ID A0A2S6CJF0_9PEZI Unreviewed; 382 AA.
AC A0A2S6CJF0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 08-NOV-2023, entry version 15.
DE RecName: Full=Branched-chain-amino-acid aminotransferase {ECO:0008006|Google:ProtNLM};
GN ORFNames=CBER1_04933 {ECO:0000313|EMBL:PPJ59855.1};
OS Cercospora berteroae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=357750 {ECO:0000313|EMBL:PPJ59855.1, ECO:0000313|Proteomes:UP000237631};
RN [1] {ECO:0000313|Proteomes:UP000237631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS538.71 {ECO:0000313|Proteomes:UP000237631};
RA de Jonge R., Ebert M.K., Huitt-Roehl C.R., Pal P., Suttle J.C.,
RA Spanner R.E., Neubauer J.D., Jurick W.M.II., Stott K.A., Secor G.A.,
RA Thomma B.P.H.J., Van de Peer Y., Townsend C.A., Bolton M.D.;
RT "Conservation of a gene cluster reveals novel cercosporin biosynthetic
RT mechanisms and extends production to the genus Colletotrichum.";
RL bioRxiv 0:0-0(2017).
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:PPJ59855.1}.
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DR EMBL; PNEN01000346; PPJ59855.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6CJF0; -.
DR STRING; 357750.A0A2S6CJF0; -.
DR OrthoDB; 1304at2759; -.
DR Proteomes; UP000237631; 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 Reference proteome {ECO:0000313|Proteomes:UP000237631}.
FT REGION 359..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 193
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR006468-1"
SQ SEQUENCE 382 AA; 41521 MW; 054A97E0CBCE5437 CRC64;
MASSFPPPPV NTIDWDDIGF KVREVNGHIE STYSVKTGEW TAPQFVQDPF LRLHGMAPGL
NYGMQCYEGL KASRGPDDKT IGIFRPQANA ERMQHSASFV SMPDVPVELF KKSVHLAVSL
NAAYVPPHRT GASMYIRPLL FGSSAQLGLD PPEEYTFLVF VMPTGVYHGV HPVACLILED
FDRAAPEGTG SAKIGGNYAP VLRHSGKAKK EGFGITLHLD SRTRTEVDEF STSGFIGIHG
NPEEGCTIVV PDSKNVIKSV TSNTICEIAK SWGWKVEQRP IKYNEIGTFT EIAAAGTAAA
LVPIKSITMR SKNDTFKYQG GGDEPGPAVV KLLAQLKGIQ QGKIKDEFGW VEQVREYEPE
EYAHDGAGQS NGVNGATPNE LP
//
