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LAT1 dihydrolipoyllysine-residue acetyltransferase [ Saccharomyces cerevisiae S288C ]

Gene ID: 855653, updated on 17-May-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
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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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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