CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.160 | 3 Solenoid |
|
2.160.10 | UDP N-Acetylglucosamine Acyltransferase; domain 1 |
|
2.160.10.10 | Hexapeptide repeat proteins |
Domain Context
CATH Clusters
| Superfamily | Hexapeptide repeat proteins |
| Functional Family | Bifunctional protein GlmU |
Enzyme Information
| 2.3.1.157 |
Glucosamine-1-phosphate N-acetyltransferase.
based on mapping to UniProt P9WMN3
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 P9WMN3
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)
| P9WMN3 |
GLMU_MYCTU
Mycobacterium tuberculosis H37Rv
Bifunctional protein GlmU
|
PDB Structure
| PDB | 4HCQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structures identify an atypical two-metal-ion mechanism for uridyltransfer in GlmU: its significance to sugar nucleotidyl transferases
J.Mol.Biol.
|
