NOX_THET8
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 03-AUG-2022, entry version 118.
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; Deinococcus-Thermus; 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}.
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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 STRING; 300852.55771807; -.
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 OMA; MFLQNIM; -.
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 Gene3D; 3.40.109.10; -; 1.
DR InterPro; IPR029479; Nitroreductase.
DR InterPro; IPR000415; Nitroreductase-like.
DR Pfam; PF00881; Nitroreductase; 1.
DR SUPFAM; SSF55469; SSF55469; 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
