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NADH dehydrogenase (EC 1.6.99.3) (H(2)O(2)-forming NADH oxidase) (NADH:oxygen oxidoreductase)

 NOX_THET8               Reviewed;         205 AA.
Q60049; Q53306; Q5SL68;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
29-MAR-2005, sequence version 2.
07-JUN-2017, entry version 102.
RecName: Full=NADH dehydrogenase;
EC=1.6.99.3;
AltName: Full=H(2)O(2)-forming NADH oxidase;
AltName: Full=NADH:oxygen oxidoreductase;
Name=nox; OrderedLocusNames=TTHA0425;
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579).
Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
Thermus.
NCBI_TaxID=300852;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1577004; DOI=10.1111/j.1432-1033.1992.tb16852.x;
Park H.-J., Kreutzer R., Reiser C.O.A., Sprinzl M.;
"Molecular cloning and nucleotide sequence of the gene encoding a
H2O2-forming NADH oxidase from the extreme thermophilic Thermus
thermophilus HB8 and its expression in Escherichia coli.";
Eur. J. Biochem. 205:875-879(1992).
[2]
ERRATUM.
PubMed=8436145;
Park H.-J., Kreutzer R., Reiser C.O.A., Sprinzl M.;
Eur. J. Biochem. 211:909-909(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=HB8 / ATCC 27634 / DSM 579;
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y.,
Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
"Complete genome sequence of Thermus thermophilus HB8.";
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
[4]
PROTEIN SEQUENCE OF 1-32, AND CHARACTERIZATION.
PubMed=1577005; DOI=10.1111/j.1432-1033.1992.tb16853.x;
Park H.-J., Reiser C.O.A., Kondruweit S., Erdmann H., Schmid R.D.,
Sprinzl M.;
"Purification and characterization of a NADH oxidase from the
thermophile Thermus thermophilus HB8.";
Eur. J. Biochem. 205:881-885(1992).
[5]
X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) IN COMPLEX WITH FMN, AND
SUBUNIT.
PubMed=8846223; DOI=10.1038/nsb1295-1109;
Hecht H.J., Erdmann H., Park H.J., Sprinzl M., Schmid R.D.;
"Crystal structure of NADH oxidase from Thermus thermophilus.";
Nat. Struct. Biol. 2:1109-1114(1995).
-!- FUNCTION: Can oxidize either NADH or NADPH with a preference for
NADH. Can catalyze electron transfer from NADH to various electron
acceptors which include, in addition to molecular oxygen,
cytochrome c, 2,6 dichlorphenolindophenol, methylene blue,
ferricyanide or P-nitroblue tetrazolium.
-!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210;
Note=Binds 1 FMN per subunit.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 5.0.;
Temperature dependence:
Thermostable.;
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:8846223}.
-!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X60110; CAA42707.1; -; Genomic_DNA.
EMBL; S55441; AAB25458.1; -; Genomic_DNA.
EMBL; AP008226; BAD70248.1; -; Genomic_DNA.
RefSeq; WP_011227925.1; NC_006461.1.
RefSeq; YP_143691.1; NC_006461.1.
PDB; 1NOX; X-ray; 1.59 A; A=1-205.
PDBsum; 1NOX; -.
ProteinModelPortal; Q60049; -.
SMR; Q60049; -.
STRING; 300852.TTHA0425; -.
DrugBank; DB03247; Riboflavin Monophosphate.
EnsemblBacteria; BAD70248; BAD70248; BAD70248.
GeneID; 3168975; -.
KEGG; ttj:TTHA0425; -.
PATRIC; fig|300852.9.peg.425; -.
eggNOG; ENOG4108TVJ; Bacteria.
eggNOG; COG0778; LUCA.
HOGENOM; HOG000146732; -.
OMA; MFLQNIM; -.
PhylomeDB; Q60049; -.
EvolutionaryTrace; Q60049; -.
PRO; PR:Q60049; -.
Proteomes; UP000000532; Chromosome.
GO; GO:0003954; F:NADH dehydrogenase activity; IEA:UniProtKB-EC.
Gene3D; 3.40.109.10; -; 1.
InterPro; IPR029479; Nitroreductase.
InterPro; IPR000415; Nitroreductase-like.
Pfam; PF00881; Nitroreductase; 1.
SUPFAM; SSF55469; SSF55469; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Flavoprotein; FMN; NAD; Oxidoreductase; Reference proteome.
CHAIN 1 205 NADH dehydrogenase.
/FTId=PRO_0000072721.
NP_BIND 17 21 FMN. {ECO:0000269|PubMed:8846223}.
NP_BIND 158 159 FMN. {ECO:0000269|PubMed:8846223}.
BINDING 73 73 FMN. {ECO:0000269|PubMed:8846223}.
BINDING 195 195 FMN. {ECO:0000269|PubMed:8846223}.
CONFLICT 174 174 H -> R (in Ref. 1; CAA42707/AAB25458).
{ECO:0000305}.
HELIX 10 16 {ECO:0000244|PDB:1NOX}.
HELIX 30 40 {ECO:0000244|PDB:1NOX}.
HELIX 46 48 {ECO:0000244|PDB:1NOX}.
STRAND 52 57 {ECO:0000244|PDB:1NOX}.
HELIX 60 69 {ECO:0000244|PDB:1NOX}.
TURN 70 72 {ECO:0000244|PDB:1NOX}.
HELIX 75 78 {ECO:0000244|PDB:1NOX}.
STRAND 79 87 {ECO:0000244|PDB:1NOX}.
HELIX 89 94 {ECO:0000244|PDB:1NOX}.
HELIX 95 98 {ECO:0000244|PDB:1NOX}.
HELIX 107 121 {ECO:0000244|PDB:1NOX}.
HELIX 125 149 {ECO:0000244|PDB:1NOX}.
STRAND 153 157 {ECO:0000244|PDB:1NOX}.
HELIX 162 169 {ECO:0000244|PDB:1NOX}.
STRAND 176 188 {ECO:0000244|PDB:1NOX}.
HELIX 198 201 {ECO:0000244|PDB:1NOX}.
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


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