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Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

nbaC

Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
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: NAD(+) biosynthesis

    This protein is involved in step 3 of the subpathway that synthesizes quinolinate from L-kynurenine.UniRule annotation
    Proteins known to be involved in the 3 steps of the subpathway in this organism are:
    1. no protein annotated in this organism
    2. Kynureninase (kynU), Kynureninase (kynU)
    3. 3-hydroxyanthranilate 3,4-dioxygenase (nbaC)
    This subpathway is part of the pathway NAD(+) biosynthesis, which is itself part of Cofactor biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes quinolinate from L-kynurenine, the pathway NAD(+) biosynthesis and in Cofactor biosynthesis.

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei47Dioxygen1
    Metal bindingi51Iron 1; catalytic1
    Metal bindingi57Iron 1; catalytic1
    Binding sitei57Substrate1
    Metal bindingi95Iron 1; catalytic1
    Binding sitei99Substrate1
    Binding sitei110Substrate1
    Metal bindingi125Iron 21
    Metal bindingi128Iron 21
    Metal bindingi162Iron 21
    Metal bindingi165Iron 21

    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

    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
    OrganismiCupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34) (Ralstonia metallidurans)
    Taxonomic identifieri266264 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus
    Proteomesi
    • UP000002429 Componenti: Plasmid megaplasmid CH34

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi47R → A: Increases KM for 3-hydroxyanthranilate 7-fold. Decreases activity 1000-fold. 1 Publication1
    Mutagenesisi99R → A: Increases KM for 3-hydroxyanthranilate 40-fold. Decreases activity 5000-fold. 1 Publication1
    Mutagenesisi110E → A: Decreases KM for 3-hydroxyanthranilate 2-fold. Decreases activity 2000-fold. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002454771 – 1743-hydroxyanthranilate 3,4-dioxygenaseAdd BLAST174

    Interactioni

    Subunit structurei

    Homodimer.UniRule annotation1 Publication

    Structurei

    Secondary structure

    1174
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi10 – 16Combined sources7
    Helixi18 – 20Combined sources3
    Turni23 – 25Combined sources3
    Beta strandi27 – 33Combined sources7
    Beta strandi35 – 41Combined sources7
    Beta strandi43 – 45Combined sources3
    Beta strandi50 – 52Combined sources3
    Beta strandi57 – 64Combined sources8
    Beta strandi66 – 72Combined sources7
    Beta strandi75 – 81Combined sources7
    Beta strandi86 – 89Combined sources4
    Beta strandi95 – 99Combined sources5
    Beta strandi105 – 111Combined sources7
    Beta strandi119 – 124Combined sources6
    Turni126 – 128Combined sources3
    Beta strandi131 – 137Combined sources7
    Helixi142 – 145Combined sources4
    Helixi147 – 154Combined sources8
    Helixi157 – 160Combined sources4
    Turni163 – 165Combined sources3
    Helixi171 – 173Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YFUX-ray1.90A1-174[»]
    1YFWX-ray2.00A1-174[»]
    1YFXX-ray2.00A1-174[»]
    1YFYX-ray3.20A1-174[»]
    4HSJX-ray1.88A1-174[»]
    4HSLX-ray2.00A1-174[»]
    4HVOX-ray1.75A1-174[»]
    4HVQX-ray2.81A1-154[»]
    4HVRX-ray2.70A1-174[»]
    4I3PX-ray1.96A1-174[»]
    4L2NX-ray1.74A1-174[»]
    4R52X-ray1.53A1-174[»]
    4WZCX-ray1.84A1-174[»]
    ProteinModelPortaliQ1LCS4.
    SMRiQ1LCS4.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ1LCS4.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-HAO family.UniRule annotation

    Phylogenomic databases

    HOGENOMiHOG000218448.
    KOiK00452.
    OMAiKPPVGNQ.
    OrthoDBiPOG091H0LPR.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    HAMAPiMF_00825. 3_HAO. 1 hit.
    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.

    Genome annotation databases

    EnsemblBacteriaiABF12052; ABF12052; Rmet_5193.
    GeneIDi24153212.
    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.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1YFUX-ray1.90A1-174[»]
    1YFWX-ray2.00A1-174[»]
    1YFXX-ray2.00A1-174[»]
    1YFYX-ray3.20A1-174[»]
    4HSJX-ray1.88A1-174[»]
    4HSLX-ray2.00A1-174[»]
    4HVOX-ray1.75A1-174[»]
    4HVQX-ray2.81A1-154[»]
    4HVRX-ray2.70A1-174[»]
    4I3PX-ray1.96A1-174[»]
    4L2NX-ray1.74A1-174[»]
    4R52X-ray1.53A1-174[»]
    4WZCX-ray1.84A1-174[»]
    ProteinModelPortaliQ1LCS4.
    SMRiQ1LCS4.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABF12052; ABF12052; Rmet_5193.
    GeneIDi24153212.
    KEGGirme:Rmet_5193.
    PATRICi20295146. VBIRalMet4734_5615.

    Phylogenomic databases

    HOGENOMiHOG000218448.
    KOiK00452.
    OMAiKPPVGNQ.
    OrthoDBiPOG091H0LPR.

    Enzyme and pathway databases

    UniPathwayiUPA00253; UER00330.
    SABIO-RKQ1LCS4.

    Miscellaneous databases

    EvolutionaryTraceiQ1LCS4.

    Family and domain databases

    Gene3Di2.60.120.10. 1 hit.
    HAMAPiMF_00825. 3_HAO. 1 hit.
    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...

    Entry informationi

    Entry namei3HAO_CUPMC
    AccessioniPrimary (citable) accession number: Q1LCS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 11, 2006
    Last sequence update: May 30, 2006
    Last modified: November 2, 2016
    This is version 83 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

    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 one 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.