CATH Classification

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 4AC3
External Links
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.