CATH Domain 1dhnA00

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.30	2-Layer Sandwich
	3.30.1130	GTP Cyclohydrolase I, domain 2
	3.30.1130.10	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain

Domain Context

CATH Clusters

Superfamily	3.30.1130.10
Functional Family	7,8-dihydroneopterin aldolase

Enzyme Information

4.1.2.25

Dihydroneopterin aldolase.

based on mapping to UniProt P56740

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.

5.1.99.8

7,8-dihydroneopterin epimerase.

based on mapping to UniProt P56740

7,8-dihydroneopterin = 7,8-dihydromonapterin.

-!- The enzyme, which has been characterized in bacteria and plants, also has the activity of EC 4.1.2.25. -!- The enzyme from the bacterium Mycobacterium tuberculosis has an additional oxygenase function (EC 1.13.11.81).

UniProtKB Entries (1)

P56740

FOLB_STAAU

Staphylococcus aureus

Dihydroneopterin aldolase

PDB Structure

PDB	1DHN
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal structure and reaction mechanism of 7,8-dihydroneopterin aldolase from Staphylococcus aureus. Hennig, M., D'Arcy, A., Hampele, I.C., Page, M.G., Oefner, C., Dale, G.E. Nat.Struct.Biol.