CATH Domain 4kpzA01

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	Bifunctional protein GlmU

Enzyme Information

2.7.7.23

UDP-N-acetylglucosamine diphosphorylase.

based on mapping to UniProt P43889

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.

2.3.1.157

Glucosamine-1-phosphate N-acetyltransferase.

based on mapping to UniProt P43889

Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CoA + N-acetyl-alpha-D- glucosamine 1-phosphate.

-!- The enzyme from several bacteria has been shown to be bifunctional and also to possess the activity of EC 2.7.7.23.

UniProtKB Entries (1)

P43889

GLMU_HAEIN

Haemophilus influenzae Rd KW20

Bifunctional protein GlmU

PDB Structure

PDB	4KPZ
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Rational design of inhibitors of the bacterial cell wall synthetic enzyme GlmU using virtual screening and lead-hopping. Doig, P., Boriack-Sjodin, P.A., Dumas, J., Hu, J., Itoh, K., Johnson, K., Kazmirski, S., Kinoshita, T., Kuroda, S., Sato, T.O., Sugimoto, K., Tohyama, K., Aoi, H., Wakamatsu, K., Wang, H. Bioorg.Med.Chem.