CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.70 | Aldolase class I |
Domain Context
CATH Clusters
| Superfamily | Aldolase class I |
| Functional Family | Lysine 2,3-aminomutase |
Enzyme Information
| 5.4.3.2 |
Lysine 2,3-aminomutase.
based on mapping to UniProt Q9XBQ8
L-lysine = (3S)-3,6-diaminohexanoate.
-!- This enzyme is a member of the 'AdoMet radical' (radical SAM) family. -!- It contains pyridoxal phosphate and a [4Fe-4S] cluster and binds an exchangeable S-adenosyl-L-methionine molecule. -!- Activity in vitro requires a strong reductant such as dithionite and strictly anaerobic conditions. -!- A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of S-adenosyl-L-methionine, mediated by the iron- sulfur cluster. -!- S-adenosyl-L-methionine is regenerated at the end of the reaction.
|
UniProtKB Entries (1)
| Q9XBQ8 |
KAMA_CLOSU
Clostridium subterminale
L-lysine 2,3-aminomutase
|
PDB Structure
| PDB | 2A5H |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The X-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale.
Proc.Natl.Acad.Sci.Usa
|
