NQO9_THET8
ID NQO9_THET8 Reviewed; 182 AA.
AC Q56224; Q5SM51;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=NADH-quinone oxidoreductase subunit 9;
DE EC=7.1.1.- {ECO:0000269|PubMed:16469879};
DE AltName: Full=NADH dehydrogenase I subunit 9;
DE AltName: Full=NDH-1 subunit 9;
GN Name=nqo9; OrderedLocusNames=TTHA0092;
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 IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, AND 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 IN
RP COMPLEX WITH 4FE-4S CLUSTER, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP ELECTRON 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 role of the Nqo9
CC subunit appears to provide a 'connecting chain' of two clusters between
CC cluster N5 and the terminal cluster N2, and to stabilize the structure
CC of the complex by interacting with other subunits.
CC {ECO:0000269|PubMed:16469879, ECO:0000269|Ref.2}.
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:0000269|PubMed:16469879};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:16469879};
CC Note=Binds 2 [4Fe-4S] clusters per subunit. The [4Fe-4S] clusters are
CC referred to as N6a and N6b. {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. {ECO:0000269|PubMed:16469879,
CC 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 23 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U52917; AAA97946.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69915.1; -; Genomic_DNA.
DR PIR; T11906; T11906.
DR RefSeq; WP_011174264.1; NC_006461.1.
DR RefSeq; YP_143358.1; NC_006461.1.
DR PDB; 2FUG; X-ray; 3.30 A; 9/G/P/Y=1-182.
DR PDB; 2YBB; EM; 19.00 A; 8=1-182.
DR PDB; 3I9V; X-ray; 3.10 A; 9/G=1-182.
DR PDB; 3IAM; X-ray; 3.10 A; 9/G=1-182.
DR PDB; 3IAS; X-ray; 3.15 A; 9/G/P/Y=1-182.
DR PDB; 3M9S; X-ray; 4.50 A; 9/G=1-182.
DR PDB; 4HEA; X-ray; 3.30 A; 9/O=1-182.
DR PDB; 6I0D; X-ray; 3.60 A; 9/O=1-182.
DR PDB; 6I1P; X-ray; 3.21 A; 9/O=1-182.
DR PDB; 6Q8O; X-ray; 3.60 A; 9/O=1-182.
DR PDB; 6Q8W; X-ray; 3.40 A; 9/O=1-182.
DR PDB; 6Q8X; X-ray; 3.51 A; 9/O=1-182.
DR PDB; 6Y11; X-ray; 3.11 A; 9/O=1-182.
DR PDB; 6ZIY; EM; 4.25 A; 9=1-182.
DR PDB; 6ZJL; EM; 4.30 A; 9=1-182.
DR PDB; 6ZJN; EM; 6.10 A; 9=1-182.
DR PDB; 6ZJY; EM; 5.50 A; 9=1-182.
DR PDBsum; 2FUG; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 3I9V; -.
DR PDBsum; 3IAM; -.
DR PDBsum; 3IAS; -.
DR PDBsum; 3M9S; -.
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; Q56224; -.
DR SMR; Q56224; -.
DR DIP; DIP-59267N; -.
DR IntAct; Q56224; 1.
DR STRING; 300852.55771474; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69915; BAD69915; BAD69915.
DR GeneID; 3167944; -.
DR KEGG; ttj:TTHA0092; -.
DR PATRIC; fig|300852.9.peg.90; -.
DR eggNOG; COG1143; Bacteria.
DR HOGENOM; CLU_067218_4_3_0; -.
DR OMA; VDTPHAI; -.
DR PhylomeDB; Q56224; -.
DR EvolutionaryTrace; Q56224; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050136; F:NADH dehydrogenase (quinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR HAMAP; MF_01351; NDH1_NuoI; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR010226; NADH_quinone_OxRdtase_chainI.
DR PANTHER; PTHR10849; PTHR10849; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR TIGRFAMs; TIGR01971; NuoI; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 2.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell membrane; Iron; Iron-sulfur; Membrane;
KW Metal-binding; NAD; Quinone; Reference proteome; Repeat; Translocase.
FT CHAIN 1..182
FT /note="NADH-quinone oxidoreductase subunit 9"
FT /id="PRO_0000118721"
FT DOMAIN 43..73
FT /note="4Fe-4S ferredoxin-type 1"
FT DOMAIN 89..118
FT /note="4Fe-4S ferredoxin-type 2"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 57
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 63
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 98
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 101
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 104
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 108
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:16469879"
FT HELIX 4..18
FT /evidence="ECO:0007829|PDB:6Y11"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 103..107
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:4HEA"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 144..149
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 150..153
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:3I9V"
SQ SEQUENCE 182 AA; 20080 MW; 054A9F7942C64C66 CRC64;
MTLKALAQSL GITLKYLFSK PVTVPYPDAP VALKPRFHGR HVLTRHPNGL EKCIGCSLCA
AACPAYAIYV EPAENDPENP VSAGERYAKV YEINMLRCIF CGLCEEACPT GAIVLGYDFE
MADYEYSDLV YGKEDMLVDV VGTKPQRREA KRTGKPVKVG YVVPYVRPEL EGFKAPTEGG
KR
