ID   TRI5_FUSAC              Reviewed;         375 AA.
AC   Q7LJR6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 48.
DE   RecName: Full=Trichodiene synthase;
DE            EC=4.2.3.6;
DE   AltName: Full=Sesquiterpene cyclase;
DE            Short=TS;
GN   Name=TRI5;
OS   Fusarium acaciae-mearnsii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=282272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 110253 / MRC 2458 / NRRL 26752,
RC   CBS 110254 / MRC 5120 / NRRL 26754, and CBS 110255 / MRC 5122 / NRRL 26755;
RX   PubMed=12080147; DOI=10.1073/pnas.142307199;
RA   Ward T.J., Bielawski J.P., Kistler H.C., Sullivan E., O'Donnell K.;
RT   "Ancestral polymorphism and adaptive evolution in the trichothecene
RT   mycotoxin gene cluster of phytopathogenic Fusarium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:9278-9283(2002).
CC   -!- FUNCTION: TS is a member of the terpene cyclase group of enzymes. It
CC       catalyzes the isomerization and cyclization of farnesyl pyro-phosphate
CC       to form trichodiene, the first cyclic intermediate in the biosynthetic
CC       pathway for trichothecenes. It serves to branch trichothecene
CC       biosynthesis from the isoprenoid pathway.
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   -!- PATHWAY: Sesquiterpene biosynthesis; trichothecene biosynthesis.
CC   -!- MISCELLANEOUS: Trichothecenes are sesquiterpenoid toxins that act by
CC       inhibiting protein biosynthesis.
CC   -!- SIMILARITY: Belongs to the trichodiene synthase family. {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; AY102576; AAM48822.1; -; Genomic_DNA.
DR   EMBL; AY102577; AAM48830.1; -; Genomic_DNA.
DR   EMBL; AY102578; AAM48838.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7LJR6; -.
DR   SMR; Q7LJR6; -.
DR   UniPathway; UPA00267; -.
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   3: Inferred from homology;
KW   Lyase.
FT   CHAIN           1..375
FT                   /note="Trichodiene synthase"
FT                   /id="PRO_0000221573"
SQ   SEQUENCE   375 AA;  43952 MW;  2E05031E6BC860FF CRC64;
     MENFPTEYFL NTSVRLLEYI RYRDSNYTRE ERIENLHYAY NKAAHHFAQP RQQKMLKVDP
     KRLQASLQTI VGMVVYSWAK VSKECMADLS IHYTYTLVLD DSSDDPHPAM LNYFDDLQAG
     REQAHPWWAL VNEHFPNVLR HFGPFCSLNL IRSTMDFFEG CWIEQYNFGG FPGSDDYPQF
     LRRMNGLGHC VGASLWPKDL FDERKHFLEI TSAVAQMENW MVWVNDLMSF YKEFDDERDQ
     ISLVKNFVTC HEITLDEALE KLTQETLHSS KQMVAVFSDK DPQVMDTIEC FMHGYVTWHL
     CDARYRLHEI YEKVKDQDTE DAKKFCKFFE QAANVGAVAP SEWAYPQVAQ LANVRAKDDV
     KEAHKPILSS IELVE