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

Gene ID: 853482, updated on 24-Jul-2025
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 L-tryptophan. Located in cytoplasm. Orthologous to human HAAO (3-hydroxyanthranilate 3,4-dioxygenase). [provided by Alliance of Genome Resources, Apr 2025]
Orthologs
all
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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 Sequence:
NC_001142.9

Go to nucleotide: Graphics FASTA GenBank

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 (51) citations in PubMed

GeneRIFs: Gene References Into Functions

Products Interactant Other Gene Complex Source Pubs Description

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
  
enables oxidoreductase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in 'de novo' NAD+ biosynthetic process from L-tryptophan IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in 'de novo' NAD+ biosynthetic process from L-tryptophan IEA
Inferred from Electronic Annotation
more info
  
involved_in 'de novo' NAD+ biosynthetic process from L-tryptophan IGI
Inferred from Genetic Interaction
more info
 PubMed 
involved_in L-tryptophan catabolic process IEA
Inferred from Electronic Annotation
more info
  
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
  
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
  
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

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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

    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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