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   25-MAY-2022, entry version 60.
DE   RecName: Full=NADH-quinone oxidoreductase subunit 8;
DE            EC=7.1.1.-;
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; Bacteroidetes Order II. Incertae sedis;
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 Rhodothermus
RT   marinus complex I genes.";
RL   Biochim. Biophys. Acta 1709:95-103(2005).
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       menaquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC   -!- SUBUNIT: NDH-1 is composed of 14 different subunits. Subunits Nqo7-14
CC       constitute the membrane sector of the complex (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR   EMBL; AY972098; AAY42992.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4QSC6; -.
DR   SMR; Q4QSC6; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016655; F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor; IEA:UniProtKB-UniRule.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_01350; NDH1_NuoH; 1.
DR   InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO.
DR   InterPro; IPR018086; NADH_UbQ_OxRdtase_su1_CS.
DR   PANTHER; PTHR11432; PTHR11432; 1.
DR   Pfam; PF00146; NADHdh; 1.
DR   PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; NAD; Quinone; Translocase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..341
FT                   /note="NADH-quinone oxidoreductase subunit 8"
FT                   /id="PRO_0000240051"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        108..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        278..298
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
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