TRI5_PARRD
ID TRI5_PARRD Reviewed; 385 AA.
AC O13489;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 73.
DE RecName: Full=Trichodiene synthase;
DE EC=4.2.3.6;
DE AltName: Full=Sesquiterpene cyclase;
DE Short=TS;
GN Name=TRI5;
OS Paramyrothecium roridum (Myrothecium leaf spot fungus) (Myrothecium
OS roridum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Stachybotryaceae; Paramyrothecium.
OX NCBI_TaxID=1859971;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 52485 / TX 1;
RX PubMed=9529523; DOI=10.1007/s004380050666;
RA Trapp S.C., Hohn T.M., McCormick S., Jarvis B.B.;
RT "Characterization of the gene cluster for biosynthesis of macrocyclic
RT trichothecenes in Myrothecium roridum.";
RL Mol. Gen. Genet. 257:421-432(1998).
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; AF009416; AAC49957.1; -; Genomic_DNA.
DR AlphaFoldDB; O13489; -.
DR SMR; O13489; -.
DR PRIDE; O13489; -.
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..385
FT /note="Trichodiene synthase"
FT /id="PRO_0000221587"
SQ SEQUENCE 385 AA; 44869 MW; 25A492729D5B0D66 CRC64;
MDEFPTEYFL GTAVRLLENV KYRDSNYTRE ERIENLSYAN NKAAAHFAQE RQQRILKVNP
KRLEASLRTI VGMVVYSWVK VSKELMADLS IHYTYTLILD DSEDDPHNNM LTFFDDLQAG
REQKHPWWML VNEHFPNVLR HFGPFCSLNL IRSTLDFFEG CWIEQYNFHG FPGSYDFPGF
LRRMNGLGHC VGGSLWPKEL FDEQKHFLEI TSAVAQMENW MVWVNDLMSF YKEFDDPRDQ
TSLVKNYVVC DEISLTQALE KLTVDTLTSS EQMMEVFSDK DAKLMETIEC FMHGYITWHL
CDHRYRLKEV YEGTMHIETE DAIKFRKFYG QAAKVGAIEH EEWAFPTVAE RIEVRLAEEK
AAKDGQAVLT SAEPAVPQAA QEVLA