CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.40 | 3-Layer(aba) Sandwich | 
|   | 3.40.50 | Rossmann fold | 
|   | 3.40.50.880 | Class I glutamine amidotransferase (GATase) domain | 
Domain Context
CATH Clusters
| Superfamily | 3.40.50.880 | 
| Functional Family | Protein/nucleic acid deglycase DJ-1 | 
Enzyme Information
| 3.5.1.124 | Protein deglycase. based on mapping to UniProt Q99497 (1) An N(omega)-(1-hydroxy-2-oxopropyl)-[protein]-L-arginine + H(2)O = a [protein]-L-arginine + lactate. (2) An N(6)-(1-hydroxy-2-oxopropyl)-[protein]-L-lysine + H(2)O = a [protein]-L-lysine + lactate. (3) An S-(1-hydroxy-2-oxopropyl)-[protein]-L-cysteine + H(2)O = a [protein]-L-cysteine + lactate. -!- The enzyme, previously thought to be a glyoxalase, acts on glycated L-arginine, L-lysine, and L-cysteine residues within proteins that have been attacked and modified by glyoxal or 2-oxopropanal. -!- The attack forms hemithioacetal in the case of cysteines and aminocarbinols in the case of arginines and lysines. -!- The enzyme repairs the amino acids, releasing glycolate or lactate (70-80% (S)-lactate and 20-30% (R)-lactate), depending on whether the attacking agent was glyoxal or 2-oxopropanal, respectively. | 
| 3.1.2.- | Thiolester hydrolases. based on mapping to UniProt Q99497 | 
| 3.5.1.- | In linear amides. based on mapping to UniProt Q99497 | 
UniProtKB Entries (1)
| Q99497 | PARK7_HUMAN Homo sapiens Protein/nucleic acid deglycase DJ-1 | 
PDB Structure
| PDB | 2RK3 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | Structural Impact of Three Parkinsonism-Associated Missense Mutations on Human DJ-1. Biochemistry | 
