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Database: UniProt
Entry: T0LM54_COLGC
LinkDB: T0LM54_COLGC
Original site: T0LM54_COLGC 
ID   T0LM54_COLGC            Unreviewed;       250 AA.
AC   T0LM54;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Branched-chain amino acid aminotransferase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CGLO_07555 {ECO:0000313|EMBL:EQB52781.1};
OS   Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS   (Glomerella cingulata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum gloeosporioides species complex.
OX   NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB52781.1, ECO:0000313|Proteomes:UP000015530};
RN   [1] {ECO:0000313|Proteomes:UP000015530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX   PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA   Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA   Thon M., Fluhr R., Prusky D.;
RT   "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT   gloeosporioides as revealed by transcriptome analysis.";
RL   Mol. Plant Microbe Interact. 26:1345-1358(2013).
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:EQB52781.1}.
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DR   EMBL; AMYD01001514; EQB52781.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0LM54; -.
DR   STRING; 1237896.T0LM54; -.
DR   HOGENOM; CLU_031922_1_1_1; -.
DR   OMA; AEYVCPH; -.
DR   OrthoDB; 1854640at2759; -.
DR   Proteomes; UP000015530; 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   SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000015530}.
SQ   SEQUENCE   250 AA;  27303 MW;  147089175AA3A7EC CRC64;
     MPEVPEDIFL EAVHLAVRKN AEYVCPHDVK GSLYIRPFQI GSSAQIGLDP PEEFLFCVFV
     QPHIAFHGHG AIKALVLDDF DRAATRGSGA VKVGGNYAPV MRWTSEARKE GYNVLLHLDS
     QTQTEIDEFS TSGFIGIRRN GGETSLVIAD SKAAIESITA DSAAKVADSL GWRVEKRTVK
     FDELSNFTEV LAAGTAAGLV SVSCVHRKST NETFNFVPEG PAYEELWGVL KSIQNGTAMD
     SFGWRHSLQE
//
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