CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.40 | 3-Layer(aba) Sandwich | 
|   | 3.40.50 | Rossmann fold | 
|   | 3.40.50.970 | Thiamin diphosphate (ThDP)-binding fold, Pyr/PP domains | 
Domain Context
CATH Clusters
| Superfamily | 3.40.50.970 | 
| Functional Family | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase | 
Enzyme Information
| 2.2.1.9 | 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase. based on mapping to UniProt P17109 Isochorismate + 2-oxoglutarate = 5-enolpyruvoyl-6-hydroxy-2-succinyl- cyclohex-3-ene-1-carboxylate + CO(2). -!- Involved in the biosynthesis of vitamin K(2) (menaquinone). -!- In most anaerobes and all Gram-positive aerobes, menaquinone is the sole electron transporter in the respiratory chain and is essential for their survival. -!- It had previously been thought that the products of the reaction were (1R,6R)-6-hydroxy-2-succinylcyclohexa-2,4-diene-1-carboxylate (SHCHC), pyruvate and CO(2) but it is now known that two separate enzymes are involved: this enzyme and EC 4.2.99.20. -!- Under basic conditions, the product can spontaneously lose pyruvate to form SHCHC. -!- Formerly EC 2.5.1.64 and EC 2.5.1.n1. | 
UniProtKB Entries (1)
| P17109 | MEND_ECOLI Escherichia coli K-12 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase | 
PDB Structure
| PDB | 5EJA | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | |
| Primary Citation | A Thiamine-Dependent Enzyme Utilizes an Active Tetrahedral Intermediate in Vitamin K Biosynthesis J.Am.Chem.Soc. | 
