TRI5_TRIAR
ID TRI5_TRIAR Reviewed; 388 AA.
AC G0LES5;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Trichodiene synthase {ECO:0000303|PubMed:21642405};
DE EC=4.2.3.6 {ECO:0000269|PubMed:21642405};
DE AltName: Full=Sesquiterpene cyclase TRI5 {ECO:0000303|PubMed:21642405};
DE Short=TS {ECO:0000305};
DE AltName: Full=Trichothecene biosynthesis protein 5 {ECO:0000303|PubMed:21642405};
GN Name=TRI5 {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, CATALYTIC
RP ACTIVITY, 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 DISRUPTION PHENOTYPE.
RX PubMed=24889745; DOI=10.1111/1462-2920.12514;
RA Malmierca M.G., Barua J., McCormick S.P., Izquierdo-Bueno I., Cardoza R.E.,
RA Alexander N.J., Hermosa R., Collado I.G., Monte E., Gutierrez S.;
RT "Novel aspinolide production by Trichoderma arundinaceum with a potential
RT role in Botrytis cinerea antagonistic activity and plant defence priming.";
RL Environ. Microbiol. 17:1103-1118(2015).
RN [3]
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: Trichodiene synthase; part of the gene cluster that mediates
CC the production of the antimicrobial trichothecene harzianum A (HA) that
CC plays a role in Botrytis cinerea antagonistic activity and plant
CC defense priming (PubMed:21642405, PubMed:24889745). The biosynthesis of
CC 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:0000269|PubMed:24889745, ECO:0000305|PubMed:21642405,
CC ECO:0000305|PubMed:30121242}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + trichodiene;
CC Xref=Rhea:RHEA:12052, ChEBI:CHEBI:15861, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.6;
CC Evidence={ECO:0000269|PubMed:21642405};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P13513};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:P13513};
CC Note=Some of the cofactor binding sites show unusual localization
CC within the protein. {ECO:0000305};
CC -!- PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis.
CC {ECO:0000269|PubMed:21642405}.
CC -!- INDUCTION: Expression is positively regulated by the cluster-specific
CC transcription factor TRI6. {ECO:0000269|PubMed:30121242}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of harzianum A and leads
CC to the production of a larger quantity of the aspinolides B and C.
CC {ECO:0000269|PubMed:24889745}.
CC -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC inhibiting protein biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the trichodiene synthase family. {ECO:0000305}.
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DR EMBL; FR715494; CBX36793.1; -; Genomic_DNA.
DR AlphaFoldDB; G0LES5; -.
DR SMR; G0LES5; -.
DR BioCyc; MetaCyc:MON-19544; -.
DR UniPathway; UPA00267; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045482; F:trichodiene synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0016106; P:sesquiterpenoid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR010458; TRI5_ascomyc.
DR InterPro; IPR024652; Trichodiene_synth.
DR Pfam; PF06330; TRI5; 1.
DR PIRSF; PIRSF001388; TRI5; 1.
DR SFLD; SFLDG01021; Trichodiene_Synthase_Like; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..388
FT /note="Trichodiene synthase"
FT /id="PRO_0000445610"
FT REGION 109..113
FT /note="Aspartate-rich domain"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 109
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 173
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 234
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P13513"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P13513"
SQ SEQUENCE 388 AA; 44946 MW; B2FAF74B7473A607 CRC64;
MVELNDVPGE EEFPRATYLE TMVRLLDTVS YNDENFTDEE RVECLKYAYG KAAEHFAQPH
VQETLKVPPK RMAAALKTIV GMCVYSWCRV SKEVMADLSI HYTYTLLLDD SREEPAGTMA
TWYEDLLNAR PQAHGWWRLV NDFIPNVLRH YGGYCQMNMV RSTIDFFQGC WIEQHNFKGF
RGSSDYPGFL RRINGLGHCV GSSIWPIELV DEEEHFLEIT TAIAQMENWM VWTNDLFSFY
KEYFAERDQT SLVNNYVECE GITLDQALDK LCKDTIRSSE EIIQVFHDKD PKMYEILTRF
IQGYITWHLC DDRYRLVEVY EAAGDDPVAQ KFKKYAESAR RVGAIDPARY CVPSVTELCE
REMAKQSAGR SWDFGLGKIA NKISSVAQ
