CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
6 | Special |
|
6.10 | Helix non-globular |
|
6.10.140 | Helix Hairpins |
|
6.10.140.440 |
Domain Context
CATH Clusters
| Superfamily | 6.10.140.440 |
| 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.
|