ID   Q6GM94_XENLA            Unreviewed;       500 AA.
AC   Q6GM94;
DT   19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=4-aminobutyrate aminotransferase, mitochondrial {ECO:0000256|ARBA:ARBA00015937};
DE            EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE            EC=2.6.1.22 {ECO:0000256|ARBA:ARBA00012876};
DE   AltName: Full=(S)-3-amino-2-methylpropionate transaminase {ECO:0000256|ARBA:ARBA00030857};
DE   AltName: Full=GABA aminotransferase {ECO:0000256|ARBA:ARBA00031787};
DE   AltName: Full=Gamma-amino-N-butyrate transaminase {ECO:0000256|ARBA:ARBA00030204};
DE   AltName: Full=L-AIBAT {ECO:0000256|ARBA:ARBA00029760};
GN   Name=abat.L {ECO:0000313|RefSeq:NP_001083628.1,
GN   ECO:0000313|Xenbase:XB-GENE-17338517};
GN   Synonyms=abat {ECO:0000313|Xenbase:XB-GENE-17338517}, MGC68458
GN   {ECO:0000313|EMBL:AAH74179.1};
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355 {ECO:0000313|EMBL:AAH74179.1};
RN   [1] {ECO:0000313|RefSeq:NP_001083628.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=12454917; DOI=10.1002/dvdy.10174;
RA   Klein S.L., Strausberg R.L., Wagner L., Pontius J., Clifton S.W.,
RA   Richardson P.;
RT   "Genetic and genomic tools for Xenopus research: The NIH Xenopus
RT   initiative.";
RL   Dev. Dyn. 225:384-391(2002).
RN   [2] {ECO:0000313|EMBL:AAH74179.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney {ECO:0000313|EMBL:AAH74179.1};
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|RefSeq:NP_001083628.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00033650};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13994;
CC         Evidence={ECO:0000256|ARBA:ARBA00033650};
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:0000256|ARBA:ARBA00033680};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23353;
CC         Evidence={ECO:0000256|ARBA:ARBA00033680};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000256|ARBA:ARBA00011748}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC       ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; BC074179; AAH74179.1; -; mRNA.
DR   RefSeq; NP_001083628.1; NM_001090159.1.
DR   DNASU; 399028; -.
DR   GeneID; 399028; -.
DR   KEGG; xla:399028; -.
DR   AGR; Xenbase:XB-GENE-17338517; -.
DR   Xenbase; XB-GENE-17338517; abat.L.
DR   OrthoDB; 177625at2759; -.
DR   Proteomes; UP000186698; Chromosome 9_10L.
DR   Bgee; 399028; Expressed in kidney and 19 other cell types or tissues.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
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.
PE   2: Evidence at transcript level;
KW   Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000186698}.
SQ   SEQUENCE   500 AA;  56317 MW;  E38241100E9FA3B8 CRC64;
     MASVLLARQV TLNLQQNTRL LVPCVRYVSQ AAAKKNVDFE YDGPLMKTEV PGPRSKELIK
     QLSKIQNSEA VHFFCNYEES RGNYLVDVDG NRMLDLYSQI SSIPIGYNHP ALIKVLQQPQ
     NLSSFVNRPA LGILPPENFT EKLEDSLLSI GPKGLRQVIT MSCGSCSNEN AFKLIFMWYR
     NKERGPTGVT KEELDSCMIN QLPGCPDYSI LSFMGGFHGR TMGCLATTHS KAIHKLDVPS
     FDWPIAPFPR LKYPLEQFVK ENQDEEARCL EEVEDLIVKY RKKKKTVAGI VVEPIQSEGG
     DNHASDDFFR KLRDIARKHG CAFLVDEVQT GGGSTGKFWA HEHWGMDDPA DVVTFSKKMI
     TGGFFHKEEL RPDAPYRIFN TWLGDPSKNL LLAEVLNVIK REDLLSNTVQ AGKALHDGLL
     DFQARYPHLV SRARGRGTFC SFDAPSDAIR NQIILQARNK GIVLGGCGDK SIRFRPTLVF
     KEHHAHLFLN IFNDILADFK
//