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 27-MAR-2024, entry version 147. 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; Deinococcota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 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; 3.10.20.600; -; 1. DR Gene3D; 6.10.250.1450; -; 1. DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1. DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 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 NCBIfam; TIGR01959; nuoF_fam; 1. DR PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1. DR PANTHER; PTHR43578:SF1; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1. 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; SSF142019; Nqo1 FMN-binding domain-like; 1. DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1. DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 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 //