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Identification
NameGlyceraldehyde-3-phosphate dehydrogenase 1
Synonyms
  • GAPDH 1
Gene NameTDH1
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Specific FunctionD-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Cellular LocationCytoplasm
SMPDB Pathways
Glycolysis IPW002386 ThumbThumb?image type=greyscaleThumb?image type=simple
Vitamin B6PW002488 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glycolysis / Gluconeogenesisec00010 Map00010
SMPDB Reactions
D-Glyceraldehyde 3-phosphate + NAD + Phosphoric acidGlyceric acid 1,3-biphosphate + NADH
D-Erythrose 4-phosphate + NAD + waterNADH + hydron + 4-Phospho-D-erythronate
KEGG Reactions
NAD + D-Glyceraldehyde 3-phosphate + phosphateNADH + 3-phospho-D-glyceroyl dihydrogen phosphate + hydron
Metabolites
YMDB IDNameView
YMDB00110NADShow
YMDB00115D-Glyceraldehyde 3-phosphateShow
YMDB00143NADHShow
YMDB00223D-Erythrose 4-phosphateShow
YMDB00270Glyceric acid 1,3-biphosphateShow
YMDB00412NAD(+)Show
YMDB006723-phospho-D-glyceroyl dihydrogen phosphateShow
YMDB00862hydronShow
YMDB00890waterShow
YMDB00907phosphateShow
YMDB16145Phosphoric acidShow
YMDB162684-Phospho-D-erythronateShow
GO Classification
Component
Not Available
Function
oxidoreductase activity
catalytic activity
NAD or NADH binding
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
binding
nucleotide binding
glyceraldehyde-3-phosphate dehydrogenase activity
Process
oxidation reduction
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
metabolic process
glucose metabolic process
Gene Properties
Chromosome Locationchromosome 10
LocusYJL052W
Gene Sequence>999 bp ATGATCAGAATTGCCATTAACGGTTTCGGTAGAATCGGTAGATTGGTCTTGAGATTGGCT TTGCAAAGAAAAGACATTGAGGTTGTTGCTGTCAACGATCCATTTATCTCTAACGATTAT GCTGCTTACATGGTCAAGTACGATTCTACTCATGGTAGATACAAGGGTACTGTTTCCCAT GACGACAAGCACATCATCATTGATGGTGTCAAGATCGCTACCTACCAAGAAAGAGACCCA GCTAACTTGCCATGGGGTTCTCTAAAGATCGATGTCGCTGTTGACTCCACTGGTGTTTTC AAGGAATTGGACACCGCTCAAAAGCACATTGACGCTGGTGCCAAGAAGGTTGTCATCACT GCTCCATCTTCTTCTGCTCCAATGTTTGTTGTTGGTGTTAACCACACTAAATACACTCCA GACAAGAAGATTGTCTCCAACGCTTCTTGTACCACCAACTGTTTGGCTCCATTGGCCAAG GTTATCAACGATGCTTTCGGTATTGAAGAAGGTTTGATGACCACTGTTCACTCCATGACC GCCACTCAAAAGACTGTTGATGGTCCATCCCACAAGGACTGGAGAGGTGGTAGAACCGCT TCCGGTAACATTATCCCATCCTCTACCGGTGCTGCTAAGGCTGTCGGTAAGGTCTTGCCA GAATTGCAAGGTAAGTTGACCGGTATGGCTTTCAGAGTCCCAACCGTCGATGTTTCCGTT GTTGACTTGACTGTCAAGTTGGAAAAGGAAGCTACTTACGACCAAATCAAGAAGGCTGTT AAGGCTGCCGCTGAAGGTCCAATGAAGGGTGTTTTGGGTTACACCGAAGATGCCGTTGTC TCCTCTGATTTCTTGGGTGACACTCACGCTTCCATCTTCGATGCCTCCGCTGGTATCCAA TTGTCTCCAAAGTTCGTCAAGTTGATTTCCTGGTACGATAACGAATACGGTTACTCCGCC AGAGTTGTTGACTTGATCGAATATGTTGCCAAGGCTTAA
Protein Properties
Pfam Domain Function
Protein Residues332
Protein Molecular Weight35749.60156
Protein Theoretical pI8.57
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Glyceraldehyde-3-phosphate dehydrogenase 1 MIRIAINGFGRIGRLVLRLALQRKDIEVVAVNDPFISNDYAAYMVKYDSTHGRYKGTVSH DDKHIIIDGVKIATYQERDPANLPWGSLKIDVAVDSTGVFKELDTAQKHIDAGAKKVVIT APSSSAPMFVVGVNHTKYTPDKKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSMT ATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSV VDLTVKLEKEATYDQIKKAVKAAAEGPMKGVLGYTEDAVVSSDFLGDTHASIFDASAGIQ LSPKFVKLISWYDNEYGYSARVVDLIEYVAKA
References
External Links
ResourceLink
Saccharomyces Genome Database TDH1
Uniprot IDP00360
Uniprot NameG3P1_YEAST
GenBank Gene IDAY693001
Genebank Protein ID51013453
General Reference
  • Holland, J. P., Labieniec, L., Swimmer, C., Holland, M. J. (1983). "Homologous nucleotide sequences at the 5' termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehydrogenase gene families. The primary structure of a third yeast glyceraldehyde-3-phosphate dehydrogenase gene." J Biol Chem 258:5291-5299.6833300
  • Galibert, F., Alexandraki, D., Baur, A., Boles, E., Chalwatzis, N., Chuat, J. C., Coster, F., Cziepluch, C., De Haan, M., Domdey, H., Durand, P., Entian, K. D., Gatius, M., Goffeau, A., Grivell, L. A., Hennemann, A., Herbert, C. J., Heumann, K., Hilger, F., Hollenberg, C. P., Huang, M. E., Jacq, C., Jauniaux, J. C., Katsoulou, C., Karpfinger-Hartl, L., et, a. l. .. (1996). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." EMBO J 15:2031-2049.8641269
  • Hu, Y., Rolfs, A., Bhullar, B., Murthy, T. V., Zhu, C., Berger, M. F., Camargo, A. A., Kelley, F., McCarron, S., Jepson, D., Richardson, A., Raphael, J., Moreira, D., Taycher, E., Zuo, D., Mohr, S., Kane, M. F., Williamson, J., Simpson, A., Bulyk, M. L., Harlow, E., Marsischky, G., Kolodner, R. D., LaBaer, J. (2007). "Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Genome Res 17:536-543.17322287
  • Norbeck, J., Blomberg, A. (1997). "Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins." Yeast 13:1519-1534.9509572
  • Kadokura, T., Ito, T., Takano, S., Nakazato, A., Hara, H., Watanabe, S., Kudo, T., Takeda, M., Kaneko, T. (2000). "Divergence of glyceraldehyde-3-phosphate dehydrogenase isozymes in Saccharomyces cerevisiae complex." Syst Appl Microbiol 23:198-205.10930071
  • Grandier-Vazeille, X., Bathany, K., Chaignepain, S., Camougrand, N., Manon, S., Schmitter, J. M. (2001). "Yeast mitochondrial dehydrogenases are associated in a supramolecular complex." Biochemistry 40:9758-9769.11502169
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Faergeman, N. J., Mann, M., Jensen, O. N. (2005). "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Mol Cell Proteomics 4:310-327.15665377
  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956