ID   NQO12_THET8             Reviewed;         606 AA.
AC   Q56227; Q5SM48;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   04-NOV-2008, entry version 50.
DE   RecName: Full=NADH-quinone oxidoreductase subunit 12;
DE            EC=1.6.99.5;
DE   AltName: Full=NADH dehydrogenase I chain 12;
DE   AltName: Full=NDH-1 subunit 12;
GN   Name=nqo12; OrderedLocusNames=TTHA0095;
OS   Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97172490; PubMed=9020134; DOI=10.1074/jbc.272.7.4201;
RA   Yano T., Chu S.S., Sled' V.D., Ohnishi T., Yagi T.;
RT   "The proton-translocating NADH-quinone oxidoreductase (NDH-1) of
RT   thermophilic bacterium Thermus thermophilus HB-8. Complete DNA
RT   sequence of the gene cluster and thermostable properties of the
RT   expressed NQO2 subunit.";
RL   J. Biol. Chem. 272:4201-4211(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
RA   Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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       menaquinone. Couples the redox reaction to proton translocation
CC       (for every two electrons transferred, four hydrogen ions are
CC       translocated across the cytoplasmic membrane), and thus conserves
CC       the redox energy in a proton gradient required for the synthesis
CC       of ATP.
CC   -!- CATALYTIC ACTIVITY: NADH + quinone = NAD(+) + quinol.
CC   -!- SUBUNIT: NDH-1 is composed of 15 different subunits, nqo1 to
CC       nqo15. The complex has a L-shaped structure, with the hydrophobic
CC       arm (subunits nqo7, nqo8 and nqo10 to nqo14) embedded in the
CC       membrane and the hydrophilic peripheral arm (subunits nqo1 to
CC       nqo6, nqo9 and nqo15) 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 5 family.
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DR   EMBL; U52917; AAA97949.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD69918.1; -; Genomic_DNA.
DR   PIR; T11909; T11909.
DR   RefSeq; YP_143361.1; -.
DR   GeneID; 3169613; -.
DR   GenomeReviews; AP008226_GR; TTHA0095.
DR   KEGG; ttj:TTHA0095; -.
DR   NMPDR; fig|300852.3.peg.126; -.
DR   HOGENOM; Q56227; -.
DR   BioCyc; TTHE300852:TTHA0095-MON; -.
DR   GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR   InterPro; IPR003945; NADHpl_OxRdtase_5.
DR   InterPro; IPR003916; NADHub_OxRdtase_5.
DR   InterPro; IPR001750; Oxidored_q1.
DR   InterPro; IPR001516; OxRdtase_q1_N.
DR   Pfam; PF00361; Oxidored_q1; 1.
DR   Pfam; PF00662; Oxidored_q1_N; 1.
DR   PRINTS; PR01434; NADHDHGNASE5.
DR   PRINTS; PR01435; NPOXDRDTASE5.
DR   TIGRFAMs; TIGR01974; NDH_I_L; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane; NAD;
KW   Oxidoreductase; Quinone; Transmembrane.
FT   CHAIN         1    606       NADH-quinone oxidoreductase subunit 12.
FT                                /FTId=PRO_0000118212.
FT   TRANSMEM      1     21       Potential.
FT   TRANSMEM     29     49       Potential.
FT   TRANSMEM     75     95       Potential.
FT   TRANSMEM    104    124       Potential.
FT   TRANSMEM    126    146       Potential.
FT   TRANSMEM    165    185       Potential.
FT   TRANSMEM    206    226       Potential.
FT   TRANSMEM    234    254       Potential.
FT   TRANSMEM    266    286       Potential.
FT   TRANSMEM    303    323       Potential.
FT   TRANSMEM    325    345       Potential.
FT   TRANSMEM    364    384       Potential.
FT   TRANSMEM    397    417       Potential.
FT   TRANSMEM    441    461       Potential.
FT   TRANSMEM    492    512       Potential.
FT   TRANSMEM    584    604       Potential.
SQ   SEQUENCE   606 AA;  65141 MW;  47318E8F2665295C CRC64;
     MALLGTILLP LLGFALLGLF GKRMREPLPG VLASGLVLAS FLLGAGLLLS GGARFQAEWL
     PGIPFSLLLD NLSGFMLLIV TGVGFLIHVY AIGYMGGDPG YSRFFAYFNL FIAMMLTLVL
     ADSYPVMFIG WEGVGLASFL LIGFWYKNPQ YADSARKAFI VNRIGDLGFM LGMAILWALY
     GTLSISELKE AMEGPLKNPD LLALAGLLLF LGAVGKSAQI PLMVWLPDAM AGPTPVSALI
     HAATMVTAGV YLIARSSFLY SVLPDVSYAI AVVGLLTAAY GALSAFGQTD IKKIVAYSTI
     SQLGYMFLAA GVGAYWVALF HVFTHAFFKA LLFLASGSVI HALGGEQDVR KMGGLWKHLP
     QTRWHALIGA LALGGLPLLS GFWSKDAILA ATLTYPFGGV GFYVGALLVA VLTAMYAMRW
     FVLVFLGEER GHHHPHEAPP VMLWPNHLLA LGSVLAGYLA LPHPLPNVLE PFLKPALAEV
     EAHHLSLGAE WGLIALSAAV ALLGLWAGFV FFQRKVFPAW YLAFEAASRE AFYVDRAYNA
     LIVNPLKALA EALFYGDRGL LSGYFGLGGA ARSLGQGLAR LQTGYLRVYA LLFVLGALLL
     LGVMRW
//