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P47096

- 3HAO_YEAST

UniProt

P47096 - 3HAO_YEAST

Protein

3-hydroxyanthranilate 3,4-dioxygenase

Gene

BNA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 Feb 1996)
      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.

    Catalytic activityi

    3-hydroxyanthranilate + O2 = 2-amino-3-carboxymuconate semialdehyde.1 PublicationUniRule annotation

    Cofactori

    Fe2+ ion.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei45 – 451DioxygenUniRule annotation
    Metal bindingi49 – 491Iron; catalytic
    Metal bindingi55 – 551Iron; catalytic
    Binding sitei55 – 551SubstrateUniRule annotation
    Metal bindingi97 – 971Iron; catalytic
    Binding sitei101 – 1011SubstrateUniRule annotation
    Binding sitei111 – 1111SubstrateUniRule annotation
    Metal bindingi126 – 1261Divalent metal cation
    Metal bindingi129 – 1291Divalent metal cation
    Metal bindingi163 – 1631Divalent metal cation
    Metal bindingi166 – 1661Divalent metal cation

    GO - Molecular functioni

    1. 3-hydroxyanthranilate 3,4-dioxygenase activity Source: SGD
    2. ferrous iron binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. 'de novo' NAD biosynthetic process from tryptophan Source: SGD
    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

    BioCyciMetaCyc:MONOMER-8161.
    YEAST:YJR025C-MONOMER.
    BRENDAi1.13.11.6. 984.
    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
    Synonyms:HAD1
    Ordered Locus Names:YJR025C
    ORF Names:J1550
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome X

    Organism-specific databases

    CYGDiYJR025c.
    SGDiS000003786. BNA1.

    Subcellular locationi

    Cytoplasm 1 PublicationUniRule annotation. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: SGD
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 1771773-hydroxyanthranilate 3,4-dioxygenasePRO_0000064375Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei176 – 1761Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP47096.
    PaxDbiP47096.
    PeptideAtlasiP47096.

    Expressioni

    Gene expression databases

    GenevestigatoriP47096.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi33778. 47 interactions.
    DIPiDIP-4759N.
    IntActiP47096. 1 interaction.
    MINTiMINT-529506.
    STRINGi4932.YJR025C.

    Structurei

    Secondary structure

    1
    177
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi9 – 168
    Helixi17 – 204
    Beta strandi21 – 244
    Beta strandi26 – 305
    Beta strandi32 – 398
    Beta strandi41 – 433
    Beta strandi48 – 503
    Beta strandi55 – 628
    Beta strandi64 – 707
    Beta strandi72 – 754
    Beta strandi77 – 837
    Beta strandi87 – 915
    Beta strandi97 – 1015
    Beta strandi106 – 1127
    Beta strandi116 – 1183
    Beta strandi121 – 1255
    Turni127 – 1293
    Beta strandi132 – 1376
    Beta strandi140 – 1423
    Helixi145 – 15511
    Helixi158 – 1614
    Turni164 – 1663

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1ZVFX-ray2.41A/B1-175[»]
    ProteinModelPortaliP47096.
    SMRiP47096. Positions 1-175.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP47096.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the 3-HAO family.UniRule annotation

    Phylogenomic databases

    eggNOGiNOG77058.
    GeneTreeiENSGT00390000013008.
    HOGENOMiHOG000218448.
    KOiK00452.
    OMAiHINQTPE.
    OrthoDBiEOG7QK0Q0.

    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.

    P47096-1 [UniParc]FASTAAdd to Basket

    « Hide

    MFNTTPINID KWLKENEGLL KPPVNNYCLH KGGFTVMIVG GPNERTGYHI    50
    NPTPEWFYQK KGSMLLKVVD ETDAEPKFID IIINEGDSYL LPGNVPHSPV 100
    RFADTVGIVV EQDRPGGEND KIRWYCSHCR QVVHESELQM LDLGTQVKEA 150
    ILDFENDVEK RTCFHCKTLN YARPQSN 177
    Length:177
    Mass (Da):20,235
    Last modified:February 1, 1996 - v1
    Checksum:i930D69F486632417
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49525 Genomic DNA. Translation: CAA89550.1.
    X87297 Genomic DNA. Translation: CAA60720.1.
    AY558309 Genomic DNA. Translation: AAS56635.1.
    BK006943 Genomic DNA. Translation: DAA08814.1.
    PIRiS57043.
    RefSeqiNP_012559.1. NM_001181683.1.

    Genome annotation databases

    EnsemblFungiiYJR025C; YJR025C; YJR025C.
    GeneIDi853482.
    KEGGisce:YJR025C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z49525 Genomic DNA. Translation: CAA89550.1 .
    X87297 Genomic DNA. Translation: CAA60720.1 .
    AY558309 Genomic DNA. Translation: AAS56635.1 .
    BK006943 Genomic DNA. Translation: DAA08814.1 .
    PIRi S57043.
    RefSeqi NP_012559.1. NM_001181683.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1ZVF X-ray 2.41 A/B 1-175 [» ]
    ProteinModelPortali P47096.
    SMRi P47096. Positions 1-175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33778. 47 interactions.
    DIPi DIP-4759N.
    IntActi P47096. 1 interaction.
    MINTi MINT-529506.
    STRINGi 4932.YJR025C.

    Proteomic databases

    MaxQBi P47096.
    PaxDbi P47096.
    PeptideAtlasi P47096.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YJR025C ; YJR025C ; YJR025C .
    GeneIDi 853482.
    KEGGi sce:YJR025C.

    Organism-specific databases

    CYGDi YJR025c.
    SGDi S000003786. BNA1.

    Phylogenomic databases

    eggNOGi NOG77058.
    GeneTreei ENSGT00390000013008.
    HOGENOMi HOG000218448.
    KOi K00452.
    OMAi HINQTPE.
    OrthoDBi EOG7QK0Q0.

    Enzyme and pathway databases

    UniPathwayi UPA00253 ; UER00330 .
    BioCyci MetaCyc:MONOMER-8161.
    YEAST:YJR025C-MONOMER.
    BRENDAi 1.13.11.6. 984.

    Miscellaneous databases

    EvolutionaryTracei P47096.
    NextBioi 974095.
    PROi P47096.

    Gene expression databases

    Genevestigatori P47096.

    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 sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon."
      Zagulski M., Babinska B., Gromadka R., Migdalski A., Rytka J., Sulicka J., Herbert C.J.
      Yeast 11:1179-1186(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X."
      Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K.
      , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.
      EMBO J. 15:2031-2049(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis."
      Kucharczyk R., Zagulski M., Rytka J., Herbert C.J.
      FEBS Lett. 424:127-130(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, PATHWAY.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: a special subgroup of the type III extradiol dioxygenases."
      Li X., Guo M., Fan J., Tang W., Wang D., Ge H., Rong H., Teng M., Niu L., Liu Q., Hao Q.
      Protein Sci. 15:761-773(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 1-175 IN COMPLEX WITH DIVALENT METAL IONS, SUBUNIT.

    Entry informationi

    Entry namei3HAO_YEAST
    AccessioniPrimary (citable) accession number: P47096
    Secondary accession number(s): D6VWJ8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: February 1, 1996
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2330 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, 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
    4. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    5. Yeast chromosome X
      Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names

    External Data

    Dasty 3