CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.1180 | Undecaprenyl pyrophosphate synthetase |
|
3.40.1180.10 | Decaprenyl diphosphate synthase-like |
Domain Context
CATH Clusters
| Superfamily | Decaprenyl diphosphate synthase-like |
| Functional Family | Isoprenyl transferase |
Enzyme Information
| 2.5.1.86 |
Trans,polycis-decaprenyl diphosphate synthase.
based on mapping to UniProt P9WFF7
(2Z,6E)-farnesyl diphosphate + 7 isopentenyl diphosphate = 7 diphosphate + (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30Z,34E)-decaprenyl diphosphate.
-!- The enzyme is involved in the biosynthesis of decaprenyl phosphate, which plays a central role in the biosynthesis of essential mycobacterial cell wall components, such as the mycolyl- arabinogalactan-peptidoglycan complex and lipoarabinomannan.
|
| 2.5.1.87 |
Ditrans,polycis-polyprenyl diphosphate synthase ((2E,6E)-farnesyl diphosphate specific).
based on mapping to UniProt P9WFF7
(2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = n diphosphate + ditrans,polycis-polyprenyl diphosphate (n = 10-55).
-!- The enzyme is involved in biosynthesis of dolichol (a long-chain polyprenol) with a saturated alpha-isoprene unit, which serves as a glycosyl carrier in protein glycosylation. -!- The yeast Saccharomyces cerevisiae has two different enzymes that catalyze this reaction. -!- Rer2p synthesizes a well-defined family of polyprenols of 13-18 isoprene residues with dominating C(80) (16 isoprene residues) extending to C(120), while Srt1p synthesizes mainly polyprenol with 22 isoprene subunits. -!- Largest Srt1p products reach C(290). -!- The enzyme from Arabidopsis thaliana catalyzes the formation of polyprenyl diphosphates with predominant carbon number C(120).
|
UniProtKB Entries (1)
| P9WFF7 |
DPDS_MYCTU
Mycobacterium tuberculosis H37Rv
Decaprenyl diphosphate synthase
|
PDB Structure
| PDB | 2VG3 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The structural basis of chain length control in Rv1086.
J. Mol. Biol.
|
