CATH Classification

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 4M5N
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The identification, analysis and structure-based development of novel inhibitors of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase.
Yun, M.K., Hoagland, D., Kumar, G., Waddell, M.B., Rock, C.O., Lee, R.E., White, S.W.
Bioorg.Med.Chem.