CATH Domain 2yqcA01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.550	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
	3.90.550.10	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Domain Context

CATH Clusters

Superfamily	Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A
Functional Family	UDP-N-acetylglucosamine diphosphorylase 2

Enzyme Information

2.7.7.23

UDP-N-acetylglucosamine diphosphorylase.

based on mapping to UniProt O74933

UTP + N-acetyl-alpha-D-glucosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-glucosamine.

-!- Part of the pathway for acetamido sugar biosynthesis in bacteria and archaea. -!- The enzyme from several bacteria (e.g., Escherichia coli, Bacillus subtilis and Haemophilus influenzae) has been shown to be bifunctional and also to possess the activity of EC 2.3.1.157. -!- The enzyme from plants and animals is also active toward N-acetyl- alpha-D-galactosamine 1-phosphate (cf. EC 2.7.7.83), while the bacterial enzyme shows low activity toward that substrate.

UniProtKB Entries (1)

O74933

UAP1_CANAX

Candida albicans

UDP-N-acetylglucosamine pyrophosphorylase

PDB Structure

PDB	2YQC
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Escherichia
Primary Citation	Crystal Structure of Uridine-diphospho-N-acetylglucosamine Pyrophosphorylase from Candida albicans and Catalytic Reaction Mechanism Maruyama, D., Nishitani, Y., Nonaka, T., Kita, A., Fukami, T.A., Mio, T., Yamada-Okabe, H., Yamada-Okabe, T., Miki, K. J.Biol.Chem.