CATH Classification

Domain Context

CATH Clusters

Superfamily Hexapeptide repeat proteins
Functional Family

Enzyme Information

2.3.1.157
Glucosamine-1-phosphate N-acetyltransferase.
based on mapping to UniProt Q97R46
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 Q97R46
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)

Q97R46
GLMU_STRPN
Streptococcus pneumoniae TIGR4
Bifunctional protein GlmU

PDB Structure

PDB 1HM0
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
Crystal structure of Streptococcus pneumoniae N-acetylglucosamine-1-phosphate uridyltransferase bound to acetyl-coenzyme A reveals a novel active site architecture.
Sulzenbacher, G., Gal, L., Peneff, C., Fassy, F., Bourne, Y.
J.Biol.Chem.