CATH Classification

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.
Liu, W., Peterson, P.E., Carter, R.J., Zhou, X., Langston, J.A., Fisher, A.J., Toney, M.D.
Biochemistry