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
//