ID   A0A0R3QWU0_9BILA        Unreviewed;       425 AA.
AC   A0A0R3QWU0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Aminotran_1_2 domain-containing protein {ECO:0000313|WBParaSite:BTMF_0001220601-mRNA-1};
GN   ORFNames=BTMF_LOCUS10226 {ECO:0000313|EMBL:VDO34728.1};
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_0001220601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0001220601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO34728.1, 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-II pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00008392}.
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DR   EMBL; UZAG01017444; VDO34728.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3QWU0; -.
DR   STRING; 42155.A0A0R3QWU0; -.
DR   WBParaSite; BTMF_0001220601-mRNA-1; BTMF_0001220601-mRNA-1; BTMF_0001220601.
DR   Proteomes; UP000050602; Unplaced.
DR   Proteomes; UP000280834; Unassembled WGS sequence.
DR   GO; GO:0008890; F:glycine C-acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006567; P:threonine catabolic process; IEA:InterPro.
DR   CDD; cd06454; KBL_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   HAMAP; MF_00985; 2am3keto_CoA_ligase; 1.
DR   InterPro; IPR011282; 2am3keto_CoA_ligase.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR01822; 2am3keto_CoA; 1.
DR   PANTHER; PTHR13693:SF102; 2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR13693; CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280834};
KW   Transferase {ECO:0000256|ARBA:ARBA00023315}.
FT   DOMAIN          69..414
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   425 AA;  47326 MW;  8897AB2A8F8A0A47 CRC64;
     MAAQQILFNR IRLFHFSLNQ SYSTARQQFI DLLNKELSTI QDAGTYKNER VIVGRQGMKI
     KIMNYNMPLL NFCANNYLGL SSHPEVIKAG QEAIDTHGAG MSSVRFICGT QDIHRTLEQK
     LAKFHDREDA ILYAACFDAN GGLFEVLTSK QYNDEDAVIS DELNHASIID GIRLCKAKRY
     RYRHVDLNDL EQILKETQNR RRRIIATDGV FSMDGDVAPL KEICDLADRF NALVFVDDCH
     ATGFFGPTGR GTEEHLGVQG RIDIINSTLG KALGGTMGGY TTGPKPFIDL LRQRSRPYLF
     SNSLAPSIVG SSIKVLDLLT NSSEFTNSLK SNVSHFRKSL TDAGFNVMGN SDHPICPVFL
     GDARLASTFA DEMLKKGIYV IGFSYPVVPK DKARIRVQIS AAHTKQQIDQ CISAFKTIGK
     KLNVI
//