ID   TRI5_FUSCU              Reviewed;         375 AA.
AC   Q8NIG9; Q7Z8C2;
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 culmorum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=5516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=CBS 110269 / FRC R-5321 / MRC 1787 / NRRL 3288, and
RC   CBS 417.86 / FRC R-8504 / IMI 309344 / NRRL 25475;
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IBT2303;
RA   Eriksson A.R.B., Schnurer J.;
RT   "Trichodiene synthase (Tri5) targeted PCR for identification of Fusarium
RT   culmorum, F. graminearum, F. poae and F. sporotrichioides.";
RL   Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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; AY102571; AAM48782.1; -; Genomic_DNA.
DR   EMBL; AY102602; AAM49030.1; -; Genomic_DNA.
DR   EMBL; AY130291; AAN05033.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8NIG9; -.
DR   SMR; Q8NIG9; -.
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_0000221579"
FT   VARIANT         165
FT                   /note="Q -> H (in strain: IBT2303)"
SQ   SEQUENCE   375 AA;  43966 MW;  4EF324FD72440C26 CRC64;
     MENFPTEYFL NTSVRLLEYI RYRDSNYTRE ERIENLHYAY NKAAHHFAQP RQQQMLKVDP
     KRLQASLQTI VGMVVYSWAK VSKECMADLS IHYTYTLVLD DSSDDPHPAM LNYFDDLQAG
     REQSHPWWAL VNEHFPNVLR HFGPFCSLNL IRSTMDFFEG CWIEQYNFGG FPGSDDYPQF
     LRRMNGLGHC VGASLWPKDL FDERKNFLEI TTAVAQMENW MVWVNDLMSF YKEFDDERDQ
     ISLVKNFVTC HEITLDEALE KLTQETLHSS KQMVAVFADK DPQVMDTIEC FMHGYVTWHL
     CDARYRLHEI YEKVKDQDTE DAKKFCKFFE QAANVGAVAP SEWAYPQVAQ LANVRAKDDM
     KEAQKPILSS IELVE