ID   TRI5_FUSPS              Reviewed;         375 AA.
AC   Q8NID7; Q8NJC8;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Trichodiene synthase;
DE            EC=4.2.3.6;
DE   AltName: Full=Sesquiterpene cyclase;
DE            Short=TS;
GN   Name=TRI5;
OS   Fusarium pseudograminearum (Wheat and barley crown-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=101028;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 109949 / FRC R-5291 / MAFF 237835 / NRRL 28334,
RC   CBS 109953 / FRC R-6215 / MAFF 237846 / NRRL 28338,
RC   CBS 109954 / FRC R-6761 / MAFF 237837 / NRRL 28065, and
RC   CBS 109956 / FGSC 9095 / FRC R-5291 / MAFF 237835 / NRRL 28062;
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}.
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DR   EMBL; AY102580; AAM48854.1; -; Genomic_DNA.
DR   EMBL; AY102582; AAM48870.1; -; Genomic_DNA.
DR   EMBL; AY102583; AAM48878.1; -; Genomic_DNA.
DR   EMBL; AY102585; AAM48894.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NID7; -.
DR   SMR; Q8NID7; -.
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_0000221583"
FT   VARIANT         279
FT                   /note="N -> D (in strain: NRRL 28065)"
SQ   SEQUENCE   375 AA;  43837 MW;  B38F7DD5BC57246D CRC64;
     MENFPTEYFL NTSVRLLEYI RYRDSNYTRE ERIENLHYAY NKAAHHFAQP RQQQLLKVDP
     KRLQASLQTI VGMVVYSWAK VSKECMADLS IHYTYTLVLD DSSDDPYPAM LNYFGDLQAG
     REQAHPWWAL VNEHFPNVLR HFGPFCSLNL IRSTMDFFEG CWIEQYNFGG FPGSDDYPQF
     LRRMNGLGHC VGASLWPKDL FDERKHFLEI TSAVAQMENW MVWVNDLMSF YKEFDDERDQ
     ISLVKNFVTC HEITLDEALE KLTQETLHSS KQMVAVFSNK DPQVMDTIEC FMHGYVTWHL
     CDARYRLHEI YEKVKDQDTE DAKKFCKFFE QAANVGAVAP SEWAYPPVAQ LANVRAKGDV
     KEAQKPFLSS IELVE