CATH Domain 1nbuA00

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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 P9WNC5 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 P9WNC5 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).
1.13.11.81	7,8-dihydroneopterin oxygenase. based on mapping to UniProt P9WNC5 7,8-dihydroneopterin + O(2) = 7,8-dihydroxanthopterin + formate + glycolaldehyde. -!- The enzyme from the bacterium Mycobacterium tuberculosis is multifunctional and also catalyzes the epimerisation of the 2'-hydroxy group of 7,8-dihydroneopterin (EC 5.1.99.8) and the reaction of EC 4.1.2.25.

UniProtKB Entries (1)

FOLB_MYCTU

Mycobacterium tuberculosis H37Rv

Dihydroneopterin aldolase

PDB Structure

PDB	1NBU
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Regulation by oligomerization in a mycobacterial folate biosynthetic enzyme. Goulding, C.W., Apostol, M.I., Sawaya, M.R., Phillips, M., Parseghian, A., Eisenberg, D. J.Mol.Biol.