GABT_PIG
ID GABT_PIG Reviewed; 500 AA.
AC P80147; P27820;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 2.
DT 03-AUG-2022, entry version 162.
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 Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=1559966; DOI=10.1016/s0021-9258(18)42506-9;
RA Kwon O.S., Park J., Churchich J.E.;
RT "Brain 4-aminobutyrate aminotransferase. Isolation and sequence of a cDNA
RT encoding the enzyme.";
RL J. Biol. Chem. 267:7215-7216(1992).
RN [2]
RP PROTEIN SEQUENCE OF 29-500.
RC TISSUE=Liver;
RX PubMed=1521531; DOI=10.1111/j.1432-1033.1992.tb17193.x;
RA de Biase D., Maras B., Bossa F., Barra D., John R.A.;
RT "Protein structure of pig liver 4-aminobutyrate aminotransferase and
RT comparison with a cDNA-deduced sequence.";
RL Eur. J. Biochem. 208:351-357(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS), PYRIDOXAL PHOSPHATE AT LYS-357, AND
RP SUBUNIT.
RC TISSUE=Liver;
RX PubMed=10393538; DOI=10.1021/bi990478j;
RA Storici P., Capitani G., De Biase D., Moser M., John R.A., Jansonius J.N.,
RA Schirmer T.;
RT "Crystal structure of GABA-aminotransferase, a target for antiepileptic
RT drug therapy.";
RL Biochemistry 38:8628-8634(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG,
RP PYRIDOXAL PHOSPHATE AT LYS-357, AND COFACTOR.
RX PubMed=14534310; DOI=10.1074/jbc.m305884200;
RA Storici P., De Biase D., Bossa F., Bruno S., Mozzarelli A., Peneff C.,
RA Silverman R.B., Schirmer T.;
RT "Structures of gamma-aminobutyric acid (GABA) aminotransferase, a pyridoxal
RT 5'-phosphate, and [2Fe-2S] cluster-containing enzyme, complexed with gamma-
RT ethynyl-GABA and with the antiepilepsy drug vigabatrin.";
RL J. Biol. Chem. 279:363-373(2004).
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:0000269|PubMed:10393538, ECO:0000269|PubMed:14534310};
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000269|PubMed:14534310};
CC Note=Binds 1 [2Fe-2S] cluster per homodimer.
CC {ECO:0000269|PubMed:14534310};
CC -!- SUBUNIT: Homodimer; disulfide-linked.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; M84802; AAA96981.1; -; mRNA.
DR RefSeq; NP_999428.1; NM_214263.1.
DR PDB; 1OHV; X-ray; 2.30 A; A/B/C/D=29-500.
DR PDB; 1OHW; X-ray; 2.30 A; A/B/C/D=29-500.
DR PDB; 1OHY; X-ray; 2.80 A; A/B/C/D=29-500.
DR PDB; 4Y0D; X-ray; 2.19 A; A/B/C/D=39-500.
DR PDB; 4Y0H; X-ray; 1.63 A; A/B/C/D=39-500.
DR PDB; 4Y0I; X-ray; 1.66 A; A/B/C/D=39-499.
DR PDB; 4ZSW; X-ray; 1.70 A; A/B/C/D=39-499.
DR PDB; 4ZSY; X-ray; 1.70 A; A/B/C/D=39-499.
DR PDB; 6B6G; X-ray; 1.95 A; A/B/C/D=39-500.
DR PDBsum; 1OHV; -.
DR PDBsum; 1OHW; -.
DR PDBsum; 1OHY; -.
DR PDBsum; 4Y0D; -.
DR PDBsum; 4Y0H; -.
DR PDBsum; 4Y0I; -.
DR PDBsum; 4ZSW; -.
DR PDBsum; 4ZSY; -.
DR PDBsum; 6B6G; -.
DR AlphaFoldDB; P80147; -.
DR SMR; P80147; -.
DR BioGRID; 1149627; 1.
DR STRING; 9823.ENSSSCP00000008445; -.
DR BindingDB; P80147; -.
DR ChEMBL; CHEMBL2266; -.
DR PaxDb; P80147; -.
DR PeptideAtlas; P80147; -.
DR PRIDE; P80147; -.
DR Ensembl; ENSSSCT00000039445; ENSSSCP00000045366; ENSSSCG00000007909.
DR Ensembl; ENSSSCT00005031973; ENSSSCP00005019489; ENSSSCG00005020319.
DR Ensembl; ENSSSCT00005032000; ENSSSCP00005019507; ENSSSCG00005020319.
DR Ensembl; ENSSSCT00005032107; ENSSSCP00005019569; ENSSSCG00005020319.
DR Ensembl; ENSSSCT00005032119; ENSSSCP00005019578; ENSSSCG00005020319.
DR Ensembl; ENSSSCT00015041462; ENSSSCP00015016382; ENSSSCG00015030409.
DR Ensembl; ENSSSCT00030013900; ENSSSCP00030006205; ENSSSCG00030010026.
DR Ensembl; ENSSSCT00035087217; ENSSSCP00035036388; ENSSSCG00035064690.
DR Ensembl; ENSSSCT00045039444; ENSSSCP00045027448; ENSSSCG00045022701.
DR Ensembl; ENSSSCT00050078286; ENSSSCP00050033681; ENSSSCG00050057376.
DR Ensembl; ENSSSCT00060044527; ENSSSCP00060018992; ENSSSCG00060032875.
DR Ensembl; ENSSSCT00065094756; ENSSSCP00065041447; ENSSSCG00065068901.
DR GeneID; 397500; -.
DR KEGG; ssc:397500; -.
DR CTD; 18; -.
DR VGNC; VGNC:96910; ABAT.
DR eggNOG; KOG1405; Eukaryota.
DR GeneTree; ENSGT00550000074885; -.
DR HOGENOM; CLU_016922_12_1_1; -.
DR InParanoid; P80147; -.
DR OMA; DPPDMVT; -.
DR OrthoDB; 566705at2759; -.
DR BRENDA; 2.6.1.19; 6170.
DR SABIO-RK; P80147; -.
DR ChiTaRS; ABAT; pig.
DR EvolutionaryTrace; P80147; -.
DR PRO; PR:P80147; -.
DR Proteomes; UP000008227; Chromosome 3.
DR Proteomes; UP000314985; Unplaced.
DR Bgee; ENSSSCG00000007909; Expressed in adult mammalian kidney and 45 other tissues.
DR ExpressionAtlas; P80147; baseline and differential.
DR Genevisible; P80147; SS.
DR GO; GO:0032144; C:4-aminobutyrate transaminase complex; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:UniProtKB.
DR GO; GO:0005759; C:mitochondrial matrix; TAS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0032145; F:succinate-semialdehyde dehydrogenase binding; IDA: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.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; 3D-structure; Acetylation; Aminotransferase;
KW Direct protein sequencing; 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:0000269|PubMed:1521531"
FT CHAIN 29..500
FT /note="4-aminobutyrate aminotransferase, mitochondrial"
FT /id="PRO_0000001251"
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:0000269|PubMed:14534310"
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:0000269|PubMed:10393538"
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:0000269|PubMed:14534310"
FT BINDING 220
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:14534310,
FT ECO:0000305|PubMed:10393538"
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:0000269|PubMed:10393538,
FT ECO:0000269|PubMed:14534310"
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:0000269|PubMed:10393538"
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"
FT CONFLICT 454
FT /note="I -> N (in Ref. 1; AAA96981)"
FT /evidence="ECO:0000305"
FT HELIX 53..65
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 92..97
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:4Y0H"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 139..145
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 147..150
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 164..184
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 191..197
FT /evidence="ECO:0007829|PDB:4Y0H"
FT TURN 198..200
FT /evidence="ECO:0007829|PDB:4Y0H"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 209..213
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 232..235
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 259..282
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 287..292
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:4Y0H"
FT TURN 298..300
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:4Y0H"
FT TURN 328..335
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 336..339
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 340..344
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 360..366
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 373..378
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:4ZSW"
FT HELIX 386..401
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 404..425
FT /evidence="ECO:0007829|PDB:4Y0H"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 431..436
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 439..443
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 465..467
FT /evidence="ECO:0007829|PDB:4Y0H"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:4Y0H"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:4Y0H"
FT HELIX 482..498
FT /evidence="ECO:0007829|PDB:4Y0H"
SQ SEQUENCE 500 AA; 56620 MW; BFD0B80846CEF5B7 CRC64;
MASVLLTRRL ACSFRHNHRL LVPGWRHISQ AAAKVDVEFD YDGPLMKTEV PGPRSRELMK
QLNIIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSIPIGYSHP ALVKLVQQPQ
NVSTFINRPA LGILPPENFV EKLRESLLSV APKGMSQLIT MACGSCSNEN AFKTIFMWYR
SKERGQSAFS KEELETCMIN QAPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS
FDWPIAPFPR LKYPLEEFVK ENQQEEARCL EEVEDLIVKY RKKKKTVAGI IVEPIQSEGG
DNHASDDFFR KLRDISRKHG CAFLVDEVQT GGGSTGKFWA HEHWGLDDPA DVMTFSKKMM
TGGFFHKEEF RPNAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLSNAAH AGKVLLTGLL
DLQARYPQFI SRVRGRGTFC SFDTPDESIR NKLISIARNK GVMLGGCGDK SIRFRPTLVF
RDHHAHLFLN IFSDILADFK
