CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.50 | FAD/NAD(P)-binding domain |
|
3.50.50.60 | FAD/NAD(P)-binding domain |
Domain Context
CATH Clusters
| Superfamily | FAD/NAD(P)-binding domain |
| Functional Family | Geranylgeranyl diphosphate reductase BchP |
Enzyme Information
| 1.3.1.101 |
2,3-bis-O-geranylgeranyl-sn-glycerol 1-phosphate reductase (NAD(P)H).
based on mapping to UniProt Q9HKS9
2,3-bis-(O-phytanyl)-sn-glycerol 1-phosphate + 8 NAD(P)(+) = 2,3-bis- (O-geranylgeranyl)-sn-glycerol 1-phosphate + 8 NAD(P)H.
-!- The enzyme from the archaeon Thermoplasma acidophilum is involved in the biosynthesis of membrane lipids. -!- In vivo the reaction occurs in the reverse direction with the formation of 2,3-bis-O-phytanyl-sn-glycerol 1-phosphate. -!- cf. EC 1.3.7.11.
|
UniProtKB Entries (1)
| Q9HKS9 |
GGR_THEAC
Thermoplasma acidophilum DSM 1728
Digeranylgeranylglycerophospholipid reductase
|
PDB Structure
| PDB | 3OZ2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Insights into substrate specificity of geranylgeranyl reductases revealed by the structure of digeranylgeranylglycerophospholipid reductase, an essential enzyme in the biosynthesis of archaeal membrane lipids.
J.Mol.Biol.
|