NQO1_THET8
ID NQO1_THET8 Reviewed; 438 AA.
AC Q56222; Q5SM54;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=NADH-quinone oxidoreductase subunit 1;
DE EC=7.1.1.-;
DE AltName: Full=NADH dehydrogenase I chain 1;
DE AltName: Full=NDH-1 subunit 1;
GN Name=nqo1; OrderedLocusNames=TTHA0089;
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 PARTIAL PROTEIN SEQUENCE, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY,
RP EPR 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 FMN AND 4FE-4S CLUSTER, FUNCTION, SUBUNIT, SUBCELLULAR
RP LOCATION, DOMAIN, AND 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 Nqo1 subunit contains
CC the NADH-binding site and the primary electron acceptor FMN.
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=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000269|PubMed:16469879};
CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:16469879};
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 N3. {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 -!- DOMAIN: The subunit can be separated roughly into four domains: an N-
CC terminal domain (residues 7 to 72) ending with a glycine-rich loop,
CC followed by a Rossman-fold domain (73 to 240), a ubiquitin-like domain
CC (241 to 335) and a C-terminal four-helical bundle containing cluster N3
CC (336 to 438). {ECO:0000269|PubMed:16469879}.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
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DR EMBL; U52917; AAA97943.1; -; Genomic_DNA.
DR EMBL; AP008226; BAD69912.1; -; Genomic_DNA.
DR PIR; T11903; T11903.
DR RefSeq; WP_011227700.1; NC_006461.1.
DR RefSeq; YP_143355.1; NC_006461.1.
DR PDB; 2FUG; X-ray; 3.30 A; 1/A/J/S=1-438.
DR PDB; 2YBB; EM; 19.00 A; 1=1-438.
DR PDB; 3I9V; X-ray; 3.10 A; 1/A=1-438.
DR PDB; 3IAM; X-ray; 3.10 A; 1/A=1-438.
DR PDB; 3IAS; X-ray; 3.15 A; 1/A/J/S=1-438.
DR PDB; 3M9S; X-ray; 4.50 A; 1/A=1-438.
DR PDB; 4HEA; X-ray; 3.30 A; 1/B=1-438.
DR PDB; 6I0D; X-ray; 3.60 A; 1/B=1-438.
DR PDB; 6I1P; X-ray; 3.21 A; 1/B=1-438.
DR PDB; 6Q8O; X-ray; 3.60 A; 1/B=1-438.
DR PDB; 6Q8W; X-ray; 3.40 A; 1/B=1-438.
DR PDB; 6Q8X; X-ray; 3.51 A; 1/B=1-438.
DR PDB; 6Y11; X-ray; 3.11 A; 1/B=1-438.
DR PDB; 6ZIY; EM; 4.25 A; 1=1-438.
DR PDB; 6ZJL; EM; 4.30 A; 1=1-438.
DR PDB; 6ZJN; EM; 6.10 A; 1=1-438.
DR PDB; 6ZJY; EM; 5.50 A; 1=1-438.
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; Q56222; -.
DR SMR; Q56222; -.
DR DIP; DIP-59259N; -.
DR IntAct; Q56222; 1.
DR STRING; 300852.55771471; -.
DR TCDB; 3.D.1.3.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR EnsemblBacteria; BAD69912; BAD69912; BAD69912.
DR GeneID; 3168453; -.
DR KEGG; ttj:TTHA0089; -.
DR PATRIC; fig|300852.9.peg.87; -.
DR eggNOG; COG1894; Bacteria.
DR HOGENOM; CLU_014881_0_1_0; -.
DR OMA; CREGTDW; -.
DR PhylomeDB; Q56222; -.
DR EvolutionaryTrace; Q56222; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Cell membrane; Direct protein sequencing;
KW Flavoprotein; FMN; Iron; Iron-sulfur; Membrane; Metal-binding; NAD;
KW Quinone; Reference proteome; Translocase.
FT CHAIN 1..438
FT /note="NADH-quinone oxidoreductase subunit 1"
FT /id="PRO_0000118567"
FT BINDING 66..69
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305"
FT BINDING 75
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 92..96
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000305"
FT BINDING 180..185
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 218..220
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 353
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 356
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 359
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16469879"
FT BINDING 400
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:16469879"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:6I1P"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:3IAM"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 29..34
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 35..38
FT /evidence="ECO:0007829|PDB:6Y11"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 65..68
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2FUG"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 139..154
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 185..192
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:3IAM"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 221..225
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 227..232
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 235..239
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:2FUG"
FT STRAND 244..260
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 272..277
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 278..280
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 287..291
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 293..297
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 300..302
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 313..316
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 317..319
FT /evidence="ECO:0007829|PDB:3I9V"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 337..351
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 361..365
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 366..374
FT /evidence="ECO:0007829|PDB:3I9V"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 381..394
FT /evidence="ECO:0007829|PDB:3I9V"
FT HELIX 402..426
FT /evidence="ECO:0007829|PDB:3I9V"
SQ SEQUENCE 438 AA; 48632 MW; 73ADB3AF31BBE4C0 CRC64;
MTGPILSGLD PRFERTLYAH VGKEGSWTLD YYLRHGGYET AKRVLKEKTP DEVIEEVKRS
GLRGRGGAGF PTGLKWSFMP KDDGKQHYLI CNADESEPGS FKDRYILEDV PHLLIEGMIL
AGYAIRATVG YIYVRGEYRR AADRLEQAIK EARARGYLGK NLFGTDFSFD LHVHRGAGAY
ICGEETALMN SLEGLRANPR LKPPFPAQSG LWGKPTTINN VETLASVVPI MERGADWFAQ
MGTEQSKGMK LYQISGPVKR PGVYELPMGT TFRELIYEWA GGPLEPIQAI IPGGSSTPPL
PFTEEVLDTP MSYEHLQAKG SMLGTGGVIL IPERVSMVDA MWNLTRFYAH ESCGKCTPCR
EGVAGFMVNL FAKIGTGQGE EKDVENLEAL LPLIEGRSFC PLADAAVWPV KGSLRHFKDQ
YLALAREKRP VPRPSLWR
