NQO10_THET8
ID NQO10_THET8 Reviewed; 176 AA.
AC Q56225; Q5SM50;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=NADH-quinone oxidoreductase subunit 10;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I chain 10;
DE AltName: Full=NDH-1 subunit 10;
GN Name=nqo10; OrderedLocusNames=TTHA0093;
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 6 family. {ECO:0000305}.
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DR EMBL; U52917; AAA97947.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69916.1; -; Genomic_DNA.
DR PIR; T11907; T11907.
DR RefSeq; WP_011227703.1; NC_006461.1.
DR RefSeq; YP_143359.1; NC_006461.1.
DR PDB; 4HE8; X-ray; 3.30 A; D/J=1-176.
DR PDB; 4HEA; X-ray; 3.30 A; J/R=1-176.
DR PDB; 6I0D; X-ray; 3.60 A; J/R=1-176.
DR PDB; 6I1P; X-ray; 3.21 A; J/R=1-176.
DR PDB; 6Q8O; X-ray; 3.60 A; J/R=1-176.
DR PDB; 6Q8W; X-ray; 3.40 A; J/R=1-176.
DR PDB; 6Q8X; X-ray; 3.51 A; J/R=1-176.
DR PDB; 6Y11; X-ray; 3.11 A; J/R=1-176.
DR PDB; 6ZIY; EM; 4.25 A; J=1-176.
DR PDB; 6ZJL; EM; 4.30 A; J=1-176.
DR PDB; 6ZJN; EM; 6.10 A; J=1-176.
DR PDB; 6ZJY; EM; 5.50 A; J=1-176.
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; Q56225; -.
DR SMR; Q56225; -.
DR DIP; DIP-59268N; -.
DR IntAct; Q56225; 15.
DR STRING; 300852.55771475; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69916; BAD69916; BAD69916.
DR GeneID; 3169626; -.
DR KEGG; ttj:TTHA0093; -.
DR PATRIC; fig|300852.9.peg.91; -.
DR eggNOG; COG0839; Bacteria.
DR HOGENOM; CLU_085957_4_1_0; -.
DR OMA; MLVNKRE; -.
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; 1.20.120.1200; -; 1.
DR InterPro; IPR001457; NADH_UbQ/plastoQ_OxRdtase_su6.
DR InterPro; IPR042106; Nuo/plastoQ_OxRdtase_6_NuoJ.
DR Pfam; PF00499; Oxidored_q3; 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..176
FT /note="NADH-quinone oxidoreductase subunit 10"
FT /id="PRO_0000118369"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 26..46
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT HELIX 2..21
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 25..45
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 49..57
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 63..73
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 76..79
FT /evidence="ECO:0007829|PDB:4HE8"
FT HELIX 89..108
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 124..131
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 136..157
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 176 AA; 18551 MW; 802325655FE3AAB1 CRC64;
MSLLEGLALF LLLLSGVLVV TLRNAIHAAL ALILNFLVLA GVYVALDARF LGFIQVIVYA
GAIVVLFLFV IMLLFAAQGE IGFDPLVRSR PLAALLALGV AGILAAGLWG LDLAFTQDLK
GGLPQALGPL LYGDWLFVLL AVGFLLMAAT VVAVALVEPG KASRAKEAEK REEVAR
