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    BIO3 adenosylmethionine-8-amino-7-oxononanoate transaminase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855795, updated on 17-May-2024

    Summary

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    Gene symbol
    BIO3
    Gene description
    adenosylmethionine-8-amino-7-oxononanoate transaminase
    Primary source
    FungiDB:YNR058W
    Locus tag
    YNR058W
    See related
    SGD:S000005341; AllianceGenome:SGD:S000005341; VEuPathDB:YNR058W
    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 adenosylmethionine-8-amino-7-oxononanoate transaminase activity. Involved in biotin biosynthetic process. Predicted to be located in cytoplasm. Predicted to be active in mitochondrion. Orthologous to human ETNPPL (ethanolamine-phosphate phospho-lyase). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See BIO3 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (734291..735733)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene Bio5p Neighboring gene dethiobiotin synthase Neighboring gene putative alpha-1,3-mannosyltransferase Neighboring gene ferric-chelate reductase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001146.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The reacquisition of biotin prototrophy in Saccharomyces cerevisiae involved horizontal gene transfer, gene duplication and gene clustering. Hall C, et al. Genetics, 2007 Dec. PMID 18073433, Free PMC Article
    2. Characterization of the biotin biosynthesis pathway in Saccharomyces cerevisiae and evidence for a cluster containing BIO5, a novel gene involved in vitamer uptake. Phalip V, et al. Gene, 1999 May 17. PMID 10333520
    3. A genetic approach of wine yeast fermentation capacity in nitrogen-starvation reveals the key role of nitrogen signaling. Brice C, et al. BMC Genomics, 2014 Jun 19. PMID 24947828, Free PMC Article
    4. Identification by comparative transcriptomics of core regulatory genes for higher alcohol production in a top-fermenting yeast at different temperatures in beer fermentation. Sun ZG, et al. Appl Microbiol Biotechnol, 2019 Jun. PMID 31073877
    5. Yeast genes involved in sulfur and nitrogen metabolism affect the production of volatile thiols from Sauvignon Blanc musts. Harsch MJ, et al. Appl Microbiol Biotechnol, 2013 Jan. PMID 22684328

    See all (21) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Quantitative trait loci analysis suggest that polymorphism in the coding region of GCN1, MDS3, ARG81 and BIO3 could account for differences in nitrogen requirement.
      Title: A genetic approach of wine yeast fermentation capacity in nitrogen-starvation reveals the key role of nitrogen signaling.
    Submit: New GeneRIF Correction

    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 adenosylmethionine-8-amino-7-oxononanoate transaminase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables adenosylmethionine-8-amino-7-oxononanoate transaminase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables adenosylmethionine-8-amino-7-oxononanoate transaminase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dethiobiotin synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables pyridoxal phosphate binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transaminase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in biotin biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in biotin biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in biotin biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in biotin biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm ISS
    Inferred from Sequence or Structural Similarity
    more info
    		 PubMed 
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    adenosylmethionine-8-amino-7-oxononanoate transaminase
    NP_014456.1
    • 7,8-diamino-pelargonic acid aminotransferase (DAPA); catalyzes the second step in the biotin biosynthesis pathway; BIO3 is in a cluster of 3 genes (BIO3, BIO4, and BIO5) that mediate biotin synthesis; BIO3 and BIO4 were acquired by horizontal gene transfer (HGT) from bacteria

    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_001146.8 Reference assembly

      Range
      734291..735733
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183235.1 → NP_014456.1  TPA: adenosylmethionine-8-amino-7-oxononanoate transaminase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014456.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W1N3, E9P967, P50277, Q4R1J0
      UniProtKB/TrEMBL
      A0A8H4BVY9, A6ZSD2, B3LPI5, C7GIY7, C8ZFT7
      Conserved Domains (1) summary
      cl18945
      Location:15 → 472
      AAT_I; Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the ...
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P50277.1

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