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Q739J0

- 3HAO_BACC1

UniProt

Q739J0 - 3HAO_BACC1

Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

nbaC

Organism
Bacillus cereus (strain ATCC 10987)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 75 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      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

    Binds 2 Fe2+ ions per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei47 – 471DioxygenUniRule annotation
    Metal bindingi51 – 511Iron 1; catalyticUniRule annotation
    Metal bindingi57 – 571Iron 1; catalyticUniRule annotation
    Binding sitei57 – 571SubstrateUniRule annotation
    Metal bindingi96 – 961Iron 1; catalyticUniRule annotation
    Binding sitei100 – 1001SubstrateUniRule annotation
    Binding sitei110 – 1101SubstrateUniRule annotation
    Metal bindingi125 – 1251Iron 2UniRule annotation
    Metal bindingi128 – 1281Iron 2UniRule annotation
    Metal bindingi162 – 1621Iron 2UniRule annotation
    Metal bindingi165 – 1651Iron 2UniRule 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
    Gene namesi
    Name:nbaCUniRule annotation
    Ordered Locus Names:BCE_2151
    OrganismiBacillus cereus (strain ATCC 10987)
    Taxonomic identifieri222523 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000002527: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1791793-hydroxyanthranilate 3,4-dioxygenasePRO_0000245473Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi222523.BCE_2151.

    Structurei

    3D structure databases

    ProteinModelPortaliQ739J0.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-HAO family.UniRule annotation

    Phylogenomic databases

    eggNOGiNOG77058.
    HOGENOMiHOG000218448.
    KOiK00452.
    OMAiHILLANT.
    OrthoDBiEOG6PW234.

    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.

    Q739J0-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSKTLQSFNL LKWIDENKEL LKPPVNNKVI WQDSEFIAMI LGGPNRRRDF    50
    HVDPSDEFFY QIKGECYVEC ITEEGKREVV TVKEGDVFML PAMVPHSPHR 100
    VANTYGLVIE RKRNQGELED FVWFCDECNH EMHRVRVQLS DIEKQVKEAI 150
    HSFNSNKEIR ACKNCGHIMP EEVEEWKCE 179
    Length:179
    Mass (Da):21,084
    Last modified:July 5, 2004 - v1
    Checksum:i1A4A10AA8AC192AC
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS41072.1.
    RefSeqiNP_978464.1. NC_003909.8.
    WP_000047732.1. NC_003909.8.

    Genome annotation databases

    EnsemblBacteriaiAAS41072; AAS41072; BCE_2151.
    GeneIDi2748280.
    KEGGibca:BCE_2151.
    PATRICi18853102. VBIBacCer118379_2053.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE017194 Genomic DNA. Translation: AAS41072.1 .
    RefSeqi NP_978464.1. NC_003909.8.
    WP_000047732.1. NC_003909.8.

    3D structure databases

    ProteinModelPortali Q739J0.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 222523.BCE_2151.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAS41072 ; AAS41072 ; BCE_2151 .
    GeneIDi 2748280.
    KEGGi bca:BCE_2151.
    PATRICi 18853102. VBIBacCer118379_2053.

    Phylogenomic databases

    eggNOGi NOG77058.
    HOGENOMi HOG000218448.
    KOi K00452.
    OMAi HILLANT.
    OrthoDBi EOG6PW234.

    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. "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
      Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
      Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 10987.

    Entry informationi

    Entry namei3HAO_BACC1
    AccessioniPrimary (citable) accession number: Q739J0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 75 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

    Documents

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

    External Data

    Dasty 3