CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.1360 | Gyrase A; domain 2 |
|
3.30.1360.170 |
Domain Context
CATH Clusters
| Superfamily | 3.30.1360.170 |
| Functional Family | Flavin-dependent thymidylate synthase |
Enzyme Information
| 2.1.1.148 |
Thymidylate synthase (FAD).
based on mapping to UniProt Q9WYT0
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)
| Q9WYT0 |
THYX_THEMA
Thermotoga maritima MSB8
Flavin-dependent thymidylate synthase
|
PDB Structure
| PDB | 1O27 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Functional Analysis of Substrate and Cofactor Complex Structures of a Thymidylate Synthase-Complementing Protein
Structure
|
