ID A0A0R3QYE5_9BILA Unreviewed; 496 AA.
AC A0A0R3QYE5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=(S)-3-amino-2-methylpropionate transaminase {ECO:0000256|ARBA:ARBA00030857};
DE EC=2.6.1.19 {ECO:0000256|ARBA:ARBA00012912};
DE EC=2.6.1.22 {ECO:0000256|ARBA:ARBA00012876};
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 ORFNames=BTMF_LOCUS10781 {ECO:0000313|EMBL:VDO36778.1};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001276901-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0001276901-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDO36778.1, ECO:0000313|Proteomes:UP000280834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
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; UZAG01017816; VDO36778.1; -; Genomic_DNA.
DR STRING; 42155.A0A0R3QYE5; -.
DR WBParaSite; BTMF_0001276901-mRNA-1; BTMF_0001276901-mRNA-1; BTMF_0001276901.
DR Proteomes; UP000050602; Unplaced.
DR Proteomes; UP000280834; Unassembled WGS sequence.
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; 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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000280834}.
SQ SEQUENCE 496 AA; 55000 MW; D7D429320FD2FF5D CRC64;
MKTILCPLIF SRAGGNFNLF SAKWIRYMQT ATTVLGEPPR PKICGTFPGP KSKRMQVEMD
LQHQAASVKC FIDYEKSKGN YIVDADENVL LDVYMQISSL ALGYNHPDLV KAVSDPRFVT
TAVSRPALGS FPPTFFVDAM KNSLSSIAPK GCPGVQNVLC GTSSNENAIK AAFMWYQAQK
RGGSPPTKDD LDSCMKHELP GTPNLSVLSF DGSFHGRSLT ALSITHSKAI HKVDLPAFQW
PVAEFPRYKY PLEKNVSYNE QQDQKCLANV EELIKKWKET KHDIAAVIVE PIQGEGGDNH
GSPAFFQGLR DITAKHGVVF IVDEVQTGGG GTGTFWAHDS WNLSSPPDIV VFAKKLMVAG
YFYANHLQMK EPYRIYNTWL GDPTKVILLE KALKVIERDN LLEQMRKVGA TMQSELRKIE
SANNSMVQNV RGLGTFCAFD MPDRVVRDKF LEIAGNNGLL IGGCGKATVR FRPALIFTDK
HLEITLDIIT KSLSEL
//
