CATH Classification

Domain Context

CATH Clusters

Superfamily Dihydropteroate synthase-like
Functional Family Folic acid synthesis protein fol1

Enzyme Information

4.1.2.25
Dihydroneopterin aldolase.
based on mapping to UniProt P53848
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 P53848
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.
2.5.1.15
Dihydropteroate synthase.
based on mapping to UniProt P53848
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.
-!- The enzyme participates in the biosynthetic 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 plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25.

UniProtKB Entries (1)

P53848
FOL1_YEAST
Saccharomyces cerevisiae S288C
Folic acid synthesis protein FOL1

PDB Structure

PDB 2BMB
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
The Three-Dimensional Structure of the Bifunctional 6-Hydroxymethyl-7,8-Dihydropterin Pyrophosphokinase/Dihydropteroate Synthase of Saccharomyces Cerevisiae
Lawrence, M.C., Iliades, P., Fernley, R.T., Berglez, J., Pilling, P.A., Macreadie, I.G.
J.Mol.Biol.