ID   J5J6B5_BEAB2            Unreviewed;       389 AA.
AC   J5J6B5;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   08-NOV-2023, entry version 33.
DE   SubName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000313|EMBL:EJP62068.1};
GN   ORFNames=BBA_08992 {ECO:0000313|EMBL:EJP62068.1};
OS   Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS   (Tritirachium shiotae).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX   NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP62068.1, ECO:0000313|Proteomes:UP000002762};
RN   [1] {ECO:0000313|EMBL:EJP62068.1, ECO:0000313|Proteomes:UP000002762}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP62068.1,
RC   ECO:0000313|Proteomes:UP000002762};
RX   PubMed=22761991; DOI=10.1038/srep00483;
RA   Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA   St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT   "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT   Beauveria bassiana.";
RL   Sci. Rep. 2:483-483(2012).
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; JH725192; EJP62068.1; -; Genomic_DNA.
DR   RefSeq; XP_008602311.1; XM_008604089.1.
DR   AlphaFoldDB; J5J6B5; -.
DR   STRING; 655819.J5J6B5; -.
DR   GeneID; 19892004; -.
DR   HOGENOM; CLU_031922_0_0_1; -.
DR   InParanoid; J5J6B5; -.
DR   OrthoDB; 1304at2759; -.
DR   Proteomes; UP000002762; 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; PTHR11825:SF69; BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11825; SUBGROUP IIII AMINOTRANSFERASE; 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:EJP62068.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW   Transferase {ECO:0000313|EMBL:EJP62068.1}.
FT   MOD_RES         218
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   389 AA;  43367 MW;  D256986DB0E35842 CRC64;
     MVVTSTLSRL DASKLQVLQL SNPKSVPGPD DGSIFDLKTT TDRMITVSWT AQNGWANPQL
     VPYGPLSLMP TASAIQYATE CFEGMKLFRG HDGRLRLFRP LYNCQRMLRS AERISLPSFE
     PEEMLKLIRR LCLMEAPKWL PKDRIGSALY IRPTMIGTDS SLGFKVPEEA QLCIFMLYWP
     SPSMIPDKSL PVSRRGMRLV TSSKTAIRSW PGGTGQAKIG GNYGPTLLEH NKARARGYDQ
     VLWLYGPDRR ITEAGSTNFF VLWKTPTGDE GLILAGNTRQ TILELFETSF ETLEPNSLEP
     CNVLEKRITM PEIESAVAQG RVLSAFVVGT AAWIQEVEEI NVDGRQLRIN VGQAPHVSFV
     REKLAGIMLG QVENGWAEVV DEEANFGDE
//