CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.1720 | endopeptidase fold (from Nostoc punctiforme) |
|
3.90.1720.10 | endopeptidase domain like (from Nostoc punctiforme) |
Domain Context
CATH Clusters
| Superfamily | endopeptidase domain like (from Nostoc punctiforme) |
| Functional Family |
Enzyme Information
| 3.1.1.4 |
Phospholipase A(2).
based on mapping to UniProt P53816
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate.
-!- Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position.
|
| 2.3.1.- |
Transferring groups other than amino-acyl groups.
based on mapping to UniProt P53816
|
| 3.1.1.32 |
Phospholipase A(1).
based on mapping to UniProt P53816
Phosphatidylcholine + H(2)O = 2-acylglycerophosphocholine + a carboxylate.
-!- Has a much broader specificity than EC 3.1.1.4.
|
| 2.3.1.135 |
Phosphatidylcholine--retinol O-acyltransferase.
based on mapping to UniProt Q9JI60
Phosphatidylcholine + retinol--[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester--[cellular-retinol-binding- protein].
-!- A key enzyme in retinoid metabolism, catalyzing the transfer of an acyl group from the sn-1 position of phosphatidylcholine to retinol, forming retinyl esters which are then stored. -!- Recognizes the substrate both in free form and when bound to cellular-retinol-binding-protein, but has higher affinity for the bound form. -!- Can also esterify 11-cis-retinol.
|
UniProtKB Entries (2)
| Q9JI60 |
LRAT_MOUSE
Mus musculus
Lecithin retinol acyltransferase
|
| P53816 |
PLAT3_HUMAN
Homo sapiens
Phospholipase A and acyltransferase 3
|
PDB Structure
| PDB | 4Q95 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3.
Nat.Chem.Biol.
|
