TDH1/YJL052W Summary Help

Standard Name TDH1 1
Systematic Name YJL052W
Alias GLD3
Feature Type ORF, Verified
Description Glyceraldehyde-3-phosphate dehydrogenase (GAPDH), isozyme 1; involved in glycolysis and gluconeogenesis; tetramer that catalyzes the reaction of glyceraldehyde-3-phosphate to 1,3 bis-phosphoglycerate; detected in the cytoplasm and cell wall; protein abundance increases in response to DNA replication stress; GAPDH-derived antimicrobial peptides secreted by S. cerevisiae are active against a wide variety of wine-related yeasts and bateria (1, 2, 3, 4 and see Summary Paragraph)
Name Description Triose-phosphate DeHydrogenase 1
Gene Product Alias GAPDH 5
Chromosomal Location
ChrX:338271 to 339269 | ORF Map | GBrowse
Gene Ontology Annotations All TDH1 GO evidence and references
  View Computational GO annotations for TDH1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 14 genes
Classical genetics
Large-scale survey
73 total interaction(s) for 59 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 44
  • Affinity Capture-RNA: 4
  • Co-fractionation: 2
  • Co-purification: 2
  • Two-hybrid: 1

Genetic Interactions
  • Dosage Rescue: 1
  • Negative Genetic: 6
  • Phenotypic Suppression: 2
  • Positive Genetic: 4
  • Synthetic Growth Defect: 3
  • Synthetic Lethality: 4

Expression Summary
Length (a.a.) 332
Molecular Weight (Da) 35,750
Isoelectric Point (pI) 8.59
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrX:338271 to 339269 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..999 338271..339269 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 SGDIDS000003588

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is a tetramer catalyzing the reaction of glyceraldehyde-3-phosphate to 1,3 bis-phosphoglycerate. Three unlinked genes, TDH1, TDH2, and TDH3, encode related but not identical polypeptides that form catalytically active homotetramers with different specific activities (1, 2). Interestingly, these catalytically active enzymes are found in the cytoplasm and cell wall. Tdh2p and Tdh3p are detected in exponentially growing cells whereas Tdh1p is primarily detected during stationary phase (5). Therefore, it has been suggested, but not confirmed, that Tdh1p may be involved in a process other than glycolysis because it is synthesized by cells in stationary phase (6).

Glyceraldehyde-3-phosphate dehydrogenase activity is also required during gluconeogenesis, which is the process whereby glucose is synthesized from non-carbohydrate precursors, enabling yeast cells to grow on ethanol, glycerol, or peptone.

The reactions of gluconeogenesis, shown here, mediate conversion of pyruvate to glucose, which is the opposite of glycolysis, the formation of pyruvate from glucose. While these two pathways have several reactions in common, they are not the exact reverse of each other. As the glycolytic enzymes phosphofructokinase (Pfk1p, Pfk2p) and pyruvate kinase (Cdc19p) only function in the forward direction, the gluconeogenesis pathway replaces those steps with the enzymes pyruvate carboxylase (Pyc1p, Pyc2p) and phosphoenolpyruvate carboxykinase (Pck1p) -generating oxaloacetate as an intermediate from pyruvate to phosphoenolpyruvate- and also the enzyme fructose-1,6-bisphosphatase (Fbp1p) (reviewed in 7). Overall, the gluconeogenic reactions convert two molecules of pyruvate to a molecule of glucose, with the expenditure of six high-energy phosphate bonds, four from ATP and two from GTP.

Last updated: 2005-06-17 Contact SGD

References cited on this page View Complete Literature Guide for TDH1
1) McAlister L and Holland MJ  (1985) Isolation and characterization of yeast strains carrying mutations in the glyceraldehyde-3-phosphate dehydrogenase genes. J Biol Chem 260(28):15013-8
2) McAlister L and Holland MJ  (1985) Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes. J Biol Chem 260(28):15019-27
3) Tkach JM, et al.  (2012) Dissecting DNA damage response pathways by analysing protein localization and abundance changes during DNA replication stress. Nat Cell Biol 14(9):966-76
4) Branco P, et al.  (2014) Identification of novel GAPDH-derived antimicrobial peptides secreted by Saccharomyces cerevisiae and involved in wine microbial interactions. Appl Microbiol Biotechnol 98(2):843-53
5) Delgado ML, et al.  (2001) The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall proteins. Microbiology 147(Pt 2):411-7
6) Boucherie H, et al.  (1995) Differential synthesis of glyceraldehyde-3-phosphate dehydrogenase polypeptides in stressed yeast cells. FEMS Microbiol Lett 125(2-3):127-33
7) Klein CJ, et al.  (1998) Glucose control in Saccharomyces cerevisiae: the role of Mig1 in metabolic functions. Microbiology 144 ( Pt 1)():13-24