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A2R8S7

- 3HAO_ASPNC

UniProt

A2R8S7 - 3HAO_ASPNC

Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

bna1

Organism
Aspergillus niger (strain CBS 513.88 / FGSC A1513)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 51 (01 Oct 2014)
      Sequence version 1 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.UniRule annotation

    Catalytic activityi

    3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.UniRule annotation

    Cofactori

    Fe2+ ion.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei50 – 501DioxygenUniRule annotation
    Metal bindingi54 – 541Iron; catalyticUniRule annotation
    Metal bindingi60 – 601Iron; catalyticUniRule annotation
    Binding sitei60 – 601SubstrateUniRule annotation
    Metal bindingi102 – 1021Iron; catalyticUniRule annotation
    Binding sitei106 – 1061SubstrateUniRule annotation
    Binding sitei116 – 1161SubstrateUniRule annotation
    Metal bindingi131 – 1311Divalent metal cationUniRule annotation
    Metal bindingi136 – 1361Divalent metal cationUniRule annotation
    Metal bindingi170 – 1701Divalent metal cationUniRule annotation
    Metal bindingi173 – 1731Divalent metal cationUniRule annotation

    GO - Molecular functioni

    1. 3-hydroxyanthranilate 3,4-dioxygenase activity Source: UniProtKB-HAMAP
    2. ferrous iron binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from tryptophan Source: UniProtKB-HAMAP
    2. anthranilate metabolic process Source: UniProtKB-HAMAP
    3. quinolinate biosynthetic process Source: UniProtKB-HAMAP
    4. tryptophan catabolic process Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00330.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-hydroxyanthranilate 3,4-dioxygenaseUniRule annotation (EC:1.13.11.6UniRule annotation)
    Alternative name(s):
    3-hydroxyanthranilate oxygenaseUniRule annotation
    Short name:
    3-HAOUniRule annotation
    3-hydroxyanthranilic acid dioxygenaseUniRule annotation
    Short name:
    HADUniRule annotation
    Biosynthesis of nicotinic acid protein 1UniRule annotation
    Gene namesi
    Name:bna1
    ORF Names:An16g08210
    OrganismiAspergillus niger (strain CBS 513.88 / FGSC A1513)
    Taxonomic identifieri425011 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
    ProteomesiUP000006706: Chromosome 5R

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1891893-hydroxyanthranilate 3,4-dioxygenasePRO_0000361980Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi5061.CADANGAP00013037.

    Structurei

    3D structure databases

    ProteinModelPortaliA2R8S7.
    SMRiA2R8S7. Positions 5-181.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-HAO family.UniRule annotation

    Phylogenomic databases

    eggNOGiNOG77058.
    HOGENOMiHOG000218448.
    KOiK00452.
    OrthoDBiEOG7QK0Q0.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    HAMAPiMF_00825. 3_HAO.
    InterProiIPR010329. 3hydroanth_dOase.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view]
    PANTHERiPTHR15497. PTHR15497. 1 hit.
    PfamiPF06052. 3-HAO. 1 hit.
    [Graphical view]
    SUPFAMiSSF51182. SSF51182. 1 hit.
    TIGRFAMsiTIGR03037. anthran_nbaC. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    A2R8S7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLPPALNIPK WLETNSHLLQ PPVNNYCVYH PSSPATQGYT VMIVGGPNAR    50
    TDYHINTTPE FFYQYKGSML LRTVDESSTP PTFQDIPIHE GSLFLLPANT 100
    PHCPVRFKDT VGVVMEQPRK EGAVDAMRWY CRNKDCGKVV WEKRFVCTDL 150
    GTQVKQVVEE FAGDEEKRTC KACGVVARSK YEEGEVVQP 189
    Length:189
    Mass (Da):21,338
    Last modified:March 6, 2007 - v1
    Checksum:iF10A9D82A81A07A9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270377 Genomic DNA. Translation: CAK47070.1.
    RefSeqiXP_001398119.1. XM_001398082.1.

    Genome annotation databases

    EnsemblFungiiCADANGAT00013285; CADANGAP00013037; CADANGAG00013285.
    GeneIDi4989212.
    KEGGiang:ANI_1_1110144.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AM270377 Genomic DNA. Translation: CAK47070.1 .
    RefSeqi XP_001398119.1. XM_001398082.1.

    3D structure databases

    ProteinModelPortali A2R8S7.
    SMRi A2R8S7. Positions 5-181.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 5061.CADANGAP00013037.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii CADANGAT00013285 ; CADANGAP00013037 ; CADANGAG00013285 .
    GeneIDi 4989212.
    KEGGi ang:ANI_1_1110144.

    Phylogenomic databases

    eggNOGi NOG77058.
    HOGENOMi HOG000218448.
    KOi K00452.
    OrthoDBi EOG7QK0Q0.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00330 .

    Family and domain databases

    Gene3Di 2.60.120.10. 1 hit.
    HAMAPi MF_00825. 3_HAO.
    InterProi IPR010329. 3hydroanth_dOase.
    IPR014710. RmlC-like_jellyroll.
    IPR011051. RmlC_Cupin.
    [Graphical view ]
    PANTHERi PTHR15497. PTHR15497. 1 hit.
    Pfami PF06052. 3-HAO. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51182. SSF51182. 1 hit.
    TIGRFAMsi TIGR03037. anthran_nbaC. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88."
      Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J., Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R., Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X., Contreras R., Cornell M.
      , Coutinho P.M., Danchin E.G.J., Debets A.J.M., Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M., d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J., Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W., van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M., Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X., van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A., Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E., Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J., Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H., Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.
      Nat. Biotechnol. 25:221-231(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CBS 513.88 / FGSC A1513.

    Entry informationi

    Entry namei3HAO_ASPNC
    AccessioniPrimary (citable) accession number: A2R8S7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 10, 2009
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 51 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3