CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.3180 |
Domain Context
CATH Clusters
| Superfamily | 3.30.70.3180 |
| 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 | 2GQ2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
NADP+ expels both the co-factor and a substrate analog from the Mycobacterium tuberculosis ThyX active site: opportunities for anti-bacterial drug design.
J.Mol.Biol.
|
