DB code: D00104
| CATH domain | 3.90.1150.10 : Aspartate Aminotransferase, domain 1 | |
|---|---|---|
| 3.40.640.10 : Aspartate Aminotransferase; domain 2 | Catalytic domain | |
| E.C. | 2.6.1.19 2.6.1.22 | |
| CSA | 1gtx | |
| M-CSA | 1gtx | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.40.640.10 : Aspartate Aminotransferase; domain 2 | D00085 D00092 D00101 D00102 D00103 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279 |
| 3.90.1150.10 : Aspartate Aminotransferase, domain 1 | D00085 D00092 D00101 D00102 D00103 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P80147 |
4-aminobutyrate aminotransferase, mitochondrial
|
EC
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 |
NP_999428.1
(Protein)
NM_214263.1 (DNA/RNA sequence) |
PF00202
(Aminotran_3)
[Graphical View] |
| KEGG enzyme name |
|---|
|
4-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 ) |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P80147 | GABT_PIG | 4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate. (S)-3-amino-2-methylpropanoate + 2- oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate. | Homodimer. | Mitochondrion matrix. | Pyridoxal phosphate. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00251 | Glutamate metabolism | 2.6.1.19 |
| MAP00252 | Alanine and aspartate metabolism | 2.6.1.19 |
| MAP00280 | Valine, leucine and isoleucine degradation | 2.6.1.22 |
| MAP00410 | beta-Alanine metabolism | 2.6.1.19 |
| MAP00640 | Propanoate metabolism | 2.6.1.19 |
| MAP00650 | Butanoate metabolism | 2.6.1.19 |
| Compound table | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||||||
| KEGG-id | C00018 | C00334 | C00026 | C01205 | C00022 | C00232 | C00025 | C00349 | C00041 | ||||||
| E.C. |
2.6.1.19
2.6.1.19 |
2.6.1.19
|
2.6.1.19
|
2.6.1.22
|
2.6.1.22
|
2.6.1.19
|
2.6.1.19
|
2.6.1.22
|
2.6.1.22
|
||||||
| Compound | Pyridoxal phosphate | 4-Aminobutanoate | 2-Oxoglutarate | (R)-3-Amino-2-methylpropanoate | Pyruvate | Succinate semialdehyde | L-Glutamate | 2-Methyl-3-oxopropanoate | L-alanine | ||||||
| Type | aromatic ring (with nitrogen atoms),phosphate group/phosphate ion | amino acids,lipid | carbohydrate,carboxyl group | amino acids | carbohydrate,carboxyl group | carbohydrate,carboxyl group | amino acids,carboxyl group | carbohydrate,carboxyl group | amino acids | ||||||
| ChEBI |
18405 18405 |
16865 59888 16865 59888 |
30915 30915 |
16320 57731 16320 57731 |
32816 32816 |
16265 16265 |
16015 16015 |
16256 16256 |
16977 57972 16977 57972 |
||||||
| PubChem |
1051 1051 |
119 6992099 119 6992099 |
51 51 |
5459822 6971064 5459822 6971064 |
1060 1060 |
1112 1112 |
33032 44272391 88747398 33032 44272391 88747398 |
296 296 |
5950 7311724 5950 7311724 |
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| 1gtxA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gtxB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gtxC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gtxD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohvA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohvB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohvC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohvD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohwA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohwB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohwC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohwD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohyA01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohyB01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohyC01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohyD01 |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gtxA02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gtxB02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gtxC02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1gtxD02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohvA02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohvB02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohvC02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohvD02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ohwA02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-VIG |
| 1ohwB02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-VIG |
| 1ohwC02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-VIG |
| 1ohwD02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-VIG |
| 1ohyA02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-GEG |
| 1ohyB02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-GEG |
| 1ohyC02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-GEG |
| 1ohyD02 |
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Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-GEG |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| literature [5] & [6] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1gtxA01 |
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| 1gtxB01 |
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| 1gtxC01 |
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| 1gtxD01 |
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| 1ohvA01 |
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| 1ohvB01 |
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| 1ohvC01 |
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| 1ohvD01 |
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| 1ohwA01 |
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| 1ohwB01 |
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| 1ohwC01 |
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| 1ohwD01 |
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| 1ohyA01 |
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| 1ohyB01 |
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| 1ohyC01 |
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| 1ohyD01 |
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| 1gtxA02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1gtxB02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1gtxC02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1gtxD02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohvA02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohvB02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohvC02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohvD02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohwA02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohwB02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohwC02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohwD02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohyA02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohyB02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohyC02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| 1ohyD02 |
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GLU 270;LYS 329 | LYS 329(PLP binding) | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[5]
|
p.8633 | |
|
[6]
|
Scheme 2, Scheme 3 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6789830 |
| Journal | Biochem Biophys Res Commun |
| Year | 1981 |
| Volume | 99 |
| Pages | 1333-40 |
| Authors | Kim DS, Churchich JE |
| Title |
4-Aminobutyrate aminotransferase, |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7140743 |
| Journal | Eur J Biochem |
| Year | 1982 |
| Volume | 126 |
| Pages | 507-11 |
| Authors | Churchich JE |
| Title |
4-Aminobutyrate aminotransferase. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3780742 |
| Journal | Eur J Biochem |
| Year | 1986 |
| Volume | 161 |
| Pages | 289-94 |
| Authors | Choi SY, Churchich JE |
| Title | Biosynthesis of 4-aminobutyrate aminotransferase. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1901730 |
| Journal | Biochim Biophys Acta |
| Year | 1991 |
| Volume | 1077 |
| Pages | 187-91 |
| Authors | Kim YT, Churchich JE |
| Title | 4-Aminobutyrate aminotransferase: identification of lysine residues connected with catalytic activity. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) |
| Medline ID | 99321499 |
| PubMed ID | 10393538 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 8628-34 |
| Authors | Storici P, Capitani G, De Biase D, Moser M, John RA, Jansonius JN, Schirmer T |
| Title |
Crystal structure of GABA-aminotransferase, |
| Related PDB | 1gtx |
| Related UniProtKB | P80147 |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11853435 |
| Journal | J Am Chem Soc |
| Year | 2002 |
| Volume | 124 |
| Pages | 1620-4 |
| Authors | Choi S, Storici P, Schirmer T, Silverman RB |
| Title | Design of a conformationally restricted analogue of the antiepilepsy drug Vigabatrin that directs its mechanism of inactivation of gamma-aminobutyric acid aminotransferase. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14534310 |
| Journal | J Biol Chem |
| Year | 2004 |
| Volume | 279 |
| Pages | 363-73 |
| Authors | Storici P, De Biase D, Bossa F, Bruno S, Mozzarelli A, Peneff C, Silverman RB, Schirmer T |
| Title |
Structures of gamma-aminobutyric acid (GABA) aminotransferase, |
| Related PDB | 1ohv 1ohw 1ohy |
| Related UniProtKB | |
| Comments |
|---|
| Created | Updated |
|---|---|
| 2004-03-17 | 2009-02-26 |