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    BNA1 3-hydroxyanthranilate 3,4-dioxygenase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853482, updated on 9-Dec-2024

    Summary

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    Official Symbol
    BNA1
    Official Full Name
    3-hydroxyanthranilate 3,4-dioxygenase
    Primary source
    SGD:S000003786
    Locus tag
    YJR025C
    See related
    AllianceGenome:SGD:S000003786; FungiDB:YJR025C; VEuPathDB:YJR025C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    HAD1
    Summary
    Enables 3-hydroxyanthranilate 3,4-dioxygenase activity. Involved in 'de novo' NAD biosynthetic process from tryptophan. Located in cytoplasm. Orthologous to human HAAO (3-hydroxyanthranilate 3,4-dioxygenase). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See BNA1 in Genome Data Viewer
    Location:
    chromosome: X
    Exon count:
    1
    Sequence:
    Chromosome: X; NC_001142.9 (471138..471671, complement)

    Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene U4/U6-U5 snRNP complex subunit LSM8 Neighboring gene methylthioribulose 1-phosphate dehydratase MDE1 Neighboring gene gag protein Neighboring gene gag-pol fusion protein Neighboring gene gag protein Neighboring gene gag-pol fusion protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001142.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis. Kucharczyk R, et al. FEBS Lett, 1998 Mar 13. PMID 9539135
    2. Crystal structure of 3-hydroxyanthranilic acid 3,4-dioxygenase from Saccharomyces cerevisiae: a special subgroup of the type III extradiol dioxygenases. Li X, et al. Protein Sci, 2006 Apr. PMID 16522801, Free PMC Article
    3. Telomeric and rDNA silencing in Saccharomyces cerevisiae are dependent on a nuclear NAD(+) salvage pathway. Sandmeier JJ, et al. Genetics, 2002 Mar. PMID 11901108, Free PMC Article
    4. Isonicotinamide enhances Sir2 protein-mediated silencing and longevity in yeast by raising intracellular NAD+ concentration. McClure JM, et al. J Biol Chem, 2012 Jun 15. PMID 22539348, Free PMC Article
    5. Regulation of gene transcription by the histone H2A N-terminal domain. Parra MA, et al. Mol Cell Biol, 2007 Nov. PMID 17724083, Free PMC Article

    See all (50) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables 3-hydroxyanthranilate 3,4-dioxygenase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables 3-hydroxyanthranilate 3,4-dioxygenase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables 3-hydroxyanthranilate 3,4-dioxygenase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables dioxygenase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ferrous iron binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables iron ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in 'de novo' NAD biosynthetic process from tryptophan IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in 'de novo' NAD biosynthetic process from tryptophan IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in 'de novo' NAD biosynthetic process from tryptophan IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in NAD biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in anthranilate metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in pyridine nucleotide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in quinolinate biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in quinolinate metabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tryptophan catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    3-hydroxyanthranilate 3,4-dioxygenase
    NP_012559.1
    • 3-hydroxyanthranilic acid dioxygenase; required for the de novo biosynthesis of NAD from tryptophan via kynurenine; expression regulated by Hst1p

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001142.9 Reference assembly

      Range
      471138..471671 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181683.1 → NP_012559.1  TPA: 3-hydroxyanthranilate 3,4-dioxygenase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012559.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VWJ8, P47096
      UniProtKB/TrEMBL
      A6ZPZ0, B3LQC0, C7GKY1, D3UF86, G2WH35, N1P1I3
      Conserved Domains (1) summary
      cl40423
      Location:1 → 155
      cupin_RmlC-like; RmlC-like cupin superfamily
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P47096.1

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