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BNA2 dioxygenase BNA2 [ Saccharomyces cerevisiae S288C ]

Gene ID: 853541, updated on 17-May-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
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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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 metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in organic cyclic compound 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

Gene LinkOut

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