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    BNA2 dioxygenase BNA2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 853541, updated on 26-Jun-2024

    Summary

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    Gene symbol
    BNA2
    Gene description
    dioxygenase BNA2
    Primary source
    FungiDB:YJR078W
    Locus tag
    YJR078W
    See related
    SGD:S000003839; AllianceGenome:SGD:S000003839; VEuPathDB:YJR078W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables indoleamine 2,3-dioxygenase activity. Involved in 'de novo' NAD biosynthetic process from tryptophan. Located in cytoplasm. Orthologous to several human genes including IDO2 (indoleamine 2,3-dioxygenase 2). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See BNA2 in Genome Data Viewer
    Location:
    chromosome: X
    Exon count:
    1
    Sequence:
    Chromosome: X; NC_001142.9 (578860..580221)

    Chromosome X - NC_001142.9Genomic Context describing neighboring genes Neighboring gene septin CDC11 Neighboring gene Mir1p Neighboring gene uncharacterized protein Neighboring gene Aim24p Neighboring gene Eaf6p

    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. Molecular evolution and characterization of fungal indoleamine 2,3-dioxygenases. Yuasa HJ, et al. J Mol Evol, 2011 Feb. PMID 21170645
    2. Evolution of vertebrate indoleamine 2,3-dioxygenases. Yuasa HJ, et al. J Mol Evol, 2007 Dec. PMID 18026683
    3. Kynurenine aminotransferase activity of Aro8/Aro9 engage tryptophan degradation by producing kynurenic acid in Saccharomyces cerevisiae. Ohashi K, et al. Sci Rep, 2017 Sep 22. PMID 28939805, Free PMC Article
    4. Activation of protein kinase C-mitogen-activated protein kinase signaling in response to inositol starvation triggers Sir2p-dependent telomeric silencing in yeast. Lee S, et al. J Biol Chem, 2013 Sep 27. PMID 23943620, Free PMC Article
    5. A genome wide analysis of the response to uncapped telomeres in budding yeast reveals a novel role for the NAD+ biosynthetic gene BNA2 in chromosome end protection. Greenall A, et al. Genome Biol, 2008 Oct 1. PMID 18828915, Free PMC Article

    See all (32) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Molecular evolution and characterization of indoleamine 2,3-dioxygenase (BNA2) from saccharomyces cerevisiae
      Title: Molecular evolution and characterization of fungal indoleamine 2,3-dioxygenases.
    Submit: New GeneRIF Correction

    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 dioxygenase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables heme binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables indoleamine 2,3-dioxygenase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables indoleamine 2,3-dioxygenase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables indoleamine 2,3-dioxygenase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tryptophan 2,3-dioxygenase activity 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 IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in NAD biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in alpha-amino acid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tryptophan catabolic process to kynurenine IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tryptophan catabolic process to kynurenine IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    dioxygenase BNA2
    NP_012612.3
    • Tryptophan 2,3-dioxygenase or indoleamine 2,3-dioxygenase; required for de novo biosynthesis of NAD+ from tryptophan via kynurenine; up-regulated by telomere uncapping, and interacts genetically with capping gene CDC13; overexpression reduces lipid droplet accumulation by skewing glycolytic flux towards biosynthesis of shikimate, aromatic amino acids, and NAD+ during aging and extends lifespan; regulated by Hst1p and Aftp

    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
      578860..580221
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181736.3 → NP_012612.3  TPA: dioxygenase BNA2 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012612.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VWP8, P47125
      UniProtKB/TrEMBL
      A0A8H4F9F6, A6ZQ36, G2WH82
      Conserved Domains (1) summary
      pfam01231
      Location:23 → 444
      IDO; Indoleamine 2,3-dioxygenase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P47125.1

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