NQO7_THET8
ID NQO7_THET8 Reviewed; 119 AA.
AC Q56217; Q5SM59;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=NADH-quinone oxidoreductase subunit 7;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I chain 7;
DE AltName: Full=NDH-1 subunit 7;
GN Name=nqo7; OrderedLocusNames=TTHA0084;
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 3 family. {ECO:0000305}.
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DR EMBL; U52917; AAA97938.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69907.1; -; Genomic_DNA.
DR PIR; T11898; T11898.
DR RefSeq; WP_011174272.1; NC_006461.1.
DR RefSeq; YP_143350.1; NC_006461.1.
DR PDB; 4HE8; X-ray; 3.30 A; A/B=1-119.
DR PDB; 4HEA; X-ray; 3.30 A; A/P=1-119.
DR PDB; 6I0D; X-ray; 3.60 A; A/P=1-119.
DR PDB; 6I1P; X-ray; 3.21 A; A/P=1-119.
DR PDB; 6Q8O; X-ray; 3.60 A; A/P=1-119.
DR PDB; 6Q8W; X-ray; 3.40 A; A/P=1-119.
DR PDB; 6Q8X; X-ray; 3.51 A; A/P=1-119.
DR PDB; 6Y11; X-ray; 3.11 A; A/P=1-119.
DR PDB; 6ZIY; EM; 4.25 A; A=1-119.
DR PDB; 6ZJL; EM; 4.30 A; A=1-119.
DR PDB; 6ZJN; EM; 6.10 A; A=1-119.
DR PDB; 6ZJY; EM; 5.50 A; A=1-119.
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; Q56217; -.
DR SMR; Q56217; -.
DR DIP; DIP-59265N; -.
DR IntAct; Q56217; 1.
DR STRING; 300852.55771466; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69907; BAD69907; BAD69907.
DR GeneID; 3168352; -.
DR KEGG; ttj:TTHA0084; -.
DR PATRIC; fig|300852.9.peg.82; -.
DR eggNOG; COG0838; Bacteria.
DR HOGENOM; CLU_119549_0_0_0; -.
DR OMA; RFPVKYY; -.
DR PhylomeDB; Q56217; -.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.58.1610; -; 1.
DR HAMAP; MF_01394; NDH1_NuoA; 1.
DR InterPro; IPR023043; NAD(P)H_OxRDtase_bac/plastid.
DR InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR PANTHER; PTHR11058; PTHR11058; 1.
DR Pfam; PF00507; Oxidored_q4; 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;
KW Transport.
FT CHAIN 1..119
FT /note="NADH-quinone oxidoreductase subunit 7"
FT /id="PRO_0000117861"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 88..108
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 4..30
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:4HEA"
FT HELIX 60..83
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 89..113
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 119 AA; 13145 MW; 10FFA8C204B0AFF5 CRC64;
MAPIQEYVGT LIYVGVALFI GVAALLVGAL LGPKKPGRAK LMPYESGNDP AGEVKRFPVH
FYVVAMLFIL FDVEVAFLWP YAVSAGGLGL YGFLGVLAFT LLLFVGFLYE WWKGVMRWH
