NQO6_THET8
ID NQO6_THET8 Reviewed; 181 AA.
AC Q56218; Q5SM58;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=NADH-quinone oxidoreductase subunit 6;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I subunit 6;
DE AltName: Full=NDH-1 subunit 6;
GN Name=nqo6; OrderedLocusNames=TTHA0085;
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 2-9, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, EPR
RP SPECTROSCOPY, 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.
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 -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000269|PubMed:16469879};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. This [4Fe-4S] cluster is
CC referred to as N2. {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. This subunit interacts extensively with
CC Nqo4. {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 20 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U52917; AAA97939.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69908.1; -; Genomic_DNA.
DR PIR; T11899; T11899.
DR RefSeq; WP_011174271.1; NC_006461.1.
DR RefSeq; YP_143351.1; NC_006461.1.
DR PDB; 2FUG; X-ray; 3.30 A; 6/F/O/X=1-181.
DR PDB; 2YBB; EM; 19.00 A; 6=1-181.
DR PDB; 3I9V; X-ray; 3.10 A; 6/F=1-181.
DR PDB; 3IAM; X-ray; 3.10 A; 6/F=1-181.
DR PDB; 3IAS; X-ray; 3.15 A; 6/F/O/X=1-181.
DR PDB; 3M9S; X-ray; 4.50 A; 6/F=1-181.
DR PDB; 4HEA; X-ray; 3.30 A; 6/G=1-181.
DR PDB; 6I0D; X-ray; 3.60 A; 6/G=1-181.
DR PDB; 6I1P; X-ray; 3.21 A; 6/G=1-181.
DR PDB; 6Q8O; X-ray; 3.60 A; 6/G=1-181.
DR PDB; 6Q8W; X-ray; 3.40 A; 6/G=1-181.
DR PDB; 6Q8X; X-ray; 3.51 A; 6/G=1-181.
DR PDB; 6Y11; X-ray; 3.11 A; 6/G=1-181.
DR PDB; 6ZIY; EM; 4.25 A; 6=1-181.
DR PDB; 6ZJL; EM; 4.30 A; 6=1-181.
DR PDB; 6ZJN; EM; 6.10 A; 6=1-181.
DR PDB; 6ZJY; EM; 5.50 A; 6=1-181.
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; Q56218; -.
DR SMR; Q56218; -.
DR DIP; DIP-59264N; -.
DR IntAct; Q56218; 1.
DR STRING; 300852.55771467; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69908; BAD69908; BAD69908.
DR GeneID; 3168381; -.
DR KEGG; ttj:TTHA0085; -.
DR PATRIC; fig|300852.9.peg.83; -.
DR eggNOG; COG0377; Bacteria.
DR HOGENOM; CLU_055737_7_3_0; -.
DR OMA; AGWVRKS; -.
DR PhylomeDB; Q56218; -.
DR EvolutionaryTrace; Q56218; -.
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:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR HAMAP; MF_01356; NDH1_NuoB; 1.
DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su.
DR Pfam; PF01058; Oxidored_q6; 1.
DR TIGRFAMs; TIGR01957; nuoB_fam; 1.
DR PROSITE; PS01150; COMPLEX1_20K; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell membrane; Direct protein sequencing; Iron;
KW Iron-sulfur; Membrane; Metal-binding; NAD; Quinone; Reference proteome;
KW Translocase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:16584177"
FT CHAIN 2..181
FT /note="NADH-quinone oxidoreductase subunit 6"
FT /id="PRO_0000118763"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 46
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 111
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 140
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16469879"
FT HELIX 19..32
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 46..50
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 51..56
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:6Y11"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 86..88
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 89..97
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 105..108
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:3IAM"
FT HELIX 127..129
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 139..141
FT /evidence="ECO:0007829|PDB:3IAM"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:2FUG"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:2FUG"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6Y11"
SQ SEQUENCE 181 AA; 20239 MW; A1E030366E6692F1 CRC64;
MALKDLFERD VQELEREGIL FTTLEKLVAW GRSNSLWPAT FGLACCAIEM MASTDARNDL
ARFGSEVFRA SPRQADVMIV AGRLSKKMAP VMRRVWEQMP DPKWVISMGA CASSGGMFNN
YAIVQNVDSV VPVDVYVPGC PPRPEALIYA VMQLQKKVRG QAYNERGERL PPVAAWKRTR
G
