CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.560 | 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK |
Domain Context
CATH Clusters
| Superfamily | 7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK |
| Functional Family | 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase |
Enzyme Information
| 2.7.6.3 |
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
based on mapping to UniProt P26281
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8- dihydropterin diphosphate.
-!- The enzyme participates in the pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea). -!- The enzyme exists in varying types of multifunctional proteins in different organisms. -!- The enzyme from the bacterium Streptococcus pneumoniae also harbors the activity of EC 4.1.2.25, the enzyme from the plant Arabidopsis thaliana harbors the activity of EC 2.5.1.15, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities.
|
UniProtKB Entries (1)
| P26281 |
HPPK_ECOLI
Escherichia coli K-12
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase
|
PDB Structure
| PDB | 5ETO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural Basis for the Selective Binding of Inhibitors to 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase from Staphylococcus aureus and Escherichia coli.
J.Med.Chem.
|
