NQO8_THET8
ID NQO8_THET8 Reviewed; 365 AA.
AC Q60019; Q5SM52;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 126.
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; OrderedLocusNames=TTHA0091;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX 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 sequence of
RT the gene cluster and thermostable properties of the expressed NQO2
RT subunit.";
RL J. Biol. Chem. 272:4201-4211(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA 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-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC electron acceptor for the enzyme in this species is menaquinone.
CC Couples the redox reaction to proton translocation (for every two
CC electrons transferred, four hydrogen ions are translocated across the
CC cytoplasmic membrane), and thus conserves the redox energy in a proton
CC gradient required for the synthesis of ATP.
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 15 different subunits, Nqo1 to Nqo15. The
CC complex has a L-shaped structure, with the hydrophobic arm (subunits
CC Nqo7, Nqo8 and Nqo10 to Nqo14) embedded in the membrane and the
CC hydrophilic peripheral arm (subunits Nqo1 to Nqo6, Nqo9 and Nqo15)
CC protruding into the bacterial cytoplasm. The hydrophilic domain
CC contains all the redox centers.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. {ECO:0000305}.
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DR EMBL; U52917; AAA97945.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69914.1; -; Genomic_DNA.
DR PIR; T11905; T11905.
DR RefSeq; WP_011227702.1; NC_006461.1.
DR RefSeq; YP_143357.1; NC_006461.1.
DR PDB; 4HE8; X-ray; 3.30 A; C/H=1-365.
DR PDB; 4HEA; X-ray; 3.30 A; H/Q=1-365.
DR PDB; 6I0D; X-ray; 3.60 A; H/Q=1-365.
DR PDB; 6I1P; X-ray; 3.21 A; H/Q=1-365.
DR PDB; 6Q8O; X-ray; 3.60 A; H/Q=1-365.
DR PDB; 6Q8W; X-ray; 3.40 A; H/Q=1-365.
DR PDB; 6Q8X; X-ray; 3.51 A; H/Q=1-365.
DR PDB; 6Y11; X-ray; 3.11 A; H/Q=1-365.
DR PDB; 6ZIY; EM; 4.25 A; H=1-365.
DR PDB; 6ZJL; EM; 4.30 A; H=1-365.
DR PDB; 6ZJN; EM; 6.10 A; H=1-365.
DR PDB; 6ZJY; EM; 5.50 A; H=1-365.
DR PDBsum; 4HE8; -.
DR PDBsum; 4HEA; -.
DR PDBsum; 6I0D; -.
DR PDBsum; 6I1P; -.
DR PDBsum; 6Q8O; -.
DR PDBsum; 6Q8W; -.
DR PDBsum; 6Q8X; -.
DR PDBsum; 6Y11; -.
DR PDBsum; 6ZIY; -.
DR PDBsum; 6ZJL; -.
DR PDBsum; 6ZJN; -.
DR PDBsum; 6ZJY; -.
DR AlphaFoldDB; Q60019; -.
DR SMR; Q60019; -.
DR DIP; DIP-59266N; -.
DR IntAct; Q60019; 1.
DR STRING; 300852.55771473; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69914; BAD69914; BAD69914.
DR GeneID; 3169634; -.
DR KEGG; ttj:TTHA0091; -.
DR PATRIC; fig|300852.9.peg.89; -.
DR eggNOG; COG1005; Bacteria.
DR HOGENOM; CLU_015134_0_0_0; -.
DR OMA; WSGWASN; -.
DR PhylomeDB; Q60019; -.
DR Proteomes; UP000000532; Chromosome.
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; PS00667; COMPLEX1_ND1_1; 1.
DR PROSITE; PS00668; COMPLEX1_ND1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane; NAD; Quinone;
KW Reference proteome; Translocase; Transmembrane; Transmembrane helix.
FT CHAIN 1..365
FT /note="NADH-quinone oxidoreductase subunit 8"
FT /id="PRO_0000117522"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 120..140
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 336..356
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 10..42
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:6I1P"
FT STRAND 50..55
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 79..94
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:6I1P"
FT TURN 105..109
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 121..142
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 146..177
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 182..191
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 196..212
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 213..215
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 220..222
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 231..235
FT /evidence="ECO:0007829|PDB:4HEA"
FT HELIX 240..262
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 277..296
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 303..311
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 313..330
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 335..350
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 365 AA; 41009 MW; AE920CC029333C09 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 LKIAFFLFFF IWIRATWFRL
RYDQLLRFGW GFLFPLALLW FLVTALVVAL DLPRTYLLYL SALSFLVLLG AVLYTPKPAR
KGGGA
