ID   A0A3F3QDL6_9EURO        Unreviewed;       405 AA.
AC   A0A3F3QDL6;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   08-NOV-2023, entry version 12.
DE   SubName: Full=Branched-chain amino acid aminotransferase {ECO:0000313|EMBL:RDH37139.1};
GN   ORFNames=BDQ94DRAFT_183985 {ECO:0000313|EMBL:RDH37139.1};
OS   Aspergillus welwitschiae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=1341132 {ECO:0000313|EMBL:RDH37139.1, ECO:0000313|Proteomes:UP000253729};
RN   [1] {ECO:0000313|EMBL:RDH37139.1, ECO:0000313|Proteomes:UP000253729}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 139.54b {ECO:0000313|EMBL:RDH37139.1,
RC   ECO:0000313|Proteomes:UP000253729};
RG   DOE Joint Genome Institute;
RA   Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA   Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA   Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA   Mortensen U.H., Andersen M.R., Baker S.E.;
RT   "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT   speciation.";
RL   Submitted (JUL-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-IV pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00009320}.
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DR   EMBL; KZ852036; RDH37139.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3F3QDL6; -.
DR   STRING; 1341132.A0A3F3QDL6; -.
DR   OrthoDB; 1304at2759; -.
DR   Proteomes; UP000253729; Unassembled WGS sequence.
DR   GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro.
DR   GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.30.470.10; -; 1.
DR   Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR   InterPro; IPR001544; Aminotrans_IV.
DR   InterPro; IPR036038; Aminotransferase-like.
DR   InterPro; IPR005786; B_amino_transII.
DR   InterPro; IPR043132; BCAT-like_C.
DR   InterPro; IPR043131; BCAT-like_N.
DR   PANTHER; PTHR42825; AMINO ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42825:SF2; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE 3, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF01063; Aminotran_4; 1.
DR   PIRSF; PIRSF006468; BCAT1; 1.
DR   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:RDH37139.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000253729};
KW   Transferase {ECO:0000313|EMBL:RDH37139.1}.
FT   MOD_RES         215
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   405 AA;  43607 MW;  DD53FB3289DDFD46 CRC64;
     MTTPFPPPPT PSIDWTNIGF KVRDVNYHVE CTYTPQTHTW STPQLIKSPH LSIHGLSPAL
     NYGQQAYEGL KAFRHATTTT TTNDNSSRND KITIFRPTLN ATRLAHSSTI LSIPPIPTPT
     FLSAVNLAVA SNAEYVPPHH ITLTPTSGEK PGVSALYIRP LVFGSSPQIS LTPPETFTFA
     VFVTPTGLYH GISAVDALIL EEYDRTAPKG TGSAKAGGNY APVQRHSMAA YKEGYGITLH
     LDSKTRTEVD EFSTSAFIGV KYNNNGEGKV TLVQPDSVNV IDSVTAASVL EIGEKMLGYK
     VEKRSVKYEE IREFDEVIAA GTAAGLVPVR SITMKSKGDK WGFECGGDKG EGGPVCRKLL
     GLLQGIQTGE VEDVFGWNWV VREVEGVMGE GEGGGVGEEN AVNVP
//