InterPro : IPR006424

Name  Glyceraldehyde-3-phosphate dehydrogenase, type I Short Name  Glyceraldehyde-3-P_DH_1
Type  Family Description  This group of sequences represent glyceraldehyde-3-phosphate dehydrogenase (GAPDH), the enzyme responsible for the interconversion of 1,3-diphosphoglycerate and glyceraldehyde-3-phosphate, a central step in glycolysis and gluconeogenesis. Forms exist which utilise NAD (), NADP () or either (). In some species, NAD- and NADP- utilising forms exist, generally being responsible for reactions in the anabolic and catabolic directions respectively []. An additional form of gap gene is found in gamma proteobacteria and is responsible for the conversion of erythrose-4-phosphate (E4P) to 4-phospho-erythronate in the biosynthesis of pyridoxine []. This pathway of pyridoxine biosynthesis appears to be limited, however, to a relatively small number of bacterial species although it is prevalent among the gamma-proteobacteria []. This enzyme is described by . These two groups of sequences exhibit a close evolutionary relationship. There exists the possibility that some forms of GAPDH may be bifunctional and act on E4P in species which make pyridoxine and via hydroxythreonine and lack a separate E4PDH enzyme (for instance, the GAPDH from Bacillus stearothermophilushas been shown to possess a limited E4PD activity as well as a robust GAPDH activity []).
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

4 Contains

Id Name Short Name Type
IPR016040 NAD(P)-binding domain NAD(P)-bd_dom Domain
IPR020829 Glyceraldehyde 3-phosphate dehydrogenase, catalytic domain GlycerAld_3-P_DH_cat Domain
IPR020828 Glyceraldehyde 3-phosphate dehydrogenase, NAD(P) binding domain GlycerAld_3-P_DH_NAD(P)-bd Domain
IPR020830 Glyceraldehyde 3-phosphate dehydrogenase, active site GlycerAld_3-P_DH_AS Active_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR020831 Glyceraldehyde/Erythrose phosphate dehydrogenase family GlycerAld/Erythrose_P_DH Family

4 Publications

First Author Title Year Journal Volume Pages
Zhao G Biochemical characterization of gapB-encoded erythrose 4-phosphate dehydrogenase of Escherichia coli K-12 and its possible role in pyridoxal 5'-phosphate biosynthesis. 1995 J Bacteriol 177 2804-12
Fillinger S Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. 2000 J Biol Chem 275 14031-7
Mittenhuber G Phylogenetic analyses and comparative genomics of vitamin B6 (pyridoxine) and pyridoxal phosphate biosynthesis pathways. 2001 J Mol Microbiol Biotechnol 3 1-20
Boschi-Muller S Comparative enzymatic properties of GapB-encoded erythrose-4-phosphate dehydrogenase of Escherichia coli and phosphorylating glyceraldehyde-3-phosphate dehydrogenase. 1997 J Biol Chem 272 15106-12



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)