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B2AAJ5

- 3HAO_PODAN

UniProt

B2AAJ5 - 3HAO_PODAN

Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

BNA1

Organism
Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 41 (01 Oct 2014)
      Sequence version 1 (20 May 2008)
      Previous versions | rss
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    • Comment

    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 sitei44 – 441DioxygenUniRule annotation
    Metal bindingi48 – 481Iron; catalyticUniRule annotation
    Metal bindingi54 – 541Iron; catalyticUniRule annotation
    Binding sitei54 – 541SubstrateUniRule annotation
    Metal bindingi95 – 951Iron; catalyticUniRule annotation
    Binding sitei99 – 991SubstrateUniRule annotation
    Binding sitei109 – 1091SubstrateUniRule annotation
    Metal bindingi124 – 1241Divalent metal cationUniRule annotation
    Metal bindingi127 – 1271Divalent metal cationUniRule annotation
    Metal bindingi161 – 1611Divalent metal cationUniRule annotation
    Metal bindingi164 – 1641Divalent 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:BNA1UniRule annotation
    Ordered Locus Names:PODANS_1_4230
    OrganismiPodospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383) (Pleurage anserina)
    Taxonomic identifieri515849 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesLasiosphaeriaceaePodospora
    ProteomesiUP000001197: Chromosome 1

    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 – 1851853-hydroxyanthranilate 3,4-dioxygenasePRO_0000361994Add
    BLAST

    Structurei

    3D structure databases

    ProteinModelPortaliB2AAJ5.
    SMRiB2AAJ5. Positions 3-164.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-HAO family.UniRule annotation

    Phylogenomic databases

    KOiK00452.

    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.

    B2AAJ5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLTQPINLPK WLEENSHLLK PPINNYCVYN EGFTVMIVGG PNARTDYHIN    50
    QTPEWFYQHR GAMLLKIVDP TDNNTFKDII IRQGDMFLLP PNTPHNPVRF 100
    ADTVGIVLEQ ERPEGSIDRM RWYCQSCKEI VHEASFHCTD LGTQIKAAVE 150
    AFKEDEEKRT CKKCGEVAAW KPAEGSLKDP NLEEA 185
    Length:185
    Mass (Da):21,186
    Last modified:May 20, 2008 - v1
    Checksum:iD50D06BC49568576
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU633438 Genomic DNA. Translation: CAP60107.1.
    RefSeqiXP_001912625.1. XM_001912590.1.

    Genome annotation databases

    GeneIDi6196987.
    KEGGipan:PODANSg09674.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU633438 Genomic DNA. Translation: CAP60107.1 .
    RefSeqi XP_001912625.1. XM_001912590.1.

    3D structure databases

    ProteinModelPortali B2AAJ5.
    SMRi B2AAJ5. Positions 3-164.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 6196987.
    KEGGi pan:PODANSg09674.

    Phylogenomic databases

    KOi K00452.

    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: S / ATCC MYA-4624 / DSM 980 / FGSC 10383.

    Entry informationi

    Entry namei3HAO_PODAN
    AccessioniPrimary (citable) accession number: B2AAJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 10, 2009
    Last sequence update: May 20, 2008
    Last modified: October 1, 2014
    This is version 41 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