CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.5 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
1.20.5.3070 |
Domain Context
CATH Clusters
| Superfamily | 1.20.5.3070 |
| Functional Family |
Enzyme Information
| 2.1.1.148 |
Thymidylate synthase (FAD).
based on mapping to UniProt O41156
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)
| O41156 |
THYX_PBCV1
Paramecium bursaria Chlorella virus 1
Probable flavin-dependent thymidylate synthase
|
PDB Structure
| PDB | 4FZB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Mechanistic and structural basis for inhibition of thymidylate synthase ThyX.
Open Biology
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