ID   TRI3_TRIAR              Reviewed;         520 AA.
AC   G0KYB1;
DT   07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT   19-OCT-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=Trichothecene O-acetyltransferase TRI3 {ECO:0000303|PubMed:21642405};
DE            EC=2.3.2.- {ECO:0000305|PubMed:21642405};
DE   AltName: Full=Trichothecene biosynthesis cluster protein 3 {ECO:0000303|PubMed:21642405};
GN   Name=TRI3 {ECO:0000303|PubMed:21642405};
OS   Trichoderma arundinaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=490622;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=IBT 40837;
RX   PubMed=21642405; DOI=10.1128/aem.00595-11;
RA   Cardoza R.E., Malmierca M.G., Hermosa M.R., Alexander N.J., McCormick S.P.,
RA   Proctor R.H., Tijerino A.M., Rumbero A., Monte E., Gutierrez S.;
RT   "Identification of loci and functional characterization of trichothecene
RT   biosynthesis genes in filamentous fungi of the genus Trichoderma.";
RL   Appl. Environ. Microbiol. 77:4867-4877(2011).
RN   [2]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=30121242; DOI=10.1016/j.fgb.2018.08.002;
RA   Lindo L., McCormick S.P., Cardoza R.E., Brown D.W., Kim H.S.,
RA   Alexander N.J., Proctor R.H., Gutierrez S.;
RT   "Effect of deletion of a trichothecene toxin regulatory gene on the
RT   secondary metabolism transcriptome of the saprotrophic fungus Trichoderma
RT   arundinaceum.";
RL   Fungal Genet. Biol. 119:29-46(2018).
CC   -!- FUNCTION: Trichothecene O-acetyltransferase; part of the gene cluster
CC       that mediates the production of the antimicrobial trichothecene
CC       harzianum A (HA) that plays a role in Botrytis cinerea antagonistic
CC       activity and plant defense priming (PubMed:21642405). The biosynthesis
CC       of harzianum A begins with the cyclization of farnesyl diphosphate to
CC       trichodiene and is catalyzed by the trichodiene synthase TRI5
CC       (PubMed:21642405). Trichodiene undergoes a series of oxygenations
CC       catalyzed by the cytochrome P450 monooxygenase TRI4. TRI4 controls the
CC       addition of 3 oxygens at C-2, C-11, and the C-12, C-13-epoxide to form
CC       the intermediate isotrichodiol (PubMed:21642405). Isotrichodiol then
CC       undergoes a non-enzymatic isomerization and cyclization to form 12,13-
CC       epoxytrichothec-9-ene (EPT) which is further converted to trichodermol
CC       by the cytochrome P450 monooxygenase TRI11 via C-4 hydroxylation
CC       (PubMed:21642405). The last step of HA synthesis is esterification of
CC       an octatriendioyl moiety to the C-4 oxygen of trichodermol. The
CC       octatriendioyl moiety is probably produced by the polyketide synthase
CC       TRI17 and the esterification performed by the trichothecene O-
CC       acetyltransferase TRI3 (Probable). {ECO:0000269|PubMed:21642405,
CC       ECO:0000305|PubMed:21642405, ECO:0000305|PubMed:30121242}.
CC   -!- PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis.
CC       {ECO:0000305|PubMed:21642405}.
CC   -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC       transcription factor TRI6. {ECO:0000269|PubMed:30121242}.
CC   -!- SIMILARITY: Belongs to the trichothecene O-acetyltransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FN394495; CAY87361.1; -; Genomic_DNA.
DR   AlphaFoldDB; G0KYB1; -.
DR   SMR; G0KYB1; -.
DR   BioCyc; MetaCyc:MON-19549; -.
DR   UniPathway; UPA00267; -.
DR   GO; GO:0016407; F:acetyltransferase activity; IEA:InterPro.
DR   GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:InterPro.
DR   Gene3D; 3.30.559.10; -; 1.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR009992; Tri3/Sat12/Sat16/Mac1.
DR   Pfam; PF07428; Tri3; 1.
PE   2: Evidence at transcript level;
KW   Transferase.
FT   CHAIN           1..520
FT                   /note="Trichothecene O-acetyltransferase TRI3"
FT                   /id="PRO_0000445608"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  58638 MW;  8EFCB575ABA45B25 CRC64;
     MGSKLPELPK LSPEKHRWEK SNVDPRVLQR RGIGSEAIVG MERSNRRGQY DLYLLATLRT
     AHVSTSTPLS LLYLKEKLEL ALLVMRFEHP ECACTVTWDD QVPPIIQYAS PQNDEEALMW
     AKSSVHIRTT SQTGFDVRYE IEGKRQDLDQ DNMEPSRPIV IYLISNVTNG DAQLTSGATV
     DVLLHMNHLF WDGISARMFT GDLFRELNKL INSNEQELPK LQWGTEASNL SAPVLDALKI
     NIEELREEFE AASNQFVKAL YENYGGWGLE FKSGLGLPRT DIHTSTATES KAIINGVKTR
     LGPQYTISHL AQAAVVIAML EIIQPPNLTD KDIFVSPMPV NGRRWLKDGL ADHHYSICET
     GAVIRIENIK SLVLNNNNDK GYRPRCDEKK PGEDVKKSFD QWLGNPYQLA LGLAVHTLEA
     SFLTANPMPF DKVAAPFFIS DGRNEQFIPA SITTTTGEIL MTIDNFVFFL NQCLPYLAIR
     LESWKDASTL SVCYNKANYS QEEATKFLKC VAKYMLIFSQ