LAT1/YNL071W Summary Help

Standard Name LAT1
Systematic Name YNL071W
Alias ODP2 , PDA2
Feature Type ORF, Verified
Description Dihydrolipoamide acetyltransferase component (E2) of pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA (1 and see Summary Paragraph)
Chromosomal Location
ChrXIV:491523 to 492971 | ORF Map | GBrowse
Gbrowse
Gene Ontology Annotations All LAT1 GO evidence and references
  View Computational GO annotations for LAT1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
High-throughput
Pathways
Mutant phenotypes All LAT1 Phenotype evidence and references
Classical genetics
null
overexpression
Large-scale survey
null
Resources
interactions All LAT1 Interaction evidence and references
248 total interaction(s) for 158 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 20
  • Affinity Capture-RNA: 1
  • Protein-RNA: 1
Genetic Interactions
  • Negative Genetic: 167
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 3
  • Positive Genetic: 50
  • Synthetic Growth Defect: 2
  • Synthetic Lethality: 2
  • Synthetic Rescue: 1
Resources
Expression Summary
histogram
Resources
Protein Information All LAT1 Protein evidence and references
Localization
Phosphorylation PhosphoGRID | PhosphoPep Database
Structure
Homologs
sequence information
ChrXIV:491523 to 492971 | ORF Map | GBrowse
SGD ORF map
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..1449 491523..492971 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
Resources
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000005015
SUMMARY PARAGRAPH for LAT1

LAT1 encodes the dihydrolipoamide acetyltransferase component (E2) of the yeast pyruvate dehydrogenase complex, which catalyzes the oxidative decarboxylation of pyruvate to acetyl-CoA (2, 1, 3, 4). Pyruvate dehydrogenase complexes are extremely large multienzyme structures, and the E2 subunit provides the central core, playing both an enzymatic and structural role (3). Multiple E2 (Lat1p) subunits act as a scaffold for the binding of pyruvate dehydrogenase (E1; Pda1p and Pdb1p), dihydrolipoamide dehydrogenase (E3; Lpd1p), and the Lpd1p-binding protein (Protein X; Pdx1p) (2, 3). The pyruvate dehydrogenase complex is located in the mitochondrial matrix (5). Cells lacking Lat1p are viable, but they lacked pyruvate dehydrogenase activity (2). Mutations in DLAT, the human dihydrolipoamide acetyltransferase gene, cause lactic acidosis (maple syrup urine disease, type II) (OMIM) (6).

Last updated: 2005-07-01

References cited on this page View Complete Literature Guide for LAT1
1) Niu XD, et al.  (1988) Cloning and nucleotide sequence of the gene for dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 85(20):7546-50
2) Lawson JE, et al.  (1991) Functional analysis of the domains of dihydrolipoamide acetyltransferase from Saccharomyces cerevisiae. Biochemistry 30(47):11249-54
3) Stoops JK, et al.  (1997) On the unique structural organization of the Saccharomyces cerevisiae pyruvate dehydrogenase complex. J Biol Chem 272(9):5757-64
4) Pronk JT, et al.  (1996) Pyruvate metabolism in Saccharomyces cerevisiae. Yeast 12(16):1607-33
5) Lawson JE, et al.  (1991) Disruption and mutagenesis of the Saccharomyces cerevisiae PDX1 gene encoding the protein X component of the pyruvate dehydrogenase complex. Biochemistry 30(11):2834-9
6) Foury F  (1997) Human genetic diseases: a cross-talk between man and yeast. Gene 195(1):1-10