CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 3 | Alpha Beta | 
|   | 3.90 | Alpha-Beta Complex | 
|   | 3.90.1150 | Aspartate Aminotransferase, domain 1 | 
|   | 3.90.1150.10 | Aspartate Aminotransferase, domain 1 | 
Domain Context
CATH Clusters
| Superfamily | Aspartate Aminotransferase, domain 1 | 
| Functional Family | 4-aminobutyrate aminotransferase | 
Enzyme Information
| 2.6.1.48 | 5-aminovalerate transaminase. based on mapping to UniProt P22256 5-aminopentanoate + 2-oxoglutarate = 5-oxopentanoate + L-glutamate. | 
| 2.6.1.19 | 4-aminobutyrate--2-oxoglutarate transaminase. based on mapping to UniProt P22256 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate. -!- Some preparations also act on beta-alanine, 5-aminopentanoate and (R,S)-3-amino-2-methylpropanoate. | 
UniProtKB Entries (1)
| P22256 | GABT_ECOLI Escherichia coli K-12 4-aminobutyrate aminotransferase GabT | 
PDB Structure
| PDB | 1SZU | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | Kinetic and Crystallographic Analysis of Active Site Mutants of Escherichia coligamma-Aminobutyrate Aminotransferase. Biochemistry | 
