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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

nbaC

Organism
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the oxidative ring opening of 3-hydroxyanthranilate to 2-amino-3-carboxymuconate semialdehyde, which spontaneously cyclizes to quinolinate.UniRule annotation1 Publication

Catalytic activityi

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

Cofactori

Fe2+UniRule annotation1 PublicationNote: Binds 2 Fe2+ ions per subunit.UniRule annotation1 Publication

Enzyme regulationi

Inhibited by 4-chloro-3-hydroxyanthranilate. Mechanism of inactivation involves the oxidation of the catalytic active site Fe2+ to the catalytically inactive Fe3+ oxidation state, superoxide production, and formation of two disulfide bonds between Cys-125 and Cys-128, and Cys-162 and Cys-165. Enzyme can be reactivated under reducing conditions.1 Publication

Kineticsi

  1. KM=22.4 µM for 3-hydroxyanthranilate1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei47 – 471Dioxygen
    Metal bindingi51 – 511Iron 1; catalytic
    Metal bindingi57 – 571Iron 1; catalytic
    Binding sitei57 – 571Substrate
    Metal bindingi95 – 951Iron 1; catalytic
    Binding sitei99 – 991Substrate
    Binding sitei110 – 1101Substrate
    Metal bindingi125 – 1251Iron 2
    Metal bindingi128 – 1281Iron 2
    Metal bindingi162 – 1621Iron 2
    Metal bindingi165 – 1651Iron 2

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Dioxygenase, Oxidoreductase

    Keywords - Biological processi

    Pyridine nucleotide biosynthesis

    Keywords - Ligandi

    Iron, Metal-binding

    Enzyme and pathway databases

    BioCyciCMET266264:GJ5G-5688-MONOMER.
    SABIO-RKQ1LCS4.
    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:Rmet_5193
    Encoded oniPlasmid megaplasmid0 Publication
    OrganismiRalstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
    Taxonomic identifieri266264 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    ProteomesiUP000002429 Componenti: Plasmid megaplasmid CH34

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi47 – 471R → A: Increases KM for 3-hydroxyanthranilate 7-fold. Decreases activity 1000-fold. 1 Publication
    Mutagenesisi99 – 991R → A: Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold. 1 Publication
    Mutagenesisi110 – 1101E → A: Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1741743-hydroxyanthranilate 3,4-dioxygenasePRO_0000245477Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Protein-protein interaction databases

    STRINGi266264.Rmet_5193.

    Structurei

    Secondary structure

    1
    174
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi10 – 167Combined sources
    Helixi17 – 204Combined sources
    Turni23 – 253Combined sources
    Beta strandi27 – 337Combined sources
    Beta strandi35 – 417Combined sources
    Beta strandi43 – 453Combined sources
    Beta strandi50 – 523Combined sources
    Beta strandi57 – 648Combined sources
    Beta strandi66 – 727Combined sources
    Beta strandi75 – 817Combined sources
    Beta strandi86 – 894Combined sources
    Beta strandi95 – 995Combined sources
    Beta strandi105 – 1117Combined sources
    Beta strandi119 – 1246Combined sources
    Turni126 – 1283Combined sources
    Beta strandi131 – 1377Combined sources
    Helixi142 – 1454Combined sources
    Helixi147 – 1559Combined sources
    Helixi157 – 1604Combined sources
    Turni163 – 1653Combined sources
    Helixi171 – 1733Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YFUX-ray1.90A1-174[»]
    1YFWX-ray2.00A1-174[»]
    1YFXX-ray2.00A1-174[»]
    1YFYX-ray3.20A1-174[»]
    4HSLX-ray2.00A1-174[»]
    4HVOX-ray1.75A1-174[»]
    4HVQX-ray2.81A1-154[»]
    4HVRX-ray2.70A1-174[»]
    4I3PX-ray1.96A1-174[»]
    ProteinModelPortaliQ1LCS4.
    SMRiQ1LCS4. Positions 1-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ1LCS4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-HAO family.UniRule annotation

    Phylogenomic databases

    eggNOGiNOG77058.
    HOGENOMiHOG000218448.
    KOiK00452.
    OMAiKPPVGNQ.
    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.

    Q1LCS4-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MLTYGAPFNF PRWIDEHAHL LKPPVGNRQV WQDSDFIVTV VGGPNHRTDY
    60 70 80 90 100
    HDDPLEEFFY QLRGNAYLNL WVDGRRERAD LKEGDIFLLP PHVRHSPQRP
    110 120 130 140 150
    EAGSACLVIE RQRPAGMLDG FEWYCDACGH LVHRVEVQLK SIVTDLPPLF
    160 170
    ESFYASEDKR RCPHCGQVHP GRAA
    Length:174
    Mass (Da):20,028
    Last modified:May 30, 2006 - v1
    Checksum:i385F2E3DEB3947B8
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000353 Genomic DNA. Translation: ABF12052.1.
    RefSeqiWP_011519599.1. NC_007974.2.
    YP_587321.1. NC_007974.2.

    Genome annotation databases

    EnsemblBacteriaiABF12052; ABF12052; Rmet_5193.
    KEGGirme:Rmet_5193.
    PATRICi20295146. VBIRalMet4734_5615.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000353 Genomic DNA. Translation: ABF12052.1.
    RefSeqiWP_011519599.1. NC_007974.2.
    YP_587321.1. NC_007974.2.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YFUX-ray1.90A1-174[»]
    1YFWX-ray2.00A1-174[»]
    1YFXX-ray2.00A1-174[»]
    1YFYX-ray3.20A1-174[»]
    4HSLX-ray2.00A1-174[»]
    4HVOX-ray1.75A1-174[»]
    4HVQX-ray2.81A1-154[»]
    4HVRX-ray2.70A1-174[»]
    4I3PX-ray1.96A1-174[»]
    ProteinModelPortaliQ1LCS4.
    SMRiQ1LCS4. Positions 1-174.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi266264.Rmet_5193.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABF12052; ABF12052; Rmet_5193.
    KEGGirme:Rmet_5193.
    PATRICi20295146. VBIRalMet4734_5615.

    Phylogenomic databases

    eggNOGiNOG77058.
    HOGENOMiHOG000218448.
    KOiK00452.
    OMAiKPPVGNQ.
    OrthoDBiEOG6PW234.

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00330.
    BioCyciCMET266264:GJ5G-5688-MONOMER.
    SABIO-RKQ1LCS4.

    Miscellaneous databases

    EvolutionaryTraceiQ1LCS4.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: CH34 / ATCC 43123 / DSM 2839.
    2. "The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-chloro-3-hydroxyanthranilate."
      Colabroy K.L., Zhai H., Li T., Ge Y., Zhang Y., Liu A., Ealick S.E., McLafferty F.W., Begley T.P.
      Biochemistry 44:7623-7631(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME REGULATION, IDENTIFICATION BY MASS SPECTROMETRY.
    3. "Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: the catalytic mechanism of a complex oxidation involved in NAD biosynthesis."
      Zhang Y., Colabroy K.L., Begley T.P., Ealick S.E.
      Biochemistry 44:7632-7643(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF NATIVE PROTEIN AND COMPLEXES WITH SUBSTRATES OR INHIBITOR AND IRON, COFACTOR, KINETIC PARAMETERS, MUTAGENESIS OF ARG-47; ARG-99 AND GLU-110, SUBUNIT, REACTION MECHANISM.

    Entry informationi

    Entry namei3HAO_RALME
    AccessioniPrimary (citable) accession number: Q1LCS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: May 30, 2006
    Last modified: May 27, 2015
    This is version 72 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

    3D-structure, Complete proteome, Plasmid, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.