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    LAT1 dihydrolipoyllysine-residue acetyltransferase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855653, updated on 7-Jul-2024

    Summary

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    Gene symbol
    LAT1
    Gene description
    dihydrolipoyllysine-residue acetyltransferase
    Primary source
    FungiDB:YNL071W
    Locus tag
    YNL071W
    See related
    SGD:S000005015; AllianceGenome:SGD:S000005015; VEuPathDB:YNL071W
    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
    ODP2; PDA2
    Summary
    Enables dihydrolipoyllysine-residue acetyltransferase activity. Involved in acetyl-CoA biosynthetic process from pyruvate. Located in mitochondrion. Part of mitochondrial pyruvate dehydrogenase complex. Human ortholog(s) of this gene implicated in pyruvate decarboxylase deficiency. Orthologous to human DLAT (dihydrolipoamide S-acetyltransferase). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See LAT1 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (491523..492971)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene lysine--tRNA ligase MSK1 Neighboring gene ribonuclease H2 catalytic subunit RNH201 Neighboring gene Tom7p Neighboring gene ribosomal 60S subunit protein L16B

    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. Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. The "breathing" core and its functional relationship to protein dynamics. Zhou ZH, et al. J Biol Chem, 2001 Jun 15. PMID 11285267
    2. On the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complex. Stoops JK, et al. J Biol Chem, 1997 Feb 28. PMID 9038189, Free PMC Article
    3. Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Niu XD, et al. Proc Natl Acad Sci U S A, 1988 Oct. PMID 3050999, Free PMC Article
    4. Overexpression and mutagenesis of the catalytic domain of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Niu XD, et al. Biochemistry, 1990 Sep 18. PMID 2271545
    5. Functional analysis of the domains of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Lawson JE, et al. Biochemistry, 1991 Nov 26. PMID 1958662

    See all (100) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 acyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables dihydrolipoyllysine-residue acetyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables dihydrolipoyllysine-residue acetyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables dihydrolipoyllysine-residue acetyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in acetyl-CoA biosynthetic process from pyruvate IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in acetyl-CoA biosynthetic process from pyruvate IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in acetyl-CoA biosynthetic process from pyruvate IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in small molecule metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in mitochondrial matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of pyruvate dehydrogenase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of pyruvate dehydrogenase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of pyruvate dehydrogenase complex IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    dihydrolipoyllysine-residue acetyltransferase
    NP_014328.3
    • Dihydrolipoamide acetyltransferase component (E2) of the PDC; the pyruvate dehydrogenase complex (PDC) catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA; metabolic longevity factor required for calorie restriction-mediated life span extension

    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
      491523..492971
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182909.3 → NP_014328.3  TPA: dihydrolipoyllysine-residue acetyltransferase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014328.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W1A8, P12695
      UniProtKB/TrEMBL
      A0A8H4BVS7, B3LNT0, B5VQX4, C7GIL5, N1NXZ7
      Conserved Domains (1) summary
      TIGR01349
      Location:36 → 482
      PDHac_trf_mito; pyruvate dehydrogenase complex dihydrolipoamide acetyltransferase, long form
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P12695.1

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