LIS - Legume Information System
Information about legume traits for crop improvement
GlycineMine
v5.1.0.3
Glycine data from LIS
v5.1.0.3
Glycine data from LIS
| Type | Conserved_site |
| 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 eukaryotic C1-tetrahydrofolate synthase []; a bifunctional eukaryotic mitochondrial protein; and thebifunctional Escherichia coli folD 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 other than peptide bonds.The sequence of the dehydrogenase/cyclohydrolase domain is highly conserved in all forms of the enzyme. This entry contains two conserved signature patterns; the first one is located in the N-terminal part of these enzymes and contains three acidic residues. The second pattern is a highly conserved sequence of 9 amino acids, which is located in the C-terminal section. |
| Short Name | THF_DH/CycHdrlase_CS |
