GABT_RAT
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 03-AUG-2022, entry version 166.
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}.
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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 World-2DPAGE; 0004:P50554; -.
DR jPOST; P50554; -.
DR PaxDb; P50554; -.
DR PRIDE; P50554; -.
DR Ensembl; ENSRNOT00000003633; ENSRNOP00000003633; ENSRNOG00000002636.
DR GeneID; 81632; -.
DR KEGG; rno:81632; -.
DR UCSC; RGD:620948; rat.
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; DPPDMVT; -.
DR OrthoDB; 566705at2759; -.
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 tissues.
DR Genevisible; P50554; RN.
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; IDA:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:RGD.
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; 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:0032145; F:succinate-semialdehyde dehydrogenase binding; ISS:UniProtKB.
DR GO; GO:0007568; P:aging; IDA:RGD.
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:0090331; P:negative regulation of platelet aggregation; IMP:RGD.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IC:UniProtKB.
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; 3.40.640.10; -; 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 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
