GABT_CAEEL
ID GABT_CAEEL Reviewed; 483 AA.
AC Q21217;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable 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 AltName: Full=L-AIBAT;
DE Flags: Precursor;
GN Name=gta-1; ORFNames=K04D7.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 -!- 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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P80147};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P80147}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; Z69664; CAA93517.1; -; Genomic_DNA.
DR PIR; T23312; T23312.
DR RefSeq; NP_501862.1; NM_069461.3.
DR AlphaFoldDB; Q21217; -.
DR SMR; Q21217; -.
DR BioGRID; 42999; 40.
DR STRING; 6239.K04D7.3a; -.
DR World-2DPAGE; 0020:Q21217; -.
DR EPD; Q21217; -.
DR PaxDb; Q21217; -.
DR PeptideAtlas; Q21217; -.
DR EnsemblMetazoa; K04D7.3a.1; K04D7.3a.1; WBGene00001794.
DR GeneID; 177897; -.
DR KEGG; cel:CELE_K04D7.3; -.
DR UCSC; K04D7.3; c. elegans.
DR CTD; 177897; -.
DR WormBase; K04D7.3a; CE06092; WBGene00001794; gta-1.
DR eggNOG; KOG1405; Eukaryota.
DR GeneTree; ENSGT00550000074885; -.
DR InParanoid; Q21217; -.
DR OMA; DPPDMVT; -.
DR OrthoDB; 566705at2759; -.
DR PhylomeDB; Q21217; -.
DR Reactome; R-CEL-916853; Degradation of GABA.
DR PRO; PR:Q21217; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00001794; Expressed in larva and 4 other tissues.
DR ExpressionAtlas; Q21217; baseline and differential.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; HDA:WormBase.
DR GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IBA:GO_Central.
DR GO; GO:0042135; P:neurotransmitter catabolic process; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Aminotransferase; Mitochondrion; Neurotransmitter degradation;
KW Pyridoxal phosphate; Reference proteome; Transferase; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000250"
FT CHAIN ?..483
FT /note="Probable 4-aminobutyrate aminotransferase,
FT mitochondrial"
FT /id="PRO_0000001254"
FT BINDING 148..149
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 204
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 365
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 341
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P80147"
SQ SEQUENCE 483 AA; 53055 MW; 669965D22A0C4FB0 CRC64;
MLPRLAKSSL IQQVRGVSAI ANAEPSGPSI STSIPGPKSK ALKQEMDKVH QTTSVRFHVD
YEKSFGNYVV DADGNALLDV YTQISSLPLG YNHPDLVKVA SQPHLITSLV SRPALGSFPR
TDFADGISHA LTSIAPKGLK AVQTMLCGTS ANENAIKTAF IWYQAQRRGG LGPDALHLES
CMNQQKPGTP NLSVMGFEGA FHGRSLCMLS VTRSKPIHKV DIPAFDWPIA KFPRYKYPLD
QNVAYNKKQD QECLADVEAK ISEWKRRDND VAAIIVEPIQ AEGGDHYGSP AFFQGLRDIT
SKHGIVFIVD EVQTGGGATG DIWAHDHWNL SSPPDMVTFS KKLLTGGYFY GEHLRVKEAY
RIYNTWMGDP TKLLLLEKAV EVIKRDGLIE QSREVGAEFQ KRLGELQASS GGKLDQARGR
GTFAAVDFPS GSLRDKFVDL AISNGLHCGG CGDRSLRFRP SLVYTKKHLD LTFDLLDKTL
KGL
