CATH Classification

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 4E1K
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
An aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding mode.
Larsen, N.A., Nash, T.J., Morningstar, M., Shapiro, A.B., Joubran, C., Blackett, C.J., Patten, A.D., Boriack-Sjodin, P.A., Doig, P.
Biochem.J.