ID NOX_THET8 Reviewed; 205 AA. AC Q60049; Q53306; Q5SL68; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 27-MAR-2024, entry version 123. DE RecName: Full=NADH dehydrogenase; DE EC=7.1.1.2; DE AltName: Full=H(2)O(2)-forming NADH oxidase; DE AltName: Full=NADH:oxygen oxidoreductase; GN Name=nox; OrderedLocusNames=TTHA0425; 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]. RX PubMed=1577004; DOI=10.1111/j.1432-1033.1992.tb16852.x; RA Park H.-J., Kreutzer R., Reiser C.O.A., Sprinzl M.; RT "Molecular cloning and nucleotide sequence of the gene encoding a H2O2- RT forming NADH oxidase from the extreme thermophilic Thermus thermophilus HB8 RT and its expression in Escherichia coli."; RL Eur. J. Biochem. 205:875-879(1992). RN [2] RP ERRATUM OF PUBMED:1577004. RX PubMed=8436145; RA Park H.-J., Kreutzer R., Reiser C.O.A., Sprinzl M.; RL Eur. J. Biochem. 211:909-909(1993). RN [3] 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 [4] RP PROTEIN SEQUENCE OF 1-32, AND CHARACTERIZATION. RX PubMed=1577005; DOI=10.1111/j.1432-1033.1992.tb16853.x; RA Park H.-J., Reiser C.O.A., Kondruweit S., Erdmann H., Schmid R.D., RA Sprinzl M.; RT "Purification and characterization of a NADH oxidase from the thermophile RT Thermus thermophilus HB8."; RL Eur. J. Biochem. 205:881-885(1992). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) IN COMPLEX WITH FMN, AND SUBUNIT. RX PubMed=8846223; DOI=10.1038/nsb1295-1109; RA Hecht H.J., Erdmann H., Park H.J., Sprinzl M., Schmid R.D.; RT "Crystal structure of NADH oxidase from Thermus thermophilus."; RL Nat. Struct. Biol. 2:1109-1114(1995). CC -!- FUNCTION: Can oxidize either NADH or NADPH with a preference for NADH. CC Can catalyze electron transfer from NADH to various electron acceptors CC which include, in addition to molecular oxygen, cytochrome c, 2,6 CC dichlorphenolindophenol, methylene blue, ferricyanide or P-nitroblue CC tetrazolium. CC -!- CATALYTIC ACTIVITY: CC Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + CC NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA- CC COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Note=Binds 1 FMN per subunit.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.0.; CC Temperature dependence: CC Thermostable.; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8846223}. CC -!- SIMILARITY: Belongs to the nitroreductase family. {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; X60110; CAA42707.1; -; Genomic_DNA. DR EMBL; S55441; AAB25458.1; -; Genomic_DNA. DR EMBL; AP008226; BAD70248.1; -; Genomic_DNA. DR RefSeq; WP_011227925.1; NC_006461.1. DR RefSeq; YP_143691.1; NC_006461.1. DR PDB; 1NOX; X-ray; 1.59 A; A=1-205. DR PDBsum; 1NOX; -. DR AlphaFoldDB; Q60049; -. DR SMR; Q60049; -. DR DrugBank; DB03247; Flavin mononucleotide. DR EnsemblBacteria; BAD70248; BAD70248; BAD70248. DR GeneID; 3168975; -. DR KEGG; ttj:TTHA0425; -. DR PATRIC; fig|300852.9.peg.425; -. DR eggNOG; COG0778; Bacteria. DR HOGENOM; CLU_070764_4_2_0; -. DR PhylomeDB; Q60049; -. DR EvolutionaryTrace; Q60049; -. DR PRO; PR:Q60049; -. DR Proteomes; UP000000532; Chromosome. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR CDD; cd03370; nitroreductase; 1. DR Gene3D; 3.40.109.10; NADH Oxidase; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR PANTHER; PTHR43673; NAD(P)H NITROREDUCTASE YDGI-RELATED; 1. DR PANTHER; PTHR43673:SF10; PROTEIN DRGA; 1. DR Pfam; PF00881; Nitroreductase; 1. DR SUPFAM; SSF55469; FMN-dependent nitroreductase-like; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Flavoprotein; FMN; NAD; KW Oxidoreductase; Reference proteome; Translocase. FT CHAIN 1..205 FT /note="NADH dehydrogenase" FT /id="PRO_0000072721" FT BINDING 17..21 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:8846223" FT BINDING 73 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:8846223" FT BINDING 158..159 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:8846223" FT BINDING 195 FT /ligand="FMN" FT /ligand_id="ChEBI:CHEBI:58210" FT /evidence="ECO:0000269|PubMed:8846223" FT CONFLICT 174 FT /note="H -> R (in Ref. 1; CAA42707/AAB25458)" FT /evidence="ECO:0000305" FT HELIX 10..16 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 30..40 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 46..48 FT /evidence="ECO:0007829|PDB:1NOX" FT STRAND 52..57 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 60..69 FT /evidence="ECO:0007829|PDB:1NOX" FT TURN 70..72 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 75..78 FT /evidence="ECO:0007829|PDB:1NOX" FT STRAND 79..87 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 89..94 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 95..98 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 107..121 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 125..149 FT /evidence="ECO:0007829|PDB:1NOX" FT STRAND 153..157 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 162..169 FT /evidence="ECO:0007829|PDB:1NOX" FT STRAND 176..188 FT /evidence="ECO:0007829|PDB:1NOX" FT HELIX 198..201 FT /evidence="ECO:0007829|PDB:1NOX" SQ SEQUENCE 205 AA; 22730 MW; 012742DFA85B50E5 CRC64; MEATLPVLDA KTAALKRRSI RRYRKDPVPE GLLREILEAA LRAPSAWNLQ PWRIVVVRDP ATKRALREAA FGQAHVEEAP VVLVLYADLE DALAHLDEVI HPGVQGERRE AQKQAIQRAF AAMGQEARKA WASGQSYILL GYLLLLLEAY GLGSVPMLGF DPERVRAILG LPSHAAIPAL VALGYPAEEG YPSHRLPLER VVLWR //