InterPro : IPR006422

Name  D-erythrose-4-phosphate dehydrogenase Short Name  E4P_DH_bac
Type  Family Description  This entry contains a small clade of dehydrogenases in gamma-proteobacteria which utilise NAD+ to oxidize erythrose-4-phosphate (E4P) to 4-phospho-erythronate, a precursor for the de novo synthesis of pyridoxine via 4-hydroxythreonine and D-1-deoxyxylulose []. This enzyme activity appears to have evolved from glyceraldehyde-3-phosphate dehydrogenase, whose substrate differs only in the lack of one carbon relative to E4P. It is possible that some of the GAPDH enzymes may prove to be bifunctional in certain species.
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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

1 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



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)