EzCatDB: D00104
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeD00104
CATH domainDomain 13.90.1150.10 : Aspartate Aminotransferase, domain 1
Domain 23.40.640.10 : Aspartate Aminotransferase; domain 2Catalytic domain
E.C.2.6.1.19,2.6.1.22
CSA1gtx

CATH domainRelated DB codes (homologues)
3.40.640.10 : Aspartate Aminotransferase; domain 2D00085,D00092,D00101,D00102,D00103,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,M00031,D00279
3.90.1150.10 : Aspartate Aminotransferase, domain 1D00085,D00092,D00101,D00102,D00103,D00107,D00108,D00109,D00255,D00257,D00258,D00265,D00269,D00515,M00031,D00279

Enzyme Name
UniProtKBKEGG

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
RefSeqNP_999428.1 (Protein)
NM_214263.1 (DNA/RNA sequence)
PfamPF00202 (Aminotran_3)
[Graphical view]

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

UniProtKB: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.

Compound table: links to PDB-related databases & PoSSuM

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
ChEBI18405
16865
59888
30915
16320
57731
32816
16265
16015
16256
16977
57972

PubChem1051
6992099
119
51
6971064
5459822
1060
1112
88747398
44272391
33032
296
7311724
5950

                  
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 UniProtKBP80147
[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 2008)
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)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.