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P37061

- NAOX_ENTFA

UniProt

P37061 - NAOX_ENTFA

Protein

NADH oxidase

Gene

nox

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Catalyzes the four-electron reduction of molecular oxygen to water.

    Catalytic activityi

    NADH + acceptor = NAD+ + reduced acceptor.

    Cofactori

    Binds 1 FAD per subunit.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei10 – 101Proton acceptorBy similarity
    Binding sitei32 – 321FADBy similarity
    Active sitei42 – 421Redox-active1 Publication
    Binding sitei42 – 421FADBy similarity
    Binding sitei177 – 1771NADBy similarity
    Binding sitei186 – 1861NADBy similarity
    Binding sitei243 – 2431NAD; via amide nitrogenBy similarity
    Binding sitei299 – 2991FAD; via amide nitrogenBy similarity
    Binding sitei328 – 3281NAD; via carbonyl oxygenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi7 – 115FADBy similarity
    Nucleotide bindingi110 – 1134FADBy similarity
    Nucleotide bindingi150 – 16516NADBy similarityAdd
    BLAST
    Nucleotide bindingi271 – 28111FADBy similarityAdd
    BLAST

    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

    BioCyciEFAE226185:GHI1-1572-MONOMER.
    SABIO-RKP37061.

    Protein family/group databases

    PeroxiBasei5456. EfNadOxd01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    NADH oxidase (EC:1.6.99.3)
    Short name:
    NOXase
    Gene namesi
    Name:nox
    Ordered Locus Names:EF_1586
    OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
    Taxonomic identifieri226185 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
    ProteomesiUP000001415: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 446446NADH oxidasePRO_0000184701Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei42 – 421Cysteine sulfenic acid (-SOH)1 Publication

    Post-translational modificationi

    The N-terminus is blocked.

    Keywords - PTMi

    Oxidation

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    STRINGi226185.EF1586.

    Structurei

    3D structure databases

    ProteinModelPortaliP37061.
    SMRiP37061. Positions 1-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Redox-active center

    Phylogenomic databases

    eggNOGiCOG0446.
    KOiK00356.
    OMAiHAYIPLA.
    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.

    P37061-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKVVVVGCTH AGTSAVKSIL ANHPEAEVTV YERNDNISFL SCGIALYVGG    50
    VVKNAADLFY SNPEELASLG ATVKMEHNVE EINVDDKTVT AKNLQTGATE 100
    TVSYDKLVMT TGSWPIIPPI PGIDAENILL CKNYSQANVI IEKAKDAKRV 150
    VVVGGGYIGI ELVEAFVESG KQVTLVDGLD RILNKYLDKP FTDVLEKELV 200
    DRGVNLALGE NVQQFVADEQ GKVAKVITPS QEFEADMVIM CVGFRPNTEL 250
    LKDKVDMLPN GAIEVNEYMQ TSNPDIFAAG DSAVVHYNPS QTKNYIPLAT 300
    NAVRQGMLVG RNLTEQKLAY RGTQGTSGLY LFGWKIGSTG VTKESAKLNG 350
    LDVEATVFED NYRPEFMPTT EKVLMELVYE KGTQRIVGGQ LMSKYDITQS 400
    ANTLSLAVQN KMTVEDLAIS DFFFQPHFDR PWNYLNLLAQ AALENM 446
    Length:446
    Mass (Da):48,915
    Last modified:June 1, 1994 - v1
    Checksum:iD0762A47FC3DC071
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68847 Genomic DNA. Translation: CAA48728.1.
    AE016830 Genomic DNA. Translation: AAO81372.1.
    PIRiS26965.
    RefSeqiNP_815302.1. NC_004668.1.
    WP_002361833.1. NZ_KE136528.1.

    Genome annotation databases

    EnsemblBacteriaiAAO81372; AAO81372; EF_1586.
    GeneIDi1200486.
    KEGGiefa:EF1586.
    PATRICi21853530. VBIEntFae7065_1491.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X68847 Genomic DNA. Translation: CAA48728.1 .
    AE016830 Genomic DNA. Translation: AAO81372.1 .
    PIRi S26965.
    RefSeqi NP_815302.1. NC_004668.1.
    WP_002361833.1. NZ_KE136528.1.

    3D structure databases

    ProteinModelPortali P37061.
    SMRi P37061. Positions 1-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 226185.EF1586.

    Protein family/group databases

    PeroxiBasei 5456. EfNadOxd01.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAO81372 ; AAO81372 ; EF_1586 .
    GeneIDi 1200486.
    KEGGi efa:EF1586.
    PATRICi 21853530. VBIEntFae7065_1491.

    Phylogenomic databases

    eggNOGi COG0446.
    KOi K00356.
    OMAi HAYIPLA.
    OrthoDBi EOG6QVRCJ.

    Enzyme and pathway databases

    BioCyci EFAE226185:GHI1-1572-MONOMER.
    SABIO-RK P37061.

    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. "Molecular cloning and analysis of the gene encoding the NADH oxidase from Streptococcus faecalis 10C1. Comparison with NADH peroxidase and the flavoprotein disulfide reductases."
      Ross R.P., Claiborne A.
      J. Mol. Biol. 227:658-671(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 700802 / V583.
    3. "The streptococcal flavoprotein NADH oxidase. I. Evidence linking NADH oxidase and NADH peroxidase cysteinyl redox centers."
      Ahmed S.A., Claiborne A.
      J. Biol. Chem. 264:19856-19863(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 3-17; 34-52 AND 226-250.
      Strain: ATCC 11700 / DSM 20409 / NCIMB 8661 / 10C1.
    4. "Protein-sulfenic acid stabilization and function in enzyme catalysis and gene regulation."
      Claiborne A., Miller H., Parsonage D., Ross R.P.
      FASEB J. 7:1483-1490(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACTIVE SITE, OXIDATION AT CYS-42.

    Entry informationi

    Entry nameiNAOX_ENTFA
    AccessioniPrimary (citable) accession number: P37061
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 109 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The active site is the redox-active Cys-42 oxidized to Cys-SOH. The oxidized form is stabilized by a hydrogen bond formation with His-10.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3