EzCatDB: D00104

DB codeD00104
CATH domainDomain 13.90.1150.10
Domain 23.40.640.10Catalytic domain
E.C.2.6.1.19,2.6.1.22
CSA1gtx

CATH domainRelated DB codes (homologues)
3.40.640.10D00085,D00092,D00101,D00102,D00103,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,M00031,D00279
3.90.1150.10D00085,D00092,D00101,D00102,D00103,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,M00031,D00279

Enzyme Name
Swiss-protKEGG

P80147
Protein name4-aminobutyrate aminotransferase, mitochondrial4-aminobutyrate transaminase
   (EC 2.6.1.19)

beta-alanine-oxoglutarate transaminase
   (EC 2.6.1.19)

aminobutyrate aminotransferase
   (EC 2.6.1.19)

beta-alanine aminotransferase
   (EC 2.6.1.19)

beta-alanine-oxoglutarate aminotransferase
   (EC 2.6.1.19)

gamma-aminobutyrate aminotransaminase
   (EC 2.6.1.19)

gamma-aminobutyrate transaminase
   (EC 2.6.1.19)

gamma-aminobutyrate-alpha-ketoglutarate aminotransferase
   (EC 2.6.1.19)

gamma-aminobutyrate-alpha-ketoglutarate transaminase
   (EC 2.6.1.19)

gamma-aminobutyrate:alpha-oxoglutarate aminotransferase
   (EC 2.6.1.19)

gamma-aminobutyric acid aminotransferase
   (EC 2.6.1.19)

gamma-aminobutyric acid pyruvate transaminase
   (EC 2.6.1.19)

gamma-aminobutyric acid transaminase
   (EC 2.6.1.19)

gamma-aminobutyric acid-alpha-ketoglutarate transaminase
   (EC 2.6.1.19)

gamma-aminobutyric acid-alpha-ketoglutaric acid aminotransferase
   (EC 2.6.1.19)

gamma-aminobutyric acid-2-oxoglutarate transaminase
   (EC 2.6.1.19)

gamma-aminobutyric transaminase
   (EC 2.6.1.19)

4-aminobutyrate aminotransferase
   (EC 2.6.1.19)

4-aminobutyrate-2-ketoglutarate aminotransferase
   (EC 2.6.1.19)

4-aminobutyrate-2-oxoglutarate aminotransferase
   (EC 2.6.1.19)

4-aminobutyrate-2-oxoglutarate transaminase
   (EC 2.6.1.19)

4-aminobutyric acid 2-ketoglutaric acid aminotransferase
   (EC 2.6.1.19)

4-aminobutyric acid aminotransferase
   (EC 2.6.1.19)

aminobutyrate aminotransferase
   (EC 2.6.1.19)

aminobutyrate transaminase
   (EC 2.6.1.19)

GABA aminotransferase
   (EC 2.6.1.19)

GABA transaminase
   (EC 2.6.1.19)

GABA transferase
   (EC 2.6.1.19)

GABA-alpha-ketoglutarate aminotransferase
   (EC 2.6.1.19)

GABA-alpha-ketoglutarate transaminase
   (EC 2.6.1.19)

GABA-alpha-ketoglutaric acid transaminase
   (EC 2.6.1.19)

GABA-alpha-oxoglutarate aminotransferase
   (EC 2.6.1.19)

GABA-2-oxoglutarate aminotransferase
   (EC 2.6.1.19)

GABA-2-oxoglutarate transaminase
   (EC 2.6.1.19)

GABA-oxoglutarate aminotransferase
   (EC 2.6.1.19)

GABA-oxoglutarate transaminase
   (EC 2.6.1.19)

glutamate-succinic semialdehyde transaminase
   (EC 2.6.1.19)

GabT
   (EC 2.6.1.19)

(S)-3-amino-2-methylpropionate transaminase
   (EC 2.6.1.22)

L-3-aminoisobutyrate transaminase
   (EC 2.6.1.22)

beta-aminobutyric transaminase
   (EC 2.6.1.22)

L-3-aminoisobutyric aminotransferase
   (EC 2.6.1.22)

beta-aminoisobutyrate-alpha-ketoglutarate transaminase
   (EC 2.6.1.22)

SynonymsEC 2.6.1.19
Gamma-amino-N-butyrate transaminase
GABA transaminase
GABA-T
GABA aminotransferase
GABA-AT
L-AIBAT
L-AIBAT) ((S)-3-amino-2-methylpropionate transaminase
EC 2.6.1.22

KEGG pathways
MAP codePathwaysE.C.
MAP00251Glutamate metabolism2.6.1.19
MAP00252Alanine and aspartate metabolism2.6.1.19
MAP00280Valine, leucine and isoleucine degradation2.6.1.22
MAP00410beta-Alanine metabolism2.6.1.19
MAP00640Propanoate metabolism2.6.1.19
MAP00650Butanoate metabolism2.6.1.19

Swiss-prot:Accession NumberP80147
Entry nameGABT_PIG
Activity4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.,(S)-3-amino-2-methylpropanoate + 2- oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.
SubunitHomodimer.
Subcellular locationMitochondrion matrix.
CofactorPyridoxal phosphate.


CofactorsSubstratesProductsintermediates
KEGG-idC00018C00334C00026C01205C00022C00232C00025C00349C00041
E.C.2.6.1.19,2.6.1.192.6.1.192.6.1.192.6.1.222.6.1.222.6.1.192.6.1.192.6.1.222.6.1.22
CompoundPyridoxal phosphate4-Aminobutanoate2-Oxoglutarate(R)-3-Amino-2-methylpropanoatePyruvateSuccinate semialdehydeL-Glutamate2-Methyl-3-oxopropanoateL-alanine
Typearomatic ring (with nitrogen atoms),phosphate group/phosphate ionamino acids,lipidcarbohydrate,carboxyl groupamino acidscarbohydrate,carboxyl groupcarbohydrate,carboxyl groupamino acids,carboxyl groupcarbohydrate,carboxyl groupamino acids
1gtxA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gtxB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gtxC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gtxD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohvA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohvB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohvC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohvD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohwA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohwB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohwC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohwD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohyA01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohyB01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohyC01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohyD01UnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gtxA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gtxB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gtxC02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1gtxD02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohvA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohvB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohvC02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohvD02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnbound
1ohwA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-VIG
1ohwB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-VIG
1ohwC02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-VIG
1ohwD02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-VIG
1ohyA02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-GEG
1ohyB02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-GEG
1ohyC02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-GEG
1ohyD02Bound:PLPUnboundUnboundUnboundUnboundUnboundUnboundUnboundUnboundIntermediate-analogue:PLP-GEG

Active-site residues
resource
literature [5] & [6]
pdbCatalytic residuesCofactor-binding residues
1gtxA01

1gtxB01

1gtxC01

1gtxD01

1ohvA01

1ohvB01

1ohvC01

1ohvD01

1ohwA01

1ohwB01

1ohwC01

1ohwD01

1ohyA01

1ohyB01

1ohyC01

1ohyD01

1gtxA02GLU 270;LYS 329
LYS 329(PLP binding)
1gtxB02GLU 270;LYS 329
LYS 329(PLP binding)
1gtxC02GLU 270;LYS 329
LYS 329(PLP binding)
1gtxD02GLU 270;LYS 329
LYS 329(PLP binding)
1ohvA02GLU 270;LYS 329
LYS 329(PLP binding)
1ohvB02GLU 270;LYS 329
LYS 329(PLP binding)
1ohvC02GLU 270;LYS 329
LYS 329(PLP binding)
1ohvD02GLU 270;LYS 329
LYS 329(PLP binding)
1ohwA02GLU 270;LYS 329
LYS 329(PLP binding)
1ohwB02GLU 270;LYS 329
LYS 329(PLP binding)
1ohwC02GLU 270;LYS 329
LYS 329(PLP binding)
1ohwD02GLU 270;LYS 329
LYS 329(PLP binding)
1ohyA02GLU 270;LYS 329
LYS 329(PLP binding)
1ohyB02GLU 270;LYS 329
LYS 329(PLP binding)
1ohyC02GLU 270;LYS 329
LYS 329(PLP binding)
1ohyD02GLU 270;LYS 329
LYS 329(PLP binding)

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.8633
[6]Scheme 2, Scheme 3

references
[1]
PubMed ID6789830
JournalBiochem Biophys Res Commun
Year1981
Volume99
Pages1333-40
AuthorsKim DS, Churchich JE
Title4-Aminobutyrate aminotransferase, the reaction of lysine residues connected with enzymatic activity.
[2]
PubMed ID7140743
JournalEur J Biochem
Year1982
Volume126
Pages507-11
AuthorsChurchich JE
Title4-Aminobutyrate aminotransferase. Different susceptibility to inhibitors, microenvironment of the cofactor binding site and distance of the catalytic sites.
[3]
PubMed ID3780742
JournalEur J Biochem
Year1986
Volume161
Pages289-94
AuthorsChoi SY, Churchich JE
TitleBiosynthesis of 4-aminobutyrate aminotransferase.
[4]
PubMed ID1901730
JournalBiochim Biophys Acta
Year1991
Volume1077
Pages187-91
AuthorsKim YT, Churchich JE
Title4-Aminobutyrate aminotransferase: identification of lysine residues connected with catalytic activity.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS)
Medline ID99321499
PubMed ID10393538
JournalBiochemistry
Year1999
Volume38
Pages8628-34
AuthorsStorici P, Capitani G, De Biase D, Moser M, John RA, Jansonius JN, Schirmer T
TitleCrystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy.
Related PDB1gtx
Related Swiss-protP80147
[6]
PubMed ID11853435
JournalJ Am Chem Soc
Year2002
Volume124
Pages1620-4
AuthorsChoi S, Storici P, Schirmer T, Silverman RB
TitleDesign of a conformationally restricted analogue of the antiepilepsy drug Vigabatrin that directs its mechanism of inactivation of gamma-aminobutyric acid aminotransferase.
[7]
PubMed ID14534310
JournalJ Biol Chem
Year2004
Volume279
Pages363-73
AuthorsStorici P, De Biase D, Bossa F, Bruno S, Mozzarelli A, Peneff C, Silverman RB, Schirmer T
TitleStructures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-ethynyl-GABA and with the antiepilepsy drug vigabatrin.
Related PDB1ohv,1ohw,1ohy


createdupdated
2004-03-172009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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