GenomeNet

Database: UniProt/SWISS-PROT
Entry: GABT_RAT
LinkDB: GABT_RAT
Original site: 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   23-MAY-2018, entry version 150.
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   Contains:
DE     RecName: Full=4-aminobutyrate aminotransferase, brain isoform;
DE   Contains:
DE     RecName: Full=4-aminobutyrate aminotransferase, liver isoform;
DE   Flags: Precursor;
GN   Name=Abat; Synonyms=Gabat;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=8133261;
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, AND PROTEOLYTIC
RP   PROCESSING.
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
RT   in liver and brain.";
RL   Eur. J. Biochem. 264:218-222(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
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
RT   project: 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-
CC       beta-aminoisobutyrate to succinate semialdehyde and methylmalonate
CC       semialdehyde, respectively. Can also convert delta-aminovalerate
CC       and beta-alanine.
CC   -!- CATALYTIC ACTIVITY: 4-aminobutanoate + 2-oxoglutarate = succinate
CC       semialdehyde + L-glutamate.
CC   -!- CATALYTIC ACTIVITY: (S)-3-amino-2-methylpropanoate + 2-
CC       oxoglutarate = 2-methyl-3-oxopropanoate + L-glutamate.
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:49601;
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.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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   UniGene; Rn.10090; -.
DR   ProteinModelPortal; P50554; -.
DR   SMR; P50554; -.
DR   STRING; 10116.ENSRNOP00000003633; -.
DR   BindingDB; P50554; -.
DR   ChEMBL; CHEMBL3148; -.
DR   iPTMnet; P50554; -.
DR   PhosphoSitePlus; P50554; -.
DR   SwissPalm; P50554; -.
DR   World-2DPAGE; 0004: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   eggNOG; COG0160; LUCA.
DR   GeneTree; ENSGT00550000074885; -.
DR   HOGENOM; HOG000020208; -.
DR   HOVERGEN; HBG000634; -.
DR   InParanoid; P50554; -.
DR   KO; K13524; -.
DR   OMA; IQTGGCG; -.
DR   OrthoDB; EOG091G08T5; -.
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; -.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
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; IC:UniProtKB.
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:0042493; P:response to drug; IDA: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   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004631; 4NH2But_aminotransferase_euk.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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; Complete proteome;
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     27       Mitochondrion.
FT   CHAIN        28    500       4-aminobutyrate aminotransferase, brain
FT                                isoform.
FT                                /FTId=PRO_0000001252.
FT   CHAIN        35    500       4-aminobutyrate aminotransferase, liver
FT                                isoform.
FT                                /FTId=PRO_0000001253.
FT   REGION      164    165       Pyridoxal phosphate binding.
FT                                {ECO:0000250|UniProtKB:P80147}.
FT   METAL       163    163       Iron-sulfur (2Fe-2S); shared with dimeric
FT                                partner. {ECO:0000250|UniProtKB:P80147}.
FT   METAL       166    166       Iron-sulfur (2Fe-2S); shared with dimeric
FT                                partner. {ECO:0000250|UniProtKB:P80147}.
FT   BINDING     220    220       Substrate.
FT                                {ECO:0000250|UniProtKB:P80147}.
FT   BINDING     381    381       Pyridoxal phosphate; shared with dimeric
FT                                partner. {ECO:0000250|UniProtKB:P80147}.
FT   MOD_RES     231    231       N6-succinyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     252    252       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     252    252       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     279    279       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     318    318       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     357    357       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000250|UniProtKB:P80147}.
FT   MOD_RES     413    413       N6-acetyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     413    413       N6-succinyllysine; alternate.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     452    452       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   MOD_RES     470    470       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P61922}.
FT   DISULFID    321    321       Interchain. {ECO:0000250}.
FT   CONFLICT      3      3       F -> L (in Ref. 1; AAA70415).
FT                                {ECO:0000305}.
FT   CONFLICT     25     25       S -> T (in Ref. 1; AAA70415).
FT                                {ECO:0000305}.
FT   CONFLICT     36     36       D -> T (in Ref. 1; AAA70415).
FT                                {ECO:0000305}.
FT   CONFLICT    135    170       PPENFVDKLRESLMSVAPKGMCQLITMACGSCSNEN -> L
FT                                QRTLWTSSGSPCSRWLPKACVSSSRWPAGPAPMRM (in
FT                                Ref. 1; AAA70415). {ECO:0000305}.
FT   CONFLICT    277    277       I -> N (in Ref. 1; AAA70415).
FT                                {ECO:0000305}.
FT   CONFLICT    425    425       Q -> R (in Ref. 1; AAA70415).
FT                                {ECO:0000305}.
FT   CONFLICT    447    447       E -> K (in Ref. 2 and 3; BAA25570).
FT                                {ECO:0000305}.
FT   CONFLICT    486    486       H -> Q (in Ref. 1; AAA70415).
FT                                {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
//
DBGET integrated database retrieval system