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 27-MAR-2024, entry version 171. 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}. 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; 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.ENSSSCP00000035621; -. DR BindingDB; P80147; -. DR ChEMBL; CHEMBL2266; -. DR PaxDb; 9823-ENSSSCP00000008445; -. DR PeptideAtlas; P80147; -. DR Ensembl; ENSSSCT00005031973.1; ENSSSCP00005019489.1; ENSSSCG00005020319.1. DR Ensembl; ENSSSCT00005032000.1; ENSSSCP00005019507.1; ENSSSCG00005020319.1. DR Ensembl; ENSSSCT00005032107.1; ENSSSCP00005019569.1; ENSSSCG00005020319.1. DR Ensembl; ENSSSCT00005032119.1; ENSSSCP00005019578.1; ENSSSCG00005020319.1. DR Ensembl; ENSSSCT00015041462.1; ENSSSCP00015016382.1; ENSSSCG00015030409.1. DR Ensembl; ENSSSCT00030013900.1; ENSSSCP00030006205.1; ENSSSCG00030010026.1. DR Ensembl; ENSSSCT00035087217.1; ENSSSCP00035036388.1; ENSSSCG00035064690.1. DR Ensembl; ENSSSCT00045039444.1; ENSSSCP00045027448.1; ENSSSCG00045022701.1. DR Ensembl; ENSSSCT00050078286.1; ENSSSCP00050033681.1; ENSSSCG00050057376.1. DR Ensembl; ENSSSCT00060044527.1; ENSSSCP00060018992.1; ENSSSCG00060032875.1. DR Ensembl; ENSSSCT00065094756.1; ENSSSCP00065041447.1; ENSSSCG00065068901.1. DR GeneID; 397500; -. DR KEGG; ssc:397500; -. DR CTD; 18; -. DR eggNOG; KOG1405; Eukaryota. DR HOGENOM; CLU_016922_12_1_1; -. DR InParanoid; P80147; -. DR OMA; KTQVCGI; -. DR OrthoDB; 177625at2759; -. DR BRENDA; 2.6.1.19; 6170. DR Reactome; R-SSC-916853; Degradation of GABA. DR SABIO-RK; P80147; -. DR ChiTaRS; ABAT; pig. DR EvolutionaryTrace; P80147; -. DR PRO; PR:P80147; -. DR Proteomes; UP000008227; Unplaced. DR Proteomes; UP000314985; Unplaced. DR Proteomes; UP000694570; Unplaced. DR Proteomes; UP000694571; Unplaced. DR Proteomes; UP000694720; Unplaced. DR Proteomes; UP000694722; Unplaced. DR Proteomes; UP000694723; Unplaced. DR Proteomes; UP000694724; Unplaced. DR Proteomes; UP000694725; Unplaced. DR Proteomes; UP000694726; Unplaced. DR Proteomes; UP000694727; Unplaced. DR Proteomes; UP000694728; Unplaced. DR Bgee; ENSSSCG00000007909; Expressed in adult mammalian kidney and 45 other cell types or tissues. DR ExpressionAtlas; P80147; baseline and differential. 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:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central. 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 CDD; cd00610; OAT_like; 1. DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1. DR InterPro; IPR004631; 4NH2But_aminotransferase_euk. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR049704; Aminotrans_3_PPA_site. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; TIGR00699; GABAtrns_euk; 1. DR PANTHER; PTHR43206:SF4; 4-AMINOBUTYRATE AMINOTRANSFERASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR43206; AMINOTRANSFERASE; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. DR Genevisible; P80147; SS. 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 //