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
Functions
glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity / NAD binding / NADP binding
Processes
glucose metabolic process / glycolytic process
Components
cytoplasm
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
ResourceLink
UniProtKB IDP00362
UniProtKB Entry NameG3P_GEOSE
GenBank Gene IDM24493
General References
  1. 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]
  2. 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]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02263D-glyceraldehyde 3-phosphateexperimentalunknownDetails