ID   TRI5_STACH              Reviewed;         383 AA.
AC   O59947;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Trichodiene synthase;
DE            EC=4.2.3.6;
DE   AltName: Full=Sesquiterpene cyclase;
DE            Short=TS;
GN   Name=TRI5;
OS   Stachybotrys chartarum (Toxic black mold) (Stilbospora chartarum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Stachybotryaceae; Stachybotrys.
OX   NCBI_TaxID=74722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Straus N.A., Wong B.;
RL   Submitted (MAR-1998) 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; AF053926; AAC12640.1; -; Genomic_DNA.
DR   AlphaFoldDB; O59947; -.
DR   SMR; O59947; -.
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..383
FT                   /note="Trichodiene synthase"
FT                   /id="PRO_0000221588"
SQ   SEQUENCE   383 AA;  44988 MW;  F311F4326FE82EDC CRC64;
     MEAFPTEYFL GTAVRLLENV KYRDSNYTRE ERVENLQYAY NKAAAHFAQE RQQQILKVSP
     KRLEASLRTI VGMVVYSWAK VSKELMADLS IHYTYTLILD DSEDDPHPQM LTYFDDLQSG
     NPQKHPWWML VNEHFPNVLR HFGPFCSLNL IRSTLDFFEG CWIEQYNFHG FPGSFDYPGF
     LRRMNGLGHC VGGSLWPKEN FNEQEHFLEI TSAIAQMENW MVWVNDLMSF YKEFDDPRDQ
     TSLVKNYVVS EGITLNQALE KLTQDTLQSS EQMMVVFSQK DPKIMDTIEC FMHGYITWHL
     CDNRYRLKEI YDRTKDIQTE DAMKFRKFYE QAFKVGAIEA TEWAYPTVVE RLEQRKAEEQ
     AERDEQAALA NPEKAQVAQV VLA