CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.10 | Ribbon |
|
2.10.10 | Seminal Fluid Protein PDC-109 (Domain B) |
|
2.10.10.100 |
Domain Context
CATH Clusters
| Superfamily | 2.10.10.100 |
| Functional Family | UDP-N-acetylhexosamine pyrophosphorylase isoform X1 |
Enzyme Information
| 2.7.7.23 |
UDP-N-acetylglucosamine diphosphorylase.
based on mapping to UniProt Q16222
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.
|
| 2.7.7.83 |
UDP-N-acetylgalactosamine diphosphorylase.
based on mapping to UniProt Q16222
UTP + N-acetyl-alpha-D-galactosamine 1-phosphate = diphosphate + UDP-N- acetyl-alpha-D-galactosamine.
-!- The enzyme from plants and animals also has activity toward N-acetyl- alpha-D-glucosamine 1-phosphate (cf. EC 2.7.7.23).
|
UniProtKB Entries (1)
| Q16222 |
UAP1_HUMAN
Homo sapiens
UDP-N-acetylhexosamine pyrophosphorylase
|
PDB Structure
| PDB | 1JVD |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture.
EMBO J.
|
