CATH Classification
Domain Context
CATH Clusters
| Superfamily | Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A |
| Functional Family | Bifunctional protein GlmU |
Enzyme Information
| 2.3.1.157 |
Glucosamine-1-phosphate N-acetyltransferase.
based on mapping to UniProt A5U161
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.
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| 2.7.7.23 |
UDP-N-acetylglucosamine diphosphorylase.
based on mapping to UniProt A5U161
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.
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UniProtKB Entries (1)
| A5U161 |
GLMU_MYCTA
Mycobacterium tuberculosis H37Ra
Bifunctional protein GlmU
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PDB Structure
| PDB | 3DK5 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
PknB-mediated phosphorylation of a novel substrate, N-acetylglucosamine-1-phosphate uridyltransferase, modulates its acetyltransferase activity.
J.Mol.Biol.
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