CATH Domain 5etpA00

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	5ETP
External Links	PDBSum Proteopedia
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. Dennis, M.L., Pitcher, N.P., Lee, M.D., DeBono, A.J., Wang, Z.C., Harjani, J.R., Rahmani, R., Cleary, B., Peat, T.S., Baell, J.B., Swarbrick, J.D. J.Med.Chem.