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Database: UniProt
Entry: T0JWZ7_COLGC
LinkDB: T0JWZ7_COLGC
Original site: T0JWZ7_COLGC 
ID   T0JWZ7_COLGC            Unreviewed;       429 AA.
AC   T0JWZ7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN   ORFNames=CGLO_13185 {ECO:0000313|EMBL:EQB47637.1};
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:EQB47637.1, 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   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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:EQB47637.1}.
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DR   EMBL; AMYD01002872; EQB47637.1; -; Genomic_DNA.
DR   AlphaFoldDB; T0JWZ7; -.
DR   STRING; 1237896.T0JWZ7; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   HOGENOM; CLU_017584_1_2_1; -.
DR   OMA; EYATGCN; -.
DR   OrthoDB; 1328656at2759; -.
DR   Proteomes; UP000015530; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   PANTHER; PTHR43795:SF63; PUTATIVE (AFU_ORTHOLOGUE AFUA_4G00630)-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015530}.
FT   DOMAIN          40..416
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   429 AA;  47473 MW;  45B45F099256E728 CRC64;
     MDHSLSNRGS EAAKPDDGML LWTIVQDLWD PTTNPTGYVS LGIAENSLMH ERLSEHIHKN
     LAVPMHSFTY GDGMTGSKRL KASLARFLTG HLKPVTAIQS EHVSVTNGCS SAIEHLVWAL
     GNPGDGFLLG QPHYGAFVPD VEYRTGCELV PVPFQDVDPL GAGAAQKYED ALLASRAKGV
     KIAALILCHP HNPLGRCYPR SLILDLMRLC QKYDMHLISD EIYALSVWNN AIDTQPPPVA
     FESCLSIDTT GVMDAHRLHV LWGMSKDFGA NGIRLGAIVS QHHPSFHRSL TPVGIYSSPS
     SISDHITANI LDDSEWVDGY IVENQKKLQE HYELVVAWAK QNGITYAQGA NAAFFLWIDL
     GKTYLERHPE RKVEDLSGEV MRALLSKKVF IASGKQFGSE KPGWFRIVFS NKKDLLLEGL
     KRIVEAIEE
//
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