Glyceraldehyde-3-phosphate dehydrogenase
Details
- Name
- Glyceraldehyde-3-phosphate dehydrogenase
- Synonyms
- 1.2.1.12
- GAPDH
- NAD-dependent glyceraldehyde-3-phosphate dehydrogenase
- Gene Name
- gap
- Organism
- Geobacillus stearothermophilus
- Amino acid sequence
>lcl|BSEQ0011853|Glyceraldehyde-3-phosphate dehydrogenase MAVKVGINGFGRIGRNVFRAALKNPDIEVVAVNDLTDANTLAHLLKYDSVHGRLDAEVSV NGNNLVVNGKEIIVKAERDPENLAWGEIGVDIVVESTGRFTKREDAAKHLEAGAKKVIIS APAKNEDITIVMGVNQDKYDPKAHHVISNASCTTNCLAPFAKVLHEQFGIVRGMMTTVHS YTNDQRILDLPHKDLRRARAAAESIIPTTTGAAKAVALVLPELKGKLNGMAMRVPTPNVS VVDLVAELEKEVTVEEVNAALKAAAEGELKGILAYSEEPLVSRDYNGSTVSSTIDALSTM VIDGKMVKVVSWYDNETGYSHRVVDLAAYIASKGL
- Number of residues
- 335
- Molecular Weight
- 36074.99
- Theoretical pI
- 6.43
- GO Classification
- Functionsglyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / NAD binding / NADP bindingProcessesglucose metabolic process / glycolytic processComponentscytoplasm
- General Function
- Nadp binding
- Specific Function
- Catalyzes the oxidative phosphorylation of glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor NAD. The first reaction step involves the formation of a hemiacetal intermediate between G3P and a cysteine residue, and this hemiacetal intermediate is then oxidized to a thioester, with concomitant reduction of NAD to NADH. The reduced NADH is then exchanged with the second NAD, and the thioester is attacked by a nucleophilic inorganic phosphate to produce BPG.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0005110|1008 bp ATGGCAGTCAAAGTGGGAATCAACGGATTTGGCCGCATCGGACGCAACGTCTTCCGCGCG GCATTGAAAAACCCGGACATTGAAGTGGTGGCGGTGAACGATTTAACCGATGCGAATACG CTTGCTCATTTGTTGAAGTACGACTCTGTCCATGGCCGTTTGGATGCCGAAGTGTCGGTG AACGGCAACAACTTGGTCGTCAACGGCAAAGAAATCATCGTCAAGGCGGAACGCGATCCG GAGAACTTGGCGTGGGGCGAGATCGGCGTTGACATCGTCGTTGAGTCGACCGGCCGCTTC ACGAAACGCGAAGACGCCGCCAAACATTTGGAAGCGGGTGCGAAAAAAGTGATCATTTCC GCCCCGGCGAAAAACGAAGACATTACGATCGTCATGGGCGTCAACCAAGACAAATACGAT CCGAAAGCCCATCATGTCATCTCGAACGCGTCGTGCACGACGAACTGCTTGGCGCCGTTT GCCAAAGTGCTGCATGAACAATTCGGCATCGTCCGCGGCATGATGACGACCGTTCACTCG TACACAAACGACCAACGAATTTTGGACTTGCCGCATAAAGATTTGCGCCGGGCTCGCGCC GCGGCCGAATCGATCATTCCGACGACGACCGGGGCGGCGAAAGCGGTCGCGCTCGTTTTG CCGGAATTGAAAGGAAAGTTGAACGGCATGGCGATGCGCGTGCCGACGCCGAACGTATCC GTTGTCGACTTGGTGGCGGAATTGGAAAAAGAAGTGACGGTCGAAGAAGTGAATGCCGCG TTGAAAGCAGCAGCTGAAGGCGAGCTGAAAGGCATTTTGGCCTACAGCGAAGAACCGCTC GTGTCGCGCGACTACAACGGCAGCACCGTTTCGTCGACGATCGACGCGTTGTCGACAATG GTCATTGATGGCAAAATGGTGAAAGTCGTTTCGTGGTATGACAACGAAACGGGCTATTCG CACCGCGTCGTCGACTTAGCTGCCTACATCGCCTCGAAAGGGCTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00362 UniProtKB Entry Name G3P_GEOSE GenBank Gene ID M24493 - General References
- Tesfay HS, Amelunxen RE, Goldberg ID: Nucleotide sequences of genes encoding heat-stable and heat-labile glyceraldehyde-3-phosphate dehydrogenases; amino acid sequence and protein thermostability. Gene. 1989 Oct 30;82(2):237-48. [Article]
- Tesfay HS, Amelunxen RE, Goldberg ID: Nucleotide sequences of genes encoding heat-stable and heat-labile glyceraldehyde-3-phosphate dehydrogenases; amino acid sequence and protein thermostability. Gene. 1990 Sep 28;94(1):144. [Article]
- Branlant C, Oster T, Branlant G: Nucleotide sequence determination of the DNA region coding for Bacillus stearothermophilus glyceraldehyde-3-phosphate dehydrogenase and of the flanking DNA regions required for its expression in Escherichia coli. Gene. 1989 Jan 30;75(1):145-55. [Article]
- Walker JE, Carne AF, Runswick MJ, Bridgen J, Harris JI: D-glyceraldehyde-3-phosphate dehydrogenase. Complete amino-acid sequence of the enzyme from Bacillus stearothermophilus. Eur J Biochem. 1980 Jul;108(2):549-65. [Article]
- Biesecker G, Harris JI, Thierry JC, Walker JE, Wonacott AJ: Sequence and structure of D-glyceraldehyde 3-phosphate dehydrogenase from Bacillus stearothermophilus. Nature. 1977 Mar 24;266(5600):328-33. [Article]
- Skarzynski T, Moody PC, Wonacott AJ: Structure of holo-glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus at 1.8 A resolution. J Mol Biol. 1987 Jan 5;193(1):171-87. [Article]
- Skarzynski T, Wonacott AJ: Coenzyme-induced conformational changes in glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus. J Mol Biol. 1988 Oct 20;203(4):1097-118. [Article]
- Didierjean C, Rahuel-Clermont S, Vitoux B, Dideberg O, Branlant G, Aubry A: A crystallographic comparison between mutated glyceraldehyde-3-phosphate dehydrogenases from Bacillus stearothermophilus complexed with either NAD+ or NADP+. J Mol Biol. 1997 May 16;268(4):739-59. [Article]
- Didierjean C, Corbier C, Fatih M, Favier F, Boschi-Muller S, Branlant G, Aubry A: Crystal structure of two ternary complexes of phosphorylating glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus with NAD and D-glyceraldehyde 3-phosphate. J Biol Chem. 2003 Apr 11;278(15):12968-76. Epub 2003 Feb 4. [Article]
- Moniot S, Bruno S, Vonrhein C, Didierjean C, Boschi-Muller S, Vas M, Bricogne G, Branlant G, Mozzarelli A, Corbier C: Trapping of the thioacylglyceraldehyde-3-phosphate dehydrogenase intermediate from Bacillus stearothermophilus. Direct evidence for a flip-flop mechanism. J Biol Chem. 2008 Aug 1;283(31):21693-702. doi: 10.1074/jbc.M802286200. Epub 2008 May 14. [Article]