ID   GABT_MOUSE              Reviewed;         500 AA.
AC   P61922; Q8BZA3;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=4-aminobutyrate aminotransferase, mitochondrial;
DE            EC=2.6.1.19 {ECO:0000250|UniProtKB:P50554};
DE   AltName: Full=(S)-3-amino-2-methylpropionate transaminase;
DE            EC=2.6.1.22 {ECO:0000250|UniProtKB:P50554};
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 {ECO:0000312|MGI:MGI:2443582}; Synonyms=Gabat;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
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   [3]
RP   PROTEIN SEQUENCE OF 35-47; 61-173; 221-231; 236-279; 286-310; 318-337;
RP   368-410; 414-432; 437-450 AND 461-470, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RC   STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA   Lubec G., Klug S., Friebe K., Kang S.U., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [5]
RP   SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-231; LYS-252 AND LYS-413, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-252; LYS-279; LYS-318; LYS-413;
RP   LYS-452 AND LYS-470, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=23576753; DOI=10.1073/pnas.1302961110;
RA   Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B.,
RA   Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.;
RT   "Label-free quantitative proteomics of the lysine acetylome in mitochondria
RT   identifies substrates of SIRT3 in metabolic pathways.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P61922-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P61922-2; Sequence=VSP_012005;
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; BC058079; AAH58079.1; -; mRNA.
DR   EMBL; BC058521; AAH58521.1; -; mRNA.
DR   EMBL; AK036128; BAC29312.1; -; mRNA.
DR   CCDS; CCDS27939.1; -. [P61922-1]
DR   CCDS; CCDS49754.1; -. [P61922-2]
DR   RefSeq; NP_001164449.1; NM_001170978.1. [P61922-2]
DR   RefSeq; NP_766549.2; NM_172961.3. [P61922-1]
DR   AlphaFoldDB; P61922; -.
DR   SMR; P61922; -.
DR   BioGRID; 234569; 11.
DR   IntAct; P61922; 1.
DR   MINT; P61922; -.
DR   STRING; 10090.ENSMUSP00000063548; -.
DR   BindingDB; P61922; -.
DR   ChEMBL; CHEMBL4523258; -.
DR   GlyGen; P61922; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; P61922; -.
DR   PhosphoSitePlus; P61922; -.
DR   SwissPalm; P61922; -.
DR   REPRODUCTION-2DPAGE; IPI00407499; -.
DR   jPOST; P61922; -.
DR   MaxQB; P61922; -.
DR   PaxDb; 10090-ENSMUSP00000063548; -.
DR   PeptideAtlas; P61922; -.
DR   ProteomicsDB; 271823; -. [P61922-1]
DR   ProteomicsDB; 271824; -. [P61922-2]
DR   Antibodypedia; 24533; 456 antibodies from 30 providers.
DR   DNASU; 268860; -.
DR   Ensembl; ENSMUST00000065987.14; ENSMUSP00000063548.8; ENSMUSG00000057880.13. [P61922-1]
DR   Ensembl; ENSMUST00000115839.9; ENSMUSP00000111505.3; ENSMUSG00000057880.13. [P61922-2]
DR   GeneID; 268860; -.
DR   KEGG; mmu:268860; -.
DR   UCSC; uc007yco.2; mouse. [P61922-1]
DR   UCSC; uc007ycp.2; mouse. [P61922-2]
DR   AGR; MGI:2443582; -.
DR   MGI; MGI:2443582; Abat.
DR   VEuPathDB; HostDB:ENSMUSG00000057880; -.
DR   eggNOG; KOG1405; Eukaryota.
DR   GeneTree; ENSGT00550000074885; -.
DR   HOGENOM; CLU_016922_12_0_1; -.
DR   InParanoid; P61922; -.
DR   OMA; KTQVCGI; -.
DR   OrthoDB; 177625at2759; -.
DR   PhylomeDB; P61922; -.
DR   TreeFam; TF105021; -.
DR   BRENDA; 2.6.1.19; 3474.
DR   Reactome; R-MMU-916853; Degradation of GABA.
DR   BioGRID-ORCS; 268860; 0 hits in 79 CRISPR screens.
DR   ChiTaRS; Abat; mouse.
DR   PRO; PR:P61922; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P61922; Protein.
DR   Bgee; ENSMUSG00000057880; Expressed in nucleus accumbens and 243 other cell types or tissues.
DR   ExpressionAtlas; P61922; baseline and differential.
DR   GO; GO:0032144; C:4-aminobutyrate transaminase complex; ISS:UniProtKB.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:MGI.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; ISO:MGI.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; ISO:MGI.
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; IMP:UniProtKB.
DR   GO; GO:0021549; P:cerebellum development; IEA:Ensembl.
DR   GO; GO:0007620; P:copulation; ISO:MGI.
DR   GO; GO:0035640; P:exploration behavior; ISO:MGI.
DR   GO; GO:0009449; P:gamma-aminobutyric acid biosynthetic process; ISO:MGI.
DR   GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; ISO:MGI.
DR   GO; GO:0007626; P:locomotory behavior; ISO:MGI.
DR   GO; GO:0045776; P:negative regulation of blood pressure; ISO:MGI.
DR   GO; GO:0033602; P:negative regulation of dopamine secretion; ISO:MGI.
DR   GO; GO:0014053; P:negative regulation of gamma-aminobutyric acid secretion; ISO:MGI.
DR   GO; GO:1904450; P:positive regulation of aspartate secretion; ISO:MGI.
DR   GO; GO:0045964; P:positive regulation of dopamine metabolic process; ISO:MGI.
DR   GO; GO:0031652; P:positive regulation of heat generation; ISO:MGI.
DR   GO; GO:0097151; P:positive regulation of inhibitory postsynaptic potential; ISO:MGI.
DR   GO; GO:0032024; P:positive regulation of insulin secretion; ISO:MGI.
DR   GO; GO:1902722; P:positive regulation of prolactin secretion; ISO:MGI.
DR   GO; GO:0070474; P:positive regulation of uterine smooth muscle contraction; ISO:MGI.
DR   GO; GO:0042220; P:response to cocaine; ISO:MGI.
DR   GO; GO:0045471; P:response to ethanol; ISO:MGI.
DR   GO; GO:0001666; P:response to hypoxia; ISO:MGI.
DR   GO; GO:0010039; P:response to iron ion; ISO:MGI.
DR   GO; GO:0035094; P:response to nicotine; ISO:MGI.
DR   GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
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   Genevisible; P61922; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; 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:0000250"
FT   CHAIN           29..500
FT                   /note="4-aminobutyrate aminotransferase, mitochondrial"
FT                   /id="PRO_0000001250"
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:0007744|PubMed:23806337"
FT   MOD_RES         252
FT                   /note="N6-acetyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         252
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         279
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         318
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
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:0007744|PubMed:23576753"
FT   MOD_RES         413
FT                   /note="N6-succinyllysine; alternate"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         452
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   MOD_RES         470
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23576753"
FT   DISULFID        321
FT                   /note="Interchain"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         319..374
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_012005"
SQ   SEQUENCE   500 AA;  56452 MW;  85AA331AB48355F3 CRC64;
     MAFLLITRRL ACSSQKNLHL FIPGSRYISQ AAAKVDIEFD YDGPLMKTEV PGPRSKELMK
     QLNTIQNAEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSVPIGYNHP ALAKLVQQPQ
     NASTFINRPA LGILPPENFV DKLQESLMSV APRGMSQLIT MACGSCSNEN AFKTIFMWYR
     SKERGQRGFS KEELETCMVN QSPGCPDYSI LSFMGAFHGR TMGCLATTHS KAIHKIDIPS
     FDWPIAPFPR LKYPLEEFTT DNQQEEARCL EEVEDLIVKY RKKKRTVAGI IVEPIQSEGG
     DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGCTGKFWA HEHWGLDDPA DVMTFSKKMM
     TGGFFHKEEF RPSAPYRIFN TWLGDPSKNL LLAEVINIIK REDLLNNVAR VGKTLLTGLL
     DLQAQYPQFI SRVRGRGTFC SFDTPDEAIR NKLILIARNK GVVLGGCGDK SIRFRPTLVF
     RDHHAHLFLS IFSGILADFK
//