GABT_BOVIN
ID GABT_BOVIN Reviewed; 500 AA.
AC Q9BGI0;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=4-aminobutyrate aminotransferase, mitochondrial;
DE EC=2.6.1.19;
DE AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
DE EC=2.6.1.22;
DE AltName: Full=GABA aminotransferase;
DE Short=GABA-AT;
DE AltName: Full=Gamma-amino-N-butyrate transaminase;
DE Short=GABA transaminase;
DE Short=GABA-T;
DE AltName: Full=L-AIBAT;
DE Flags: Precursor;
GN Name=ABAT; Synonyms=GABAT;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=11561735;
RA Jeon S.G., Bahn J.H., Jang J.S., Jang S.H., Lee B.R., Lee K.S., Park J.,
RA Kang T.C., Won M.H., Kim H.B., Kwo O.S., Cho S.W., Choi S.Y.;
RT "Molecular cloning and functional expression of bovine brain GABA
RT transaminase.";
RL Mol. Cells 12:91-96(2001).
CC -!- FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L-beta-
CC aminoisobutyrate to succinate semialdehyde and methylmalonate
CC semialdehyde, respectively. Can also convert delta-aminovalerate and
CC beta-alanine. {ECO:0000250|UniProtKB:P50554}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC Evidence={ECO:0000250|UniProtKB:P50554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23353;
CC Evidence={ECO:0000250|UniProtKB:P50554};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-3-amino-2-methylpropanoate + 2-oxoglutarate = 2-methyl-3-
CC oxopropanoate + L-glutamate; Xref=Rhea:RHEA:13993, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57700, ChEBI:CHEBI:58655; EC=2.6.1.22;
CC Evidence={ECO:0000250|UniProtKB:P50554};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13994;
CC Evidence={ECO:0000250|UniProtKB:P50554};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P80147};
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000250|UniProtKB:P80147};
CC Note=Binds 1 [2Fe-2S] cluster per homodimer.
CC {ECO:0000250|UniProtKB:P80147};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF305692; AAG59861.1; -; mRNA.
DR AlphaFoldDB; Q9BGI0; -.
DR SMR; Q9BGI0; -.
DR STRING; 9913.ENSBTAP00000005280; -.
DR BindingDB; Q9BGI0; -.
DR PRIDE; Q9BGI0; -.
DR eggNOG; KOG1405; Eukaryota.
DR InParanoid; Q9BGI0; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0032144; C:4-aminobutyrate transaminase complex; ISS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; NAS:UniProtKB.
DR GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0042802; F:identical protein binding; ISS:UniProtKB.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; ISS:UniProtKB.
DR GO; GO:0048148; P:behavioral response to cocaine; ISS:UniProtKB.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:UniProtKB.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IC:UniProtKB.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004631; 4NH2But_aminotransferase_euk.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00699; GABAtrns_euk; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Aminotransferase; Disulfide bond; Iron; Iron-sulfur;
KW Metal-binding; Mitochondrion; Neurotransmitter degradation;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..28
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN 29..500
FT /note="4-aminobutyrate aminotransferase, mitochondrial"
FT /id="PRO_0000001248"
FT BINDING 163
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 164..165
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 166
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 381
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT MOD_RES 231
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT MOD_RES 252
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT MOD_RES 252
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT MOD_RES 279
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT MOD_RES 318
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT MOD_RES 357
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT MOD_RES 413
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT MOD_RES 413
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT MOD_RES 452
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT MOD_RES 470
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61922"
FT DISULFID 321
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 500 AA; 56731 MW; DC622157B9326CBA CRC64;
MASMLVAQRL ACSFQHSYRL LVPGSRHISQ AAAKVDVEFD YDGRLMKTEV PGLRCQELMK
QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYSHP GLLKLIQQPQ
NASMFVNRPA LGILLPENFV EKLRQSLLSV APKGMSQLIT MACGSCSNEN GLKTIFMWYR
SKERGQRGFP QEELETCMIN QAPWCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS
FDWPIAPFPR LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG
DNHASDDFFR KLRDIPRKQC CAFLVDVVQT GGGCTGKFWA HEHWARDDPE DVMTSSKKMM
TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNAAH AGKALLTGLL
DLQARYPQFI SRVRGRGTFC SFDTPDDSIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF
RDHHAHLFLN IFSDILADFK
