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Database: UniProt
Entry: A0A2H3HUE6_FUSOX
LinkDB: A0A2H3HUE6_FUSOX
Original site: A0A2H3HUE6_FUSOX 
ID   A0A2H3HUE6_FUSOX        Unreviewed;       532 AA.
AC   A0A2H3HUE6;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   RecName: Full=Aminotransferase class I/classII domain-containing protein {ECO:0000259|Pfam:PF00155};
GN   ORFNames=AU210_002166 {ECO:0000313|EMBL:PCD43064.1};
OS   Fusarium oxysporum f. sp. radicis-cucumerinum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=327505 {ECO:0000313|EMBL:PCD43064.1, ECO:0000313|Proteomes:UP000219602};
RN   [1] {ECO:0000313|EMBL:PCD43064.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD43064.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=27387256; DOI=10.1111/1462-2920.13445;
RA   van Dam P., Fokkens L., Schmidt S.M., Linmans J.H., Kistler H.C., Ma L.J.,
RA   Rep M.;
RT   "Effector profiles distinguish formae speciales of Fusarium oxysporum.";
RL   Environ. Microbiol. 18:4087-4102(2016).
RN   [2] {ECO:0000313|EMBL:PCD43064.1, ECO:0000313|Proteomes:UP000219602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Forc016 {ECO:0000313|EMBL:PCD43064.1,
RC   ECO:0000313|Proteomes:UP000219602};
RX   PubMed=28831051; DOI=10.1038/s41598-017-07995-y;
RA   van Dam P., Fokkens L., Ayukawa Y., van der Gragt M., Ter Horst A.,
RA   Brankovics B., Houterman P.M., Arie T., Rep M.;
RT   "A mobile pathogenicity chromosome in Fusarium oxysporum for infection of
RT   multiple cucurbit species.";
RL   Sci. Rep. 7:9042-9042(2017).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:PCD43064.1}.
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DR   EMBL; MABQ02000002; PCD43064.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3HUE6; -.
DR   STRING; 327505.A0A2H3HUE6; -.
DR   OrthoDB; 5486605at2759; -.
DR   Proteomes; UP000219602; Chromosome 2.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProt.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   CDD; cd00609; AAT_like; 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; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   PANTHER; PTHR42790; AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR42790:SF21; AROMATIC_AMINOADIPATE AMINOTRANSFERASE 1; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000219602}.
FT   DOMAIN          151..520
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   532 AA;  59649 MW;  D16810E2DAD6EA0A CRC64;
     MGHSTATALG SPGGSHVKIE LMRERRATAT KIRLGIAAMS DSDMFKLPAD GKPLARKWGT
     HFSSESKRPP CILKQAAGYI KTPGLISLGG GLPSSEYFPI SEIAIRVPTA PNFSEKQHLL
     DSPASGAQIA HIGKYDTRDG TSDYDISIAF NYGQATGSPQ MMRWITEHVD LVYNPPYADW
     AVCQTVGSTG ALEQTVRMLC DQFRDDSILT EDYTFATAME TFIPQGIKVF GINMDEQGLV
     PNHMDHVLET WDEAARGARK PHLLYTVPSG QNPTGATQSL ERRREIYRVC QKHNIFIIED
     EPYYFIQMKP YTGRGTEVVA NETVDEFLTS LVPSYLSLDV DGRVLRMDSF SKVLVPGSRM
     GWITASKQVI QRYLCHAEVA NQGPSGISQL IIWKLVDETW GHEGYLKWLI DLRTNYTRRR
     NALLAACEDY LPTDIASWVP PAAGMFLWVK LDHTKHPDYL RRSLDEIEGE IFQHSIDQGV
     LFARGSWFRA EPQKELNELF LRVTFASAAE EDMCTAVQRL SAAIKKSFRI EV
//
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