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    DSD1 D-serine ammonia-lyase DSD1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 852679, updated on 9-Dec-2024

    Summary

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    Official Symbol
    DSD1
    Official Full Name
    D-serine ammonia-lyase DSD1
    Primary source
    SGD:S000003164
    Locus tag
    YGL196W
    See related
    AllianceGenome:SGD:S000003164; FungiDB:YGL196W; VEuPathDB:YGL196W
    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 D-serine ammonia-lyase activity. Involved in D-serine metabolic process. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See DSD1 in Genome Data Viewer
    Location:
    chromosome: VII
    Exon count:
    1
    Sequence:
    Chromosome: VII; NC_001139.9 (129883..131169)

    Chromosome VII - NC_001139.9Genomic Context describing neighboring genes Neighboring gene Yip4p Neighboring gene Mds3p Neighboring gene Gcn1p Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001139.9

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. A novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae. Ito T, et al. Biochem J, 2008 Jan 15. PMID 17937657
    2. Enzymatic assay of D-serine using D-serine dehydratase from Saccharomyces cerevisiae. Ito T, et al. Anal Biochem, 2007 Dec 15. PMID 17869212
    3. Insights into the structural properties of D-serine dehydratase from Saccharomyces cerevisiae: an FT-IR spectroscopic and in silico approach. Baldassarre M, et al. Biochimie, 2011 Mar. PMID 21130133
    4. Turning pyridoxal-5'-phosphate-dependent enzymes into thermostable binding proteins: D-Serine dehydratase from baker's yeast as a case study. Baldassarre M, et al. Biochimie, 2012 Feb. PMID 21896305
    5. Role of zinc ion for catalytic activity in d-serine dehydratase from Saccharomyces cerevisiae. Ito T, et al. FEBS J, 2012 Feb. PMID 22176976

    See all (27) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Data show that the Y203 does not participate in the protonation of the pyridine nitrogen (N1) of PLP, and d-serine dehydratase Dsd1p uses the cofactor in an N1-unprotonated state.
      Title: Reaction mechanism of Zn2+-dependent d-serine dehydratase: role of a conserved tyrosine residue interacting with pyridine ring nitrogen of pyridoxal 5'-phosphate.
    2. Data suggest that d-Serine dehydratase catalyzes the alpha-hydrogen abstraction and hydroxyl group elimination in a concerted fashion.
      Title: Role of zinc ion for catalytic activity in d-serine dehydratase from Saccharomyces cerevisiae.
    3. zinc is involved in the elimination of the hydroxy group of D-serine and D-threonine. D-Serine dehydratase of S. cerevisiae is probably the first example of a eukaryotic D-serine dehydratase and that of a specifically zinc-dependent pyridoxal enzyme
      Title: A novel zinc-dependent D-serine dehydratase from Saccharomyces cerevisiae.
    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 D-serine ammonia-lyase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables D-serine ammonia-lyase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables D-serine ammonia-lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding RCA
    inferred from Reviewed Computational Analysis
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in D-serine catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in D-serine metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in response to toxic substance IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cellular_component ND
    No biological Data available
    more info
    		  

    General protein information

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    Preferred Names
    D-serine ammonia-lyase DSD1
    NP_011319.2
    • D-serine dehydratase (aka D-serine ammonia-lyase); converts D-serine to pyruvate and ammonia by a reaction dependent on pyridoxal 5'-phosphate and zinc; may play a role in D-serine detoxification; L-serine is not a substrate

    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_001139.9 Reference assembly

      Range
      129883..131169
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001181061.1 → NP_011319.2  TPA: D-serine ammonia-lyase DSD1 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_011319.2

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6VTV7, P53095
      UniProtKB/TrEMBL
      A6ZTZ2, B3LHP5, B5VID7, C8Z856, G2WDR0, N1P2U1
      Conserved Domains (1) summary
      cd06817
      Location:13 → 428
      PLPDE_III_DSD; Type III Pyridoxal 5-phosphate (PLP)-Dependent Enzyme Eukaryotic D-Serine Dehydratase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P53095.2

    Gene LinkOut

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