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 | 5-aminovalerate aminotransferase / 4-aminobutyrate transaminase |
Enzyme Information
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.
|
2.6.1.22 |
(S)-3-amino-2-methylpropionate transaminase.
based on mapping to UniProt P22256
(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3- oxopropanoate + L-glutamate.
-!- Also acts on beta-alanine and other omega-amino acids having carbon chains between 2 and 5. -!- The two enantiomers of the 2-methyl-3-oxopropanoate formed by the enzyme interconvert by enolization, so that this enzyme, together with EC 2.6.1.40, provide a route for interconversion of the enantiomers of 3-amino-2-methylpropanoate.
|
UniProtKB Entries (1)
P22256 |
GABT_ECOLI
Escherichia coli K-12
4-aminobutyrate aminotransferase GabT
|
PDB Structure
PDB | 1SF2 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Crystal structures of unbound and aminooxyacetate-bound Escherichia coli gamma-aminobutyrate aminotransferase.
Biochemistry
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