ID   NQO8_THET2              Reviewed;         365 AA.
AC   Q72GD5;
DT   13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   04-NOV-2008, entry version 32.
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; OrderedLocusNames=TT_C1913;
OS   Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T.,
RA   Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R.,
RA   Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R.,
RA   Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus
RT   thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
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 (By similarity).
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 (By 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; AE017221; AAS82255.1; -; Genomic_DNA.
DR   RefSeq; YP_005882.1; -.
DR   GeneID; 2775646; -.
DR   GenomeReviews; AE017221_GR; TT_C1913.
DR   HOGENOM; Q72GD5; -.
DR   BioCyc; TTHE262724:TT_C1913-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: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; Complete proteome; Membrane; NAD;
KW   Oxidoreductase; Quinone; Transmembrane; Ubiquinone.
FT   CHAIN         1    365       NADH-quinone oxidoreductase subunit 8.
FT                                /FTId=PRO_0000240113.
FT   TRANSMEM     11     31       Potential.
FT   TRANSMEM     80    100       Potential.
FT   TRANSMEM    120    140       Potential.
FT   TRANSMEM    157    177       Potential.
FT   TRANSMEM    192    212       Potential.
FT   TRANSMEM    252    272       Potential.
FT   TRANSMEM    273    293       Potential.
FT   TRANSMEM    310    330       Potential.
FT   TRANSMEM    336    356       Potential.
SQ   SEQUENCE   365 AA;  41009 MW;  5B920A702F858C0F CRC64;
     MTWSYPVDPY WMVALKALLV VVGLLTAFAF MTLIERRLLA RFQVRMGPNR VGPFGLLQPL
     ADAIKSIFKE DIVVAQADRF LFVLAPLISV VFALLAFGLI PFGPPGSFFG YQPWVINLDL
     GILYLFAVSE LAVYGIFLSG WASGSKYSLL GSLRSSASLI SYELGLGLAL LAPVLLVGSL
     NLNDIVNWQK EHGWLFLYAF PAFLVYLIAS MAEAARTPFD LPEAEQELVG GYHTEYSSIK
     WALFQMAEYI HFITASALIP TLFLGGWTMP VLEVPYLWMF LKLAFFLFFF IWIRATWFRL
     RYDQLLRFGW GFLFPLALLW FLVTALVVAL DLPRTYLLYL SALSFLVLLG AVLYTPKPAR
     KGGGA
//