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Q60049

- NOX_THET8

UniProt

Q60049 - NOX_THET8

Protein

NADH dehydrogenase

Gene

nox

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 86 (01 Oct 2014)
      Sequence version 2 (29 Mar 2005)
      Previous versions | rss
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    Functioni

    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 activityi

    NADH + acceptor = NAD+ + reduced acceptor.

    Cofactori

    Binds 1 FMN per subunit.

    pH dependencei

    Optimum pH is 5.0.

    Temperature dependencei

    Thermostable.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei73 – 731FMN1 Publication
    Binding sitei195 – 1951FMN1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi17 – 215FMN1 Publication
    Nucleotide bindingi158 – 1592FMN1 Publication

    GO - Molecular functioni

    1. NADH dehydrogenase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Flavoprotein, FMN, NAD

    Enzyme and pathway databases

    BioCyciTTHE300852:GH8R-446-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH dehydrogenase (EC:1.6.99.3)
    Alternative name(s):
    H(2)O(2)-forming NADH oxidase
    NADH:oxygen oxidoreductase
    Gene namesi
    Name:nox
    Ordered Locus Names:TTHA0425
    OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
    Taxonomic identifieri300852 [NCBI]
    Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
    ProteomesiUP000000532: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205NADH dehydrogenasePRO_0000072721Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi300852.TTHA0425.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 167
    Helixi30 – 4011
    Helixi46 – 483
    Beta strandi52 – 576
    Helixi60 – 6910
    Turni70 – 723
    Helixi75 – 784
    Beta strandi79 – 879
    Helixi89 – 946
    Helixi95 – 984
    Helixi107 – 12115
    Helixi125 – 14925
    Beta strandi153 – 1575
    Helixi162 – 1698
    Beta strandi176 – 18813
    Helixi198 – 2014

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1NOXX-ray1.59A1-205[»]
    ProteinModelPortaliQ60049.
    SMRiQ60049. Positions 6-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ60049.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the nitroreductase family.Curated

    Phylogenomic databases

    eggNOGiCOG0778.
    HOGENOMiHOG000146732.
    OMAiANYPRSM.
    OrthoDBiEOG6N947Z.
    PhylomeDBiQ60049.

    Family and domain databases

    Gene3Di3.40.109.10. 1 hit.
    InterProiIPR029479. Nitroreductase.
    IPR000415. Nitroreductase-like.
    [Graphical view]
    PfamiPF00881. Nitroreductase. 1 hit.
    [Graphical view]
    SUPFAMiSSF55469. SSF55469. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q60049-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEATLPVLDA KTAALKRRSI RRYRKDPVPE GLLREILEAA LRAPSAWNLQ    50
    PWRIVVVRDP ATKRALREAA FGQAHVEEAP VVLVLYADLE DALAHLDEVI 100
    HPGVQGERRE AQKQAIQRAF AAMGQEARKA WASGQSYILL GYLLLLLEAY 150
    GLGSVPMLGF DPERVRAILG LPSHAAIPAL VALGYPAEEG YPSHRLPLER 200
    VVLWR 205
    Length:205
    Mass (Da):22,730
    Last modified:March 29, 2005 - v2
    Checksum:i012742DFA85B50E5
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti174 – 1741H → R in CAA42707. (PubMed:1577004)Curated
    Sequence conflicti174 – 1741H → R in AAB25458. (PubMed:1577004)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60110 Genomic DNA. Translation: CAA42707.1.
    S55441 Genomic DNA. Translation: AAB25458.1.
    AP008226 Genomic DNA. Translation: BAD70248.1.
    RefSeqiYP_143691.1. NC_006461.1.

    Genome annotation databases

    EnsemblBacteriaiBAD70248; BAD70248; BAD70248.
    GeneIDi3168975.
    KEGGittj:TTHA0425.
    PATRICi23955821. VBITheThe93045_0425.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X60110 Genomic DNA. Translation: CAA42707.1 .
    S55441 Genomic DNA. Translation: AAB25458.1 .
    AP008226 Genomic DNA. Translation: BAD70248.1 .
    RefSeqi YP_143691.1. NC_006461.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1NOX X-ray 1.59 A 1-205 [» ]
    ProteinModelPortali Q60049.
    SMRi Q60049. Positions 6-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 300852.TTHA0425.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai BAD70248 ; BAD70248 ; BAD70248 .
    GeneIDi 3168975.
    KEGGi ttj:TTHA0425.
    PATRICi 23955821. VBITheThe93045_0425.

    Phylogenomic databases

    eggNOGi COG0778.
    HOGENOMi HOG000146732.
    OMAi ANYPRSM.
    OrthoDBi EOG6N947Z.
    PhylomeDBi Q60049.

    Enzyme and pathway databases

    BioCyci TTHE300852:GH8R-446-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q60049.

    Family and domain databases

    Gene3Di 3.40.109.10. 1 hit.
    InterProi IPR029479. Nitroreductase.
    IPR000415. Nitroreductase-like.
    [Graphical view ]
    Pfami PF00881. Nitroreductase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF55469. SSF55469. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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."
      Park H.-J., Kreutzer R., Reiser C.O.A., Sprinzl M.
      Eur. J. Biochem. 205:875-879(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. Erratum
      Park H.-J., Kreutzer R., Reiser C.O.A., Sprinzl M.
      Eur. J. Biochem. 211:909-909(1993) [PubMed] [Europe PMC] [Abstract]
    3. "Complete genome sequence of Thermus thermophilus HB8."
      Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
      Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: HB8 / ATCC 27634 / DSM 579.
    4. "Purification and characterization of a NADH oxidase from the thermophile Thermus thermophilus HB8."
      Park H.-J., Reiser C.O.A., Kondruweit S., Erdmann H., Schmid R.D., Sprinzl M.
      Eur. J. Biochem. 205:881-885(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-32, CHARACTERIZATION.
    5. "Crystal structure of NADH oxidase from Thermus thermophilus."
      Hecht H.J., Erdmann H., Park H.J., Sprinzl M., Schmid R.D.
      Nat. Struct. Biol. 2:1109-1114(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) IN COMPLEX WITH FMN, SUBUNIT.

    Entry informationi

    Entry nameiNOX_THET8
    AccessioniPrimary (citable) accession number: Q60049
    Secondary accession number(s): Q53306, Q5SL68
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 86 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3