ID GABT_RAT Reviewed; 500 AA. AC P50554; O70539; Q66HM1; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 174. DE RecName: Full=4-aminobutyrate aminotransferase, mitochondrial; DE Short=beta-AlaAT I {ECO:0000303|PubMed:10447691}; DE EC=2.6.1.19 {ECO:0000269|PubMed:10447691}; DE AltName: Full=(S)-3-amino-2-methylpropionate transaminase; DE EC=2.6.1.22 {ECO:0000269|PubMed:10989446}; 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 Contains: DE RecName: Full=4-aminobutyrate aminotransferase, brain isoform {ECO:0000303|PubMed:10447691}; DE Contains: DE RecName: Full=4-aminobutyrate aminotransferase, liver isoform {ECO:0000303|PubMed:10447691}; DE Flags: Precursor; GN Name=Abat {ECO:0000312|RGD:620948}; Synonyms=Gabat; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC TISSUE=Brain; RX PubMed=8133261; DOI=10.1046/j.1471-4159.1994.62041267.x; RA Medina-Kauwe L.K., Tillakaratne N.J., Wu J.Y., Tobin A.J.; RT "A rat brain cDNA encodes enzymatically active GABA transaminase and RT provides a molecular probe for GABA-catabolizing cells."; RL J. Neurochem. 62:1267-1275(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 35-54, PROTEOLYTIC RP PROCESSING, AND SUBCELLULAR LOCATION. RC STRAIN=Sprague-Dawley; TISSUE=Brain, and Liver; RX PubMed=10447691; DOI=10.1046/j.1432-1327.1999.00612.x; RA Kontani Y., Sakata S.F., Matsuda K., Ohyama T., Sano K., Tamaki N.; RT "The mature size of rat 4-aminobutyrate aminotransferase is different in RT liver and brain."; RL Eur. J. Biochem. 264:218-222(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, FUNCTION, AND CATALYTIC RP ACTIVITY. RC STRAIN=Sprague-Dawley; TISSUE=Liver; RX PubMed=10989446; DOI=10.1016/s0076-6879(00)24247-x; RA Tamaki N., Sakata S.F., Matsuda K.; RT "Purification, properties, and sequencing of aminoisobutyrate RT aminotransferases from rat liver."; RL Methods Enzymol. 324:376-389(2000). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP PROTEIN SEQUENCE OF 253-268 AND 389-400, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord; RA Lubec G., Afjehi-Sadat L.; RL Submitted (NOV-2006) to UniProtKB. CC -!- FUNCTION: Catalyzes the conversion of gamma-aminobutyrate and L-beta- CC aminoisobutyrate to succinate semialdehyde and methylmalonate CC semialdehyde, respectively (PubMed:10447691). Can also convert delta- CC aminovalerate and beta-alanine (PubMed:10447691). CC {ECO:0000269|PubMed:10447691, ECO:0000269|PubMed:10989446}. 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:0000269|PubMed:10447691, ECO:0000269|PubMed:10989446}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23353; CC Evidence={ECO:0000305|PubMed:10447691, ECO:0000305|PubMed:10989446}; 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:0000269|PubMed:10989446}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13994; CC Evidence={ECO:0000305|PubMed:10989446}; 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 -!- BIOPHYSICOCHEMICAL PROPERTIES: [4-aminobutyrate aminotransferase, liver isoform]: CC Kinetic parameters: CC KM=1.6 mM for 4-aminobutanoate {ECO:0000269|PubMed:10447691}; CC KM=5.3 mM for beta-alanine {ECO:0000269|PubMed:10447691}; CC Vmax=0.83 umol/min/mg enzyme {ECO:0000269|PubMed:10447691}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: [4-aminobutyrate aminotransferase, brain isoform]: CC Kinetic parameters: CC KM=1.6 mM for 4-aminobutanoate {ECO:0000269|PubMed:10447691}; CC KM=6.1 mM for beta-alanine {ECO:0000269|PubMed:10447691}; CC Vmax=1 umol/min/mg enzyme {ECO:0000269|PubMed:10447691}; CC -!- SUBUNIT: Homodimer; disulfide-linked. CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix CC {ECO:0000305|PubMed:10447691}. 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; U29701; AAA70415.1; -; mRNA. DR EMBL; D87839; BAA25570.1; -; mRNA. DR EMBL; BC081787; AAH81787.1; -; mRNA. DR PIR; I56502; I56502. DR RefSeq; NP_112265.1; NM_031003.2. DR RefSeq; XP_006245822.1; XM_006245760.3. DR AlphaFoldDB; P50554; -. DR SMR; P50554; -. DR BioGRID; 249532; 1. DR IntAct; P50554; 1. DR MINT; P50554; -. DR STRING; 10116.ENSRNOP00000003633; -. DR BindingDB; P50554; -. DR ChEMBL; CHEMBL3148; -. DR DrugCentral; P50554; -. DR iPTMnet; P50554; -. DR PhosphoSitePlus; P50554; -. DR SwissPalm; P50554; -. DR jPOST; P50554; -. DR PaxDb; 10116-ENSRNOP00000003633; -. DR Ensembl; ENSRNOT00000003633.5; ENSRNOP00000003633.2; ENSRNOG00000002636.8. DR Ensembl; ENSRNOT00055043768; ENSRNOP00055035754; ENSRNOG00055025368. DR Ensembl; ENSRNOT00060017651; ENSRNOP00060013718; ENSRNOG00060010424. DR Ensembl; ENSRNOT00065004124; ENSRNOP00065002944; ENSRNOG00065002947. DR GeneID; 81632; -. DR KEGG; rno:81632; -. DR UCSC; RGD:620948; rat. DR AGR; RGD:620948; -. DR CTD; 18; -. DR RGD; 620948; Abat. DR eggNOG; KOG1405; Eukaryota. DR GeneTree; ENSGT00550000074885; -. DR HOGENOM; CLU_016922_12_1_1; -. DR InParanoid; P50554; -. DR OMA; KTQVCGI; -. DR OrthoDB; 177625at2759; -. DR PhylomeDB; P50554; -. DR TreeFam; TF105021; -. DR BRENDA; 2.6.1.19; 5301. DR Reactome; R-RNO-916853; Degradation of GABA. DR SABIO-RK; P50554; -. DR PRO; PR:P50554; -. DR Proteomes; UP000002494; Chromosome 10. DR Bgee; ENSRNOG00000002636; Expressed in liver and 15 other cell types or tissues. DR GO; GO:0032144; C:4-aminobutyrate transaminase complex; ISS:UniProtKB. DR GO; GO:0005759; C:mitochondrial matrix; IDA:RGD. 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:0003867; F:4-aminobutyrate transaminase activity; IDA:RGD. DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; ISO:RGD. 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:0032145; F:succinate-semialdehyde dehydrogenase binding; ISS:UniProtKB. DR GO; GO:0048148; P:behavioral response to cocaine; ISS:UniProtKB. DR GO; GO:0021549; P:cerebellum development; IEP:RGD. DR GO; GO:0007620; P:copulation; IMP:RGD. DR GO; GO:0035640; P:exploration behavior; IMP:RGD. DR GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; IMP:RGD. DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central. DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; ISO:RGD. DR GO; GO:0007626; P:locomotory behavior; IMP:RGD. DR GO; GO:0045776; P:negative regulation of blood pressure; IMP:RGD. DR GO; GO:0033602; P:negative regulation of dopamine secretion; IMP:RGD. DR GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; IMP:RGD. DR GO; GO:1904450; P:positive regulation of aspartate secretion; IMP:RGD. DR GO; GO:0045964; P:positive regulation of dopamine metabolic process; IMP:RGD. DR GO; GO:0031652; P:positive regulation of heat generation; IMP:RGD. DR GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; IMP:RGD. DR GO; GO:0032024; P:positive regulation of insulin secretion; IMP:RGD. DR GO; GO:1902722; P:positive regulation of prolactin secretion; IMP:RGD. DR GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; IMP:RGD. DR GO; GO:0042220; P:response to cocaine; IMP:RGD. DR GO; GO:0045471; P:response to ethanol; IDA:RGD. DR GO; GO:0001666; P:response to hypoxia; IMP:RGD. DR GO; GO:0010039; P:response to iron ion; IDA:RGD. DR GO; GO:0035094; P:response to nicotine; IMP:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; IDA:RGD. 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:SF1; 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 World-2DPAGE; 0004:P50554; -. DR Genevisible; P50554; RN. PE 1: Evidence at protein level; KW Acetylation; Aminotransferase; Direct protein sequencing; Disulfide bond; KW Iron; Iron-sulfur; Metal-binding; Mitochondrion; KW Neurotransmitter degradation; Pyridoxal phosphate; Reference proteome; KW Transferase; Transit peptide. FT TRANSIT 1..27 FT /note="Mitochondrion" FT CHAIN 28..500 FT /note="4-aminobutyrate aminotransferase, brain isoform" FT /evidence="ECO:0000303|PubMed:10447691" FT /id="PRO_0000001252" FT CHAIN 35..500 FT /note="4-aminobutyrate aminotransferase, liver isoform" FT /evidence="ECO:0000303|PubMed:10447691" FT /id="PRO_0000001253" 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" FT CONFLICT 3 FT /note="F -> L (in Ref. 1; AAA70415)" FT /evidence="ECO:0000305" FT CONFLICT 25 FT /note="S -> T (in Ref. 1; AAA70415)" FT /evidence="ECO:0000305" FT CONFLICT 36 FT /note="D -> T (in Ref. 1; AAA70415)" FT /evidence="ECO:0000305" FT CONFLICT 135..170 FT /note="PPENFVDKLRESLMSVAPKGMCQLITMACGSCSNEN -> LQRTLWTSSGSP FT CSRWLPKACVSSSRWPAGPAPMRM (in Ref. 1; AAA70415)" FT /evidence="ECO:0000305" FT CONFLICT 277 FT /note="I -> N (in Ref. 1; AAA70415)" FT /evidence="ECO:0000305" FT CONFLICT 425 FT /note="Q -> R (in Ref. 1; AAA70415)" FT /evidence="ECO:0000305" FT CONFLICT 447 FT /note="E -> K (in Ref. 2 and 3; BAA25570)" FT /evidence="ECO:0000305" FT CONFLICT 486 FT /note="H -> Q (in Ref. 1; AAA70415)" FT /evidence="ECO:0000305" SQ SEQUENCE 500 AA; 56456 MW; 1EA7180B72797B72 CRC64; MAFLLTTRRL VCSSQKNLHL FTPGSRYISQ AAAKVDFEFD YDGPLMKTEV PGPRSQELMK QLNTIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYNHP ALAKLVQQPQ NASTFINRPA LGILPPENFV DKLRESLMSV APKGMCQLIT MACGSCSNEN AFKTIFMWYR SKERGQRGFS KEELETCMVN QSPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS FDWPIAPFPR LKYPLEEFVT DNQQEEARCL EEVEDLIVKY RKKKRTVAGI IVEPIQSEGG DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMSFSKKMM TGGFFHKEEF RPSAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNVAH AGKTLLTGLL DLQAQYPQFV SRVRGRGTFC SFDTPDEAIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF RDHHAHLFLN IFSGILADFK //