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A2RIB7

- NAOX_LACLM

UniProt

A2RIB7 - NAOX_LACLM

Protein

NADH oxidase

Gene

noxE

Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 55 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the four-electron reduction of molecular oxygen to water. Active on beta-NADH, but not on alpha-NADH, beta-NADPH or alpha-NADPH. Under aerobic conditions, oxygen acts as the electron acceptor. Under anaerobic conditions, DCIP and MB can replace oxygen as the electron acceptor.1 Publication

    Catalytic activityi

    NADH + acceptor = NAD+ + reduced acceptor.1 Publication

    Cofactori

    Binds 1 FAD per subunit.1 Publication

    Enzyme regulationi

    Inhibited by hydrogen peroxide, sulfhydryl reagents and quinine, but not by EDTA.1 Publication

    Kineticsi

    1. KM=4.1 µM for beta-NADH (in the presence of oxygen)1 Publication

    Vmax=83 µmol/min/mg enzyme toward beta-NADH (in the presence of oxygen)1 Publication

    pH dependencei

    Optimum pH is 6.0-9.0. Below pH 6.0 the enzyme is reversibly inactivated, above pH 10.0 the enzyme is irreversibly inactivated.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei10 – 101Proton acceptorBy similarity
    Active sitei42 – 421Redox-activeBy similarity
    Binding sitei42 – 421FADBy similarity
    Binding sitei159 – 1591NAD; via amide nitrogenBy similarity
    Binding sitei178 – 1781NADBy similarity
    Binding sitei187 – 1871NADBy similarity
    Binding sitei244 – 2441NAD; via amide nitrogenBy similarity
    Binding sitei282 – 2821FADBy similarity
    Binding sitei298 – 2981NAD; via carbonyl oxygenBy similarity
    Binding sitei300 – 3001FAD; via amide nitrogenBy similarity
    Binding sitei329 – 3291NAD; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi7 – 115FADBy similarity
    Nucleotide bindingi109 – 1124FADBy similarity

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: InterPro
    2. NADH dehydrogenase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein, NAD

    Enzyme and pathway databases

    BioCyciLLAC416870:GCDT-419-MONOMER.
    SABIO-RKA2RIB7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH oxidase (EC:1.6.99.3)
    Short name:
    NOXase
    Gene namesi
    Name:noxEImported
    Ordered Locus Names:llmg_0408
    OrganismiLactococcus lactis subsp. cremoris (strain MG1363)
    Taxonomic identifieri416870 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeLactococcus
    ProteomesiUP000000364: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446NADH oxidasePRO_0000292941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421Cysteine sulfenic acid (-SOH)By similarity

    Keywords - PTMi

    Oxidation

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi416870.llmg_0408.

    Structurei

    3D structure databases

    ProteinModelPortaliA2RIB7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0446.
    HOGENOMiHOG000276710.
    KOiK00359.
    OMAiYMESPVL.
    OrthoDBiEOG6QVRCJ.

    Family and domain databases

    Gene3Di3.30.390.30. 1 hit.
    InterProiIPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view]
    PfamiPF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view]
    PRINTSiPR00368. FADPNR.
    SUPFAMiSSF55424. SSF55424. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A2RIB7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKIVVIGTNH AGIATANTLL EQYPGHEIVM IDRNSNMSYL GCGTAIWVGR    50
    QIEKPDELFY AKAEDFEAKG VKILTETEVS EIDFANKKVY AKTKSDDEII 100
    EAYDKLVLAT GSRPIIPNLP GKDLKGIHFL KLFQEGQAID AEFAKEKVKR 150
    IAVIGAGYIG TEIAEAAKRR GKEVLLFDAE NTSLASYYDE EFAKGMDENL 200
    AQHGIELHFG ELAKEFKANE EGYVSQIVTN KATYDVDLVI NCIGFTANSA 250
    LASDKLATFK NGAIKVDKHQ QSSDPDVYAV GDVATIYSNA LQDFTYIALA 300
    SNAVRSGIVA GHNIGGKELE SVGVQGSNGI SIFGYNMTST GLSVKAAKKL 350
    GLEVSFSDFE DKQKAWFLHE NNDSVKIRIV YETKSRRIIG AQLASKSEII 400
    AGNINMFSLA IQEKKTIDEL ALLDLFFLPH FNSPYNYMTV AALNAK 446
    Length:446
    Mass (Da):48,872
    Last modified:March 6, 2007 - v1
    Checksum:i1B1FA2FE313D6C03
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti11 – 111A → AA AA sequence 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY046926 Genomic DNA. Translation: AAL02357.1.
    AM406671 Genomic DNA. Translation: CAL97012.1.
    RefSeqiYP_001031758.1. NC_009004.1.

    Genome annotation databases

    EnsemblBacteriaiCAL97012; CAL97012; llmg_0408.
    GeneIDi4796799.
    KEGGillm:llmg_0408.
    PATRICi22281862. VBILacLac4574_0419.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY046926 Genomic DNA. Translation: AAL02357.1 .
    AM406671 Genomic DNA. Translation: CAL97012.1 .
    RefSeqi YP_001031758.1. NC_009004.1.

    3D structure databases

    ProteinModelPortali A2RIB7.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 416870.llmg_0408.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAL97012 ; CAL97012 ; llmg_0408 .
    GeneIDi 4796799.
    KEGGi llm:llmg_0408.
    PATRICi 22281862. VBILacLac4574_0419.

    Phylogenomic databases

    eggNOGi COG0446.
    HOGENOMi HOG000276710.
    KOi K00359.
    OMAi YMESPVL.
    OrthoDBi EOG6QVRCJ.

    Enzyme and pathway databases

    BioCyci LLAC416870:GCDT-419-MONOMER.
    SABIO-RK A2RIB7.

    Family and domain databases

    Gene3Di 3.30.390.30. 1 hit.
    InterProi IPR016156. FAD/NAD-linked_Rdtase_dimer.
    IPR013027. FAD_pyr_nucl-diS_OxRdtase.
    IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
    IPR023753. Pyr_nucl-diS_OxRdtase_FAD/NAD.
    IPR001327. Pyr_OxRdtase_NAD-bd_dom.
    [Graphical view ]
    Pfami PF00070. Pyr_redox. 1 hit.
    PF07992. Pyr_redox_2. 1 hit.
    PF02852. Pyr_redox_dim. 1 hit.
    [Graphical view ]
    PRINTSi PR00368. FADPNR.
    SUPFAMi SSF55424. SSF55424. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Metabolic engineering of lactic acid bacteria, the combined approach: kinetic modelling, metabolic control and experimental analysis."
      Hoefnagel M.H.N., Starrenburg M.J.C., Martens D.E., Hugenholtz J., Kleerebezem M., Van Swam I.I., Bongers R., Westerhoff H.V., Snoep J.L.
      Microbiology 148:1003-1013(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "The complete genome sequence of the lactic acid bacterial paradigm Lactococcus lactis subsp. cremoris MG1363."
      Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C., Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P., van Sinderen D., Kok J.
      J. Bacteriol. 189:3256-3270(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: MG1363.
    3. "Purification and characterisation of the water forming NADH-oxidase from Lactococcus lactis."
      Lopez de Felipe F., Hugenholtz J.
      Int. Dairy J. 11:37-44(2001)
      [AGRICOLA] [Europe PMC]
      Cited for: PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

    Entry informationi

    Entry nameiNAOX_LACLM
    AccessioniPrimary (citable) accession number: A2RIB7
    Secondary accession number(s): P81759, Q8KR34
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 55 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3