InterPro : IPR020630

Name  Tetrahydrofolate dehydrogenase/cyclohydrolase, catalytic domain Short Name  THF_DH/CycHdrlase_cat_dom
Type  Domain Description  Enzymes that participate in the transfer of one-carbon units require the coenzyme tetrahydrofolate (THF).Various reactions generate one-carbon derivatives of THF, which can be interconverted between differentoxidation states by methylene-THF dehydrogenase (), methenyl-THF cyclohydrolase ()and formyl-THF synthetase () [, ]. The dehydrogenase and cyclohydrolaseactivities are expressed by a variety of multifunctional enzymes, including the tri-functional eukaryoticC1-tetrahydrofolate synthase []; a bifunctional eukaryotic mitochondrial protein; and thebifunctional Escherichia colifolD protein [, ]. Methylene-tetrahydrofolate dehydrogenase andmethenyltetrahydrofolate cyclo-hydrolase share an overlapping active site [], and as such areusually located together in proteins, acting in tandem on the carbon-nitrogen bonds of substrates otherthan peptide bonds.This entry represents the N-terminal catalytic domain of these enzymes.
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0 Child Features

1 Contains

Id Name Short Name Type
IPR020631 Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain THF_DH/CycHdrlase_NAD-bd_dom Domain

1 Found In

Id Name Short Name Type
IPR000672 Tetrahydrofolate dehydrogenase/cyclohydrolase THF_DH/CycHdrlase Family

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Barlowe CK Site-directed mutagenesis of yeast C1-tetrahydrofolate synthase: analysis of an overlapping active site in a multifunctional enzyme. 1989 Biochemistry 28 2099-106
Price BD The isolation and characterization of a Drosophila gene encoding a putative NAD-dependent methylenetetrahydrofolate dehydrogenase-methenyltetrahydrofolate cyclohydrolase. 1993 Biochim Biophys Acta 1173 94-8



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)