| Description | This entry represents the NAD(P)-binding domain found in enzymes that belong to the tetrahydrofolate dehydrogenase/cyclohydrolase family, which are mainly found in bacteria but also in archaeal and eukaryotic organisms.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 different oxidation states by methylene-THF dehydrogenase (), methenyl-THF cyclohydrolase ( ) and formyl-THF synthetase ( ) [ , ]. The dehydrogenase and cyclohydrolase activities are expressed by a variety of multifunctional enzymes, including the tri-functional eukaryotic C1-tetrahydrofolate synthase []; a bifunctional eukaryotic mitochondrial protein; and the bifunctional Escherichia coli folD protein [, ]. Methylene-tetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclo-hydrolase share an overlapping active site [], and as such are usually located together in proteins, acting in tandem on the carbon-nitrogen bonds of substrates other than peptide bonds. | Name | Tetrahydrofolate dehydrogenase/cyclohydrolase, NAD(P)-binding domain |
| Short Name | THF_DH/CycHdrlase_NAD-bd_dom | Type | Domain |
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