ID A0A0V0VD30_9BILA Unreviewed; 492 AA.
AC A0A0V0VD30;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-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=T09_6237 {ECO:0000313|EMBL:KRX61417.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX61417.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX61417.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX61417.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRX61417.1}.
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DR EMBL; JYDN01000048; KRX61417.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0VD30; -.
DR STRING; 181606.A0A0V0VD30; -.
DR Proteomes; UP000054681; 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 Aminotransferase {ECO:0000313|EMBL:KRX61417.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transferase {ECO:0000313|EMBL:KRX61417.1}.
FT REGION 179..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 492 AA; 55009 MW; 31E4EEAC83EBAC6B CRC64;
MTILLPTAVH RWPLLFSCFR RKLCLAKPLL AGEPEGPVVT TAIPGPNSLR LKNELSEIQN
SDAVQFFVDY TKSIGNYIAD VDGNMLLDVY SQIASIPIGY NHPDLIEAVE STNMRSMFIN
RPALGVYPPK DHVQSLRSSL LVVAPPGMKN VATMMCGSCS NENAFKTAFI WYRTKQRGGK
EPTADDMRSS MQNQPPGSPQ LSVLSFQGGF HGRTLACLSC THSKAIHKVD MPALDWPVAS
FPRYKYPLDE HADYNRNEDQ QCLAEVQQLM EVYKQRGRDV AAVLVEPIQA EGGDNFASKE
FFTDLQKLTK QAGAAFIVDE VQTGCGATGR MWAHEHWDLP ESPDLVTFSK KMYLGGFYFK
PEFYVKQGYR IFNTWLGDPS KLALLDVTLR VIRRDNLLQN TQIAGRTLLA GLQALEEKFP
ALVHSARGLG TFCAITCRDV ATRDNILTRM RQRGINMGGC GEASIRFRPM LTFQTCHAEI
ILERLNAVLK EF
//
