PDC5/YLR134W Summary Help

Standard Name PDC5 1
Systematic Name YLR134W
Feature Type ORF, Verified
Description Minor isoform of pyruvate decarboxylase; key enzyme in alcoholic fermentation, decarboxylates pyruvate to acetaldehyde, regulation is glucose- and ethanol-dependent, repressed by thiamine, involved in amino acid catabolism (2, 3, 4, 5, 6, 7, 8 and see Summary Paragraph)
Name Description Pyruvate DeCarboxylase 9
Chromosomal Location
ChrXII:410723 to 412414 | ORF Map | GBrowse
Gene Ontology Annotations All PDC5 GO evidence and references
  View Computational GO annotations for PDC5
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 12 genes
Classical genetics
Large-scale survey
47 total interaction(s) for 35 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 17
  • Affinity Capture-RNA: 4
  • Biochemical Activity: 1
  • Co-purification: 1
  • PCA: 1
  • Protein-peptide: 1
  • Reconstituted Complex: 1
  • Two-hybrid: 1

Genetic Interactions
  • Negative Genetic: 11
  • Phenotypic Enhancement: 4
  • Positive Genetic: 1
  • Synthetic Growth Defect: 1
  • Synthetic Lethality: 2
  • Synthetic Rescue: 1

Expression Summary
Length (a.a.) 563
Molecular Weight (Da) 61,912
Isoelectric Point (pI) 6.41
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrXII:410723 to 412414 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1692 410723..412414 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000004124

PDC1, PDC5, and PDC6 encode three different isozymes of pyruvate decarboxylase (2, 1, 4), an enzyme which catalyzes the degradation of pyruvate into acetaldehyde and carbon dioxide, as shown here. As the key enzyme in alcoholic fermentation, pyruvate decarboxylase commits the end product of glycolysis, pyruvate, to ethanol production rather than to its other possible major metabolic fates: the TCA cycle/aerobic respiration (pyruvate converted to acetyl-CoA by the pyruvate dehydrogenase complex) or gluconeogenesis (pyruvate converted to oxaloacetate, by pyruvate carboxylase) (7 and references therein). PDC1, PDC5, and PDC6 can also decarboxylate other 2-oxo acids such as indolepyruvate and 2-keto-3-methyl-valerate, and this activity contributes to the catabolism of the amino acids isoleucine, phenylalanine, tryptophan, and valine (8 and references therein).

Pdc1p is the major isozyme and is strongly expressed in actively fermenting yeast cells. The nearly identical Pdc5p also functions during glycolytic fermentation, but is expressed only in the absence of PDC1 (1) or under thiamine limitation (3). Both PDC1 and PDC5 are under PDC autoregulation such that their promoters are activated in the absence of Pdc1p (10 and references therein). Expression of PDC1 and PDC5 also requires the transcription factor Pdc2p (11 and references therein). The third isozyme, Pdc6p, is not expressed during glucose fermentation and seems to be functional during growth on nonfermentable carbon sources (4). Transcription of PDC6 is dramatically induced under conditions of sulfur limitation, suggesting that it has a role during sulfur-limited growth (12). Consistent with this, the PDC6 gene encodes fewer sulfur-containing amino acids than does either PDC1 or PDC5 (6 codons vs. 17 or 18, respectively) (12).

Pyruvate decarboxylase is conserved among yeast, bacteria and plants and has been well-characterized on both the structural and enzymatic levels. The active enzyme is a homotetramer and requires thiamin diphosphate (ThDP) and Mg++ cofactors (13 and references therein).

Last updated: 2007-06-01 Contact SGD

References cited on this page View Complete Literature Guide for PDC5
1) Seeboth PG, et al.  (1990) pdc1(0) mutants of Saccharomyces cerevisiae give evidence for an additional structural PDC gene: cloning of PDC5, a gene homologous to PDC1. J Bacteriol 172(2):678-85
2) Kellermann E, et al.  (1986) Analysis of the primary structure and promoter function of a pyruvate decarboxylase gene (PDC1) from Saccharomyces cerevisiae. Nucleic Acids Res 14(22):8963-77
3) Muller EH, et al.  (1999) Thiamine repression and pyruvate decarboxylase autoregulation independently control the expression of the Saccharomyces cerevisiae PDC5 gene. FEBS Lett 449(2-3):245-50
4) Hohmann S  (1991) Characterization of PDC6, a third structural gene for pyruvate decarboxylase in Saccharomyces cerevisiae. J Bacteriol 173(24):7963-9
5) Liesen T, et al.  (1996) ERA, a novel cis-acting element required for autoregulation and ethanol repression of PDC1 transcription in Saccharomyces cerevisiae. Mol Microbiol 21(3):621-32
6) Hohmann S and Cederberg H  (1990) Autoregulation may control the expression of yeast pyruvate decarboxylase structural genes PDC1 and PDC5. Eur J Biochem 188(3):615-21
7) Pronk JT, et al.  (1996) Pyruvate metabolism in Saccharomyces cerevisiae. Yeast 12(16):1607-33
8) Dickinson JR, et al.  (2003) The catabolism of amino acids to long chain and complex alcohols in Saccharomyces cerevisiae. J Biol Chem 278(10):8028-34
9) Schmitt HD and Zimmermann FK  (1982) Genetic analysis of the pyruvate decarboxylase reaction in yeast glycolysis. J Bacteriol 151(3):1146-52
10) Eberhardt I, et al.  (1999) Autoregulation of yeast pyruvate decarboxylase gene expression requires the enzyme but not its catalytic activity. Eur J Biochem 262(1):191-201
11) Mojzita D and Hohmann S  (2006) Pdc2 coordinates expression of the THI regulon in the yeast Saccharomyces cerevisiae. Mol Genet Genomics 276(2):147-61
12) Boer VM, et al.  (2003) The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur. J Biol Chem 278(5):3265-74
13) Konig S  (1998) Subunit structure, function and organisation of pyruvate decarboxylases from various organisms. Biochim Biophys Acta 1385(2):271-86