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Q1LCS4

- 3HAO_RALME

UniProt

Q1LCS4 - 3HAO_RALME

Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

nbaC

Organism
Ralstonia metallidurans (strain CH34 / ATCC 43123 / DSM 2839)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (30 May 2006)
      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.1 PublicationUniRule annotation

    Catalytic activityi

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

    Cofactori

    Binds 2 Fe2+ ions per subunit.1 PublicationUniRule annotation

    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

    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

    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: 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.1 PublicationUniRule annotation

    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 – 167
    Helixi17 – 204
    Turni23 – 253
    Beta strandi27 – 337
    Beta strandi35 – 417
    Beta strandi43 – 453
    Beta strandi50 – 523
    Beta strandi57 – 648
    Beta strandi66 – 727
    Beta strandi75 – 817
    Beta strandi86 – 894
    Beta strandi95 – 995
    Beta strandi105 – 1117
    Beta strandi119 – 1246
    Turni126 – 1283
    Beta strandi131 – 1377
    Helixi142 – 1454
    Helixi147 – 1559
    Helixi157 – 1604
    Turni163 – 1653
    Helixi171 – 1733

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    OMAiHINQTPE.
    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

    MLTYGAPFNF PRWIDEHAHL LKPPVGNRQV WQDSDFIVTV VGGPNHRTDY    50
    HDDPLEEFFY QLRGNAYLNL WVDGRRERAD LKEGDIFLLP PHVRHSPQRP 100
    EAGSACLVIE RQRPAGMLDG FEWYCDACGH LVHRVEVQLK SIVTDLPPLF 150
    ESFYASEDKR RCPHCGQVHP GRAA 174
    Length:174
    Mass (Da):20,028
    Last modified:May 30, 2006 - v1
    Checksum:i385F2E3DEB3947B8
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000353 Genomic DNA. Translation: ABF12052.1.
    RefSeqiYP_587321.1. NC_007974.2.

    Genome annotation databases

    EnsemblBacteriaiABF12052; ABF12052; Rmet_5193.
    GeneIDi4042054.
    KEGGirme:Rmet_5193.
    PATRICi20295146. VBIRalMet4734_5615.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP000353 Genomic DNA. Translation: ABF12052.1 .
    RefSeqi YP_587321.1. NC_007974.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YFU X-ray 1.90 A 1-174 [» ]
    1YFW X-ray 2.00 A 1-174 [» ]
    1YFX X-ray 2.00 A 1-174 [» ]
    1YFY X-ray 3.20 A 1-174 [» ]
    4HSL X-ray 2.00 A 1-174 [» ]
    4HVO X-ray 1.75 A 1-174 [» ]
    4HVQ X-ray 2.81 A 1-154 [» ]
    4HVR X-ray 2.70 A 1-174 [» ]
    4I3P X-ray 1.96 A 1-174 [» ]
    ProteinModelPortali Q1LCS4.
    SMRi Q1LCS4. Positions 1-174.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 266264.Rmet_5193.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABF12052 ; ABF12052 ; Rmet_5193 .
    GeneIDi 4042054.
    KEGGi rme:Rmet_5193.
    PATRICi 20295146. VBIRalMet4734_5615.

    Phylogenomic databases

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

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00330 .
    BioCyci CMET266264:GJ5G-5688-MONOMER.
    SABIO-RK Q1LCS4.

    Miscellaneous databases

    EvolutionaryTracei Q1LCS4.

    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: 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: October 1, 2014
    This is version 65 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