NQO5_THET8
ID NQO5_THET8 Reviewed; 207 AA.
AC Q56219; Q5SM57;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 133.
DE RecName: Full=NADH-quinone oxidoreductase subunit 5;
DE EC=7.1.1.- {ECO:0000255|HAMAP-Rule:MF_01357, ECO:0000269|PubMed:16469879};
DE AltName: Full=NADH dehydrogenase I chain 5;
DE AltName: Full=NDH-1 subunit 5;
GN Name=nqo5; OrderedLocusNames=TTHA0086;
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.
RN [3]
RP PROTEIN SEQUENCE OF 1-8, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND
RP SUBUNIT.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=16584177; DOI=10.1021/bi0600998;
RA Hinchliffe P., Carroll J., Sazanov L.A.;
RT "Identification of a novel subunit of respiratory complex I from Thermus
RT thermophilus.";
RL Biochemistry 45:4413-4420(2006).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF ENZYME HYDROPHILIC DOMAIN,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND ELECTRON
RP TRANSFER MECHANISM.
RX PubMed=16469879; DOI=10.1126/science.1123809;
RA Sazanov L.A., Hinchliffe P.;
RT "Structure of the hydrophilic domain of respiratory complex I from Thermus
RT thermophilus.";
RL Science 311:1430-1436(2006).
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. The Nqo5 subunit may be
CC involved in the stabilization of the complex.
CC {ECO:0000269|PubMed:16469879, ECO:0000269|PubMed:16584177}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01357,
CC ECO:0000269|PubMed:16469879};
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. The N-terminal domain of this subunit
CC (residues 1 to 153) wraps around Nqo4 on one side, and the subunit
CC interacts also with Nqo9 via a two-stranded beta sheet (residues 154 to
CC 171) and with Nqo3 via an extended C-terminal loop (residues 172 to
CC 196). {ECO:0000269|PubMed:16469879, ECO:0000269|PubMed:16584177}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:16469879};
CC Peripheral membrane protein {ECO:0000305|PubMed:16469879}; Cytoplasmic
CC side {ECO:0000305|PubMed:16469879}.
CC -!- SIMILARITY: Belongs to the complex I 30 kDa subunit family.
CC {ECO:0000255|HAMAP-Rule:MF_01357}.
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DR EMBL; U52917; AAA97940.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69909.1; -; Genomic_DNA.
DR PIR; T11900; T11900.
DR RefSeq; WP_011174270.1; NC_006461.1.
DR RefSeq; YP_143352.1; NC_006461.1.
DR PDB; 2FUG; X-ray; 3.30 A; 5/E/N/W=1-207.
DR PDB; 2YBB; EM; 19.00 A; 5=1-207.
DR PDB; 3I9V; X-ray; 3.10 A; 5/E=1-207.
DR PDB; 3IAM; X-ray; 3.10 A; 5/E=1-207.
DR PDB; 3IAS; X-ray; 3.15 A; 5/E/N/W=1-207.
DR PDB; 3M9S; X-ray; 4.50 A; 5/E=1-207.
DR PDB; 4HEA; X-ray; 3.30 A; 5/F=1-207.
DR PDB; 5B3P; X-ray; 1.65 A; A=1-134.
DR PDB; 5B3Q; X-ray; 3.00 A; A=1-134.
DR PDB; 6I0D; X-ray; 3.60 A; 5/F=1-207.
DR PDB; 6I1P; X-ray; 3.21 A; 5/F=1-207.
DR PDB; 6Q8O; X-ray; 3.60 A; 5/F=1-207.
DR PDB; 6Q8W; X-ray; 3.40 A; 5/F=1-207.
DR PDB; 6Q8X; X-ray; 3.51 A; 5/F=1-207.
DR PDB; 6Y11; X-ray; 3.11 A; 5/F=1-207.
DR PDB; 6ZIY; EM; 4.25 A; 5=1-207.
DR PDB; 6ZJL; EM; 4.30 A; 5=1-207.
DR PDB; 6ZJN; EM; 6.10 A; 5=1-207.
DR PDB; 6ZJY; EM; 5.50 A; 5=1-207.
DR PDBsum; 2FUG; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 3I9V; -.
DR PDBsum; 3IAM; -.
DR PDBsum; 3IAS; -.
DR PDBsum; 3M9S; -.
DR PDBsum; 4HEA; -.
DR PDBsum; 5B3P; -.
DR PDBsum; 5B3Q; -.
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; Q56219; -.
DR SMR; Q56219; -.
DR DIP; DIP-59263N; -.
DR IntAct; Q56219; 1.
DR STRING; 300852.55771468; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69909; BAD69909; BAD69909.
DR GeneID; 3168317; -.
DR KEGG; ttj:TTHA0086; -.
DR PATRIC; fig|300852.9.peg.84; -.
DR eggNOG; COG0852; Bacteria.
DR HOGENOM; CLU_042628_5_0_0; -.
DR OMA; PTLFKEG; -.
DR PhylomeDB; Q56219; -.
DR EvolutionaryTrace; Q56219; -.
DR Proteomes; UP000000532; Chromosome.
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; 3.30.460.80; -; 1.
DR HAMAP; MF_01357; NDH1_NuoC; 1.
DR InterPro; IPR010218; NADH_DH_suC.
DR InterPro; IPR037232; NADH_quin_OxRdtase_su_C/D-like.
DR InterPro; IPR001268; NADH_UbQ_OxRdtase_30kDa_su.
DR InterPro; IPR020396; NADH_UbQ_OxRdtase_CS.
DR Pfam; PF00329; Complex1_30kDa; 1.
DR SUPFAM; SSF143243; SSF143243; 1.
DR PROSITE; PS00542; COMPLEX1_30K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; Membrane; NAD;
KW Quinone; Reference proteome; Translocase; Transport.
FT CHAIN 1..207
FT /note="NADH-quinone oxidoreductase subunit 5"
FT /id="PRO_0000118669"
FT HELIX 2..13
FT /evidence="ECO:0007829|PDB:5B3P"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5B3P"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5B3P"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:5B3P"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:5B3P"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:5B3P"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5B3Q"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:5B3P"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:5B3Q"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5B3P"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:5B3Q"
FT STRAND 100..102
FT /evidence="ECO:0007829|PDB:5B3P"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5B3P"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:5B3P"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:5B3P"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:3IAS"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:2FUG"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:2FUG"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3IAS"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:3I9V"
SQ SEQUENCE 207 AA; 23859 MW; EB6891BEF6F314AD CRC64;
MRLERVLEEA RAKGYPIEDN GLGNLWVVLP RERFKEEMAH YKAMGFNFLA DIVGLDYLTY
PDPRPERFAV VYELVSLPGW KDGDGSRFFV RVYVPEEDPR LPTVTDLWGS ANFLEREVYD
LFGIVFEGHP DLRKILTPED LEGHPLRKDY PLGETPTLFR EGRYIIPAEF RAALTGKDPG
LTFYKGGSRK GYRSLWADLK KAREVKG
