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 |
Enzyme Information
| 4.1.2.25 |
Dihydroneopterin aldolase.
based on mapping to UniProt P59657
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.
-!- The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis. -!- The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyze the epimerisation of the 2' hydroxy-group (EC 5.1.99.8). -!- The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyzes EC 5.1.99.8 and EC 1.13.11.81. -!- The enzyme from the yeast Saccharomyces cerevisiae also catalyzes the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3 and EC 2.5.1.15.
|
| 2.7.6.3 |
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase.
based on mapping to UniProt P59657
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)
| P59657 |
SULD_STRR6
Streptococcus pneumoniae R6
Bifunctional folate synthesis protein
|
PDB Structure
| PDB | 2CG8 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structure of the Bifunctional Dihydroneopterin Aldolase/6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase from Streptococcus Pneumoniae.
J.Mol.Biol.
|
