CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.1090 | Dehydroquinate synthase-like, alpha domain |
|
1.20.1090.10 | Dehydroquinate synthase-like - alpha domain |
Domain Context
CATH Clusters
| Superfamily | Dehydroquinate synthase-like - alpha domain |
| Functional Family |
Enzyme Information
| 4.2.3.152 |
2-epi-5-epi-valiolone synthase.
based on mapping to UniProt H2K887
D-sedoheptulose 7-phosphate = 2-epi-5-epi-valiolone + phosphate.
-!- The enzyme is highly specific for alpha-D-sedoheptulopyranose 7-phosphate. -!- It requires a divalent metal ion (Zn(2+) or Co(2+)) and an NAD(+) cofactor, which is transiently reduced during the reaction. -!- The enzyme is involved in the biosynthesis of C(7)N-aminocyclitol natural products, such as the valienamine moiety of the antidiabetic drug acarbose and the crop protectant validamycin A. -!- Cf. EC 4.2.3.154 and EC 4.2.3.155.
|
UniProtKB Entries (1)
| H2K887 |
VALA_STRHJ
Streptomyces hygroscopicus subsp. jinggangensis 5008
2-epi-5-epi-valiolone synthase
|
PDB Structure
| PDB | 4P53 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structure of a sedoheptulose 7-phosphate cyclase: ValA from Streptomyces hygroscopicus.
Biochemistry
|
