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Database: UniProt
Entry: A0A074S6E7_9AGAM
LinkDB: A0A074S6E7_9AGAM
Original site: A0A074S6E7_9AGAM 
ID   A0A074S6E7_9AGAM        Unreviewed;       436 AA.
AC   A0A074S6E7;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Branched-chain-amino-acid aminotransferase {ECO:0000313|EMBL:KEP55011.1};
GN   ORFNames=V565_010020 {ECO:0000313|EMBL:KEP55011.1};
OS   Rhizoctonia solani 123E.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=1423351 {ECO:0000313|EMBL:KEP55011.1, ECO:0000313|Proteomes:UP000027456};
RN   [1] {ECO:0000313|EMBL:KEP55011.1, ECO:0000313|Proteomes:UP000027456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=123E {ECO:0000313|EMBL:KEP55011.1,
RC   ECO:0000313|Proteomes:UP000027456};
RA   Cubeta M., Pakala S., Fedorova N., Thomas E., Dean R., Jabaji S., Neate S.,
RA   Toda T., Tavantzis S., Vilgalys R., Bharathan N., Pakala S., Losada L.S.,
RA   Zafar N., Nierman W.;
RL   Submitted (DEC-2013) 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}.
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:KEP55011.1}.
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DR   EMBL; AZST01000013; KEP55011.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A074S6E7; -.
DR   STRING; 1423351.A0A074S6E7; -.
DR   HOGENOM; CLU_031922_0_1_1; -.
DR   OrthoDB; 1304at2759; -.
DR   Proteomes; UP000027456; Unassembled WGS sequence.
DR   GO; GO:0004084; F:branched-chain-amino-acid transaminase activity; IEA:InterPro.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009081; P:branched-chain amino acid metabolic process; IEA:InterPro.
DR   CDD; cd01557; BCAT_beta_family; 1.
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   InterPro; IPR033939; BCAT_family.
DR   NCBIfam; TIGR01123; ilvE_II; 1.
DR   PANTHER; PTHR11825:SF44; 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   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW   ECO:0000313|EMBL:KEP55011.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027456};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KEP55011.1}.
FT   MOD_RES         246
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ   SEQUENCE   436 AA;  47357 MW;  7D30F53853F5AE9E CRC64;
     MASFLRATLR SQLKVGTKNS YSQTCRLFST SQSRLRIDIM TGEPTALPDI ESSQLKIHKN
     PNPKNPPKSS SLVFGHTFTD HMISIPWNAL SGWNTPTIIP YGPLSLDPSC TVLHYAQTVF
     EGMKAYRDEN NKVTMFRPDM NMKRMNRSAA RISLPTFNGD EMLEIIKTLV KLDSHWIPQE
     PGHSLYIRPT MIGTQRALGV APPTEALLFV ICSPVGPYYK NGFKPVRLLA TSNFIRAAPG
     GTGGYKLGAN YAPGVVPQVL AAKQGYDQNL WLIGDEHYLT EVGTMNLLVV FKHPDGTTEL
     TTPPLEDLIL PGVTRDSILA LARDHESGKA RIPGLPDNLK VSERHVKMAE VKAAAESGNL
     LEAFGAGTAA IVCPVKAIGY QGKDINIPVG DEGMGPVCKA ILDQIVARQM GTVESDWSVV
     VTEGTKGSLK GPNPVA
//
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