CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 6 | Special | 
|   | 6.10 | Helix non-globular | 
|   | 6.10.140 | Helix Hairpins | 
|   | 6.10.140.450 | 
Domain Context
CATH Clusters
| Superfamily | 6.10.140.450 | 
| Functional Family | 
Enzyme Information
| 2.1.1.148 | Thymidylate synthase (FAD). based on mapping to UniProt P9WG57 5,10-methylenetetrahydrofolate + dUMP + NADPH = dTMP + tetrahydrofolate + NADP(+). -!- Contains FAD. -!- All thymidylate synthases catalyze a reductive methylation involving the transfer of the methylene group of 5,10-methylenetetrahydrofolate to the C5-position of dUMP and a two electron reduction of the methylene group to a methyl group. -!- Unlike the classical thymidylate synthase, ThyA (EC 2.1.1.45), which uses folate as both a 1-carbon donor and a source of reducing equivalents, this enzyme uses a flavin coenzyme as a source of reducing equivalents, which are derived from NADPH. | 
UniProtKB Entries (1)
| P9WG57 | THYX_MYCTU Mycobacterium tuberculosis H37Rv Flavin-dependent thymidylate synthase | 
PDB Structure
| PDB | 2AF6 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | Structure of the Mycobacterium tuberculosis Flavin Dependent Thymidylate Synthase (MtbThyX) at 2.0A Resolution. J.Mol.Biol. | 
