ID   IDTF_CLAPA              Reviewed;         427 AA.
AC   J7FK08;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=Indole diterpene prenyltransferase idtF {ECO:0000303|PubMed:23468653};
DE            EC=2.5.1.- {ECO:0000305|PubMed:32077051};
DE   AltName: Full=Indole-diterpene biosynthesis cluster protein F {ECO:0000303|PubMed:23468653};
GN   Name=idtF {ECO:0000303|PubMed:23468653};
OS   Claviceps paspali (Rye ergot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Claviceps.
OX   NCBI_TaxID=40601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, AND FUNCTION.
RC   STRAIN=RRC-1481;
RX   PubMed=23468653; DOI=10.1371/journal.pgen.1003323;
RA   Schardl C.L., Young C.A., Hesse U., Amyotte S.G., Andreeva K., Calie P.J.,
RA   Fleetwood D.J., Haws D.C., Moore N., Oeser B., Panaccione D.G.,
RA   Schweri K.K., Voisey C.R., Farman M.L., Jaromczyk J.W., Roe B.A.,
RA   O'Sullivan D.M., Scott B., Tudzynski P., An Z., Arnaoudova E.G.,
RA   Bullock C.T., Charlton N.D., Chen L., Cox M., Dinkins R.D., Florea S.,
RA   Glenn A.E., Gordon A., Gueldener U., Harris D.R., Hollin W., Jaromczyk J.,
RA   Johnson R.D., Khan A.K., Leistner E., Leuchtmann A., Li C., Liu J., Liu J.,
RA   Liu M., Mace W., Machado C., Nagabhyru P., Pan J., Schmid J., Sugawara K.,
RA   Steiner U., Takach J.E., Tanaka E., Webb J.S., Wilson E.V., Wiseman J.L.,
RA   Yoshida R., Zeng Z.;
RT   "Plant-symbiotic fungi as chemical engineers: Multi-genome analysis of the
RT   Clavicipitaceae reveals dynamics of alkaloid loci.";
RL   PLoS Genet. 9:E1003323-E1003323(2013).
RN   [2]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=29457197; DOI=10.1007/s00253-018-8807-x;
RA   Kozak L., Szilagyi Z., Vago B., Kakuk A., Toth L., Molnar I., Pocsi I.;
RT   "Inactivation of the indole-diterpene biosynthetic gene cluster of
RT   Claviceps paspali by Agrobacterium-mediated gene replacement.";
RL   Appl. Microbiol. Biotechnol. 102:3255-3266(2018).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=32077051; DOI=10.1007/s12223-020-00777-6;
RA   Kozak L., Szilagyi Z., Toth L., Pocsi I., Molnar I.;
RT   "Functional characterization of the idtF and idtP genes in the Claviceps
RT   paspali indole diterpene biosynthetic gene cluster.";
RL   Folia Microbiol. (Praha) 65:605-613(2020).
CC   -!- FUNCTION: Indole diterpene prenyltransferase; part of the gene cluster
CC       that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT)
CC       mycotoxins that are potent tremorgens in mammals (PubMed:23468653,
CC       PubMed:29457197, PubMed:32077051). The geranylgeranyl diphosphate
CC       (GGPP) synthase idtG is proposed to catalyze the first step in IDT
CC       biosynthesis via catalysis of a series of iterative condensations of
CC       isopentenyl diphosphate (IPP) with dimethylallyl diphosphate (DMAPP),
CC       geranyl diphosphate (GPP), and farnesyl diphosphate (FPP), to form GGPP
CC       (Probable). Condensation of indole-3-glycerol phosphate with GGPP by
CC       the prenyltransferase idtC then forms 3-geranylgeranylindole (3-GGI)
CC       (Probable). Epoxidation of the two terminal alkenes of the
CC       geranylgeranyl moiety by the FAD-dependent monooxygenase idtM, and
CC       cyclization by the terpene cyclase idtB then leads to the production of
CC       paspaline (Probable). The cytochrome P450 monooxygenase idtP then
CC       catalyzes oxidative elimination of the pendant methyl group at C-12 of
CC       paspaline and generates the C-10 ketone to yield 13-desoxypaxilline
CC       (PubMed:32077051). The cytochrome P450 monooxygenase idtQ may catalyze
CC       the C-13 oxidation of 13-desoxypaxilline to afford paxilline
CC       (Probable). Considering that both paspalicine and paxilline were
CC       detected in C.paspali, idtQ also catalyzes the formation of paspalinine
CC       from 13-desoxypaxilline via paspalicine as an intermediate (Probable).
CC       Finally, the alpha-prenyltransferase idtF prenylates paspalinine at the
CC       C-20 or the C-21 positions to yield paspalitrems A and C, respectively
CC       (PubMed:32077051). The hydroxylation of paspalitrem A at C-32 by a
CC       still unknown oxidase affords paspalitrem B (Probable).
CC       {ECO:0000269|PubMed:23468653, ECO:0000269|PubMed:29457197,
CC       ECO:0000269|PubMed:32077051, ECO:0000305|PubMed:29457197}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:29457197, ECO:0000269|PubMed:32077051}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of all prenylated
CC       paspalitrems, but accumulates paspalinine and small quantities of
CC       paspaline (PubMed:32077051). Simultaneous disruption of idtB, idtC,
CC       idtF and idtG eliminates the biosynthesis of the whole spectrum of
CC       indole-diterpenes reported to be produced by C.paspali, including
CC       paspaline, paxilline, paspalinine, paspalitrem A and paspalitrem B
CC       (PubMed:29457197). {ECO:0000269|PubMed:29457197,
CC       ECO:0000269|PubMed:32077051}.
CC   -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; JN613321; AFO85419.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7FK08; -.
DR   SMR; J7FK08; -.
DR   GO; GO:0004659; F:prenyltransferase activity; IEA:UniProt.
DR   GO; GO:0009820; P:alkaloid metabolic process; IEA:InterPro.
DR   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR   CDD; cd13929; PT-DMATS_CymD; 1.
DR   InterPro; IPR033964; Aro_prenylTrfase.
DR   InterPro; IPR017795; Aro_prenylTrfase_DMATS.
DR   PANTHER; PTHR40627; PTHR40627; 1.
DR   Pfam; PF11991; Trp_DMAT; 1.
DR   SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1.
DR   TIGRFAMs; TIGR03429; arom_pren_DMATS; 1.
PE   3: Inferred from homology;
KW   Transferase.
FT   CHAIN           1..427
FT                   /note="Indole diterpene prenyltransferase idtF"
FT                   /id="PRO_0000451435"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         264
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         266
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         268
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
FT   BINDING         352
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q50EL0"
SQ   SEQUENCE   427 AA;  48316 MW;  73E927445A97749B CRC64;
     MESDKNGPAR QENDIAEKES DIRYWTRVVC PSVRSLLHAA GSYTAEDIEA QMRTLREVVL
     PDLGPRPSRA PGPSYLFQGG CPFQLSINTT SKANAVRYVW EVLGERGHTS DDPLAMQTTR
     DTVSRLSAKF GLSTKWSDVL LSALELTTKE AQKAVEKMPE WILEHLEKGA VVPRIKNLPF
     GFVAFDLKES DVSIKLYITL KAREIFTGKS AADVIFDSLR NFTPAFKPEA IDMIQNFLSG
     LSEKMPLEVI AIDCVDEAHL SEARVKLYCH STSNSFNTVK KWLTIGGKVK DENTLKGLQI
     LRSMWHLFIQ KPEGIPDDEL ETPVNLENAL KHRMYFSFEL KPGQDIPQVK TYLPIWRYAP
     SDEQAIDNFE AAFRQCHHPW GEDGTYGRIF RNALCAPPIH GDLAYIYCEK RGVYQTIYVT
     PPLLEED