFAFLYI
     WVRWTFPRFK YNQLMTLGWK YLLPIGLANV ILIALGVALF S
//