CATH Domain 4aawA01

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

Enzyme Information

2.3.1.157

Glucosamine-1-phosphate N-acetyltransferase.

based on mapping to UniProt Q8DQ18

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.

2.7.7.23

UDP-N-acetylglucosamine diphosphorylase.

based on mapping to UniProt Q8DQ18

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)

Q8DQ18

GLMU_STRR6

Streptococcus pneumoniae R6

Bifunctional protein GlmU

PDB Structure

PDB	4AAW
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	Inhibitors of Acetyltransferase Domain of N-Acetylglucosamine-1-Phosphate-Uridyltransferase/ Glucosamine-1-Phosphate-Acetyltransferase (Glmu). Part 1: Hit to Lead Evaluation of a Novel Arylsulfonamide Series. Green, O.M., McKenzie, A.R., Shapiro, A.B., Otterbein, L., Ni, H., Patten, A., Stokes, S., Albert, R., Kawatkar, S., Breed, J. Bioorg.Med.Chem.Lett.