ID B7Z1V4_HUMAN Unreviewed; 515 AA.
AC B7Z1V4;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
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};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAH11640.1};
RN [1] {ECO:0000313|EMBL:BAH11640.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Cerebellum {ECO:0000313|EMBL:BAH11640.1};
RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A.,
RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y.,
RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T.,
RA Sugano S., Nomura N., Isogai T.;
RT "NEDO human cDNA sequencing project focused on splicing variants.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; AK293983; BAH11640.1; -; mRNA.
DR AlphaFoldDB; B7Z1V4; -.
DR MaxQB; B7Z1V4; -.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProt.
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 Aminotransferase {ECO:0000313|EMBL:BAH11640.1};
KW Neurotransmitter degradation {ECO:0000256|ARBA:ARBA00022867};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:BAH11640.1}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..515
FT /note="4-aminobutyrate aminotransferase, mitochondrial"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002866669"
SQ SEQUENCE 515 AA; 58229 MW; 70DCF0AC2CC77555 CRC64;
MWWQHAKGVP VPQGVMASML LAQRLACSFQ HSYRLLVPGS RHISQAAAKV DVEFDYDGPL
MKTEVPGPRS QELMKQLNII QNAEAVHFFC NYEESRGNYL VDVDGNRMLD LYSQISSVPI
GYSHPALLKL IQQPQNASMF VNRPALGILP PENFVEKLRQ SLLSVAPKGM SQLITMACGF
CSNENALKTI FMWYRSKERG QRGFSQEELE TCMINQAPGC PDYSILSFMG AFHGRTMGCL
ATTHSKAIHK IDIPSFDWPI APFPRLKYPL EEFVKENQQE EARCLEEVED LIVKYRKKKK
TVAGIIVEPI QSEGGDNHAS DDFFRKLRDI ARKHGCAFLV DEVQTGGGCT GKFWAHEHWG
LDDPADVMTF SKKMMTGGFF HREEFRPNAP YRIFNTWLGD PSKNLLLAEV INIIKREDLL
NNAAHAGKAL LTGLLDLQAR YPQFISRVRG RGTFCSFDTP DDSIRNKLIL IARNKGVVLG
GCGDKSIRFR PTLVFRDHHA HLFLNIFSDI LADFK
//
