ID   IDTS_CLAPA              Reviewed;         259 AA.
AC   J7FIP9;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 7.
DE   RecName: Full=Indole-diterpene biosynthesis cluster protein S {ECO:0000303|PubMed:23468653};
GN   Name=idtS {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, 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.
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: Part of the gene cluster that mediates the biosynthesis of
CC       paspalitrems, indole-diterpene (IDT) mycotoxins that are potent
CC       tremorgens in mammals (PubMed:23468653, PubMed:29457197,
CC       PubMed:32077051). The geranylgeranyl diphosphate (GGPP) synthase idtG
CC       is proposed to catalyze the first step in IDT biosynthesis via
CC       catalysis of a series of iterative condensations of isopentenyl
CC       diphosphate (IPP) with dimethylallyl diphosphate (DMAPP), geranyl
CC       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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the ltmS family. {ECO:0000305}.
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DR   EMBL; JN613321; AFO85423.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7FIP9; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE   3: Inferred from homology;
KW   Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..259
FT                   /note="Indole-diterpene biosynthesis cluster protein S"
FT                   /id="PRO_0000451438"
FT   TRANSMEM        5..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        221..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   259 AA;  28679 MW;  87A70FF035729B0E CRC64;
     MSRTEASGWG FSLLQILLVL AGMVWKAREG FPIVDFLDTS GDTCSWLNPC IVPPALSCWN
     NWPWFALHLF LYTTQLVGLS AIILPPVYLI RMLGLSTALP LISLWVLHRR RRTGKGWATT
     FPPRHGEEAF LWRVLWFTGL AHVASFLVAT AASFLGREDM APWHLTNTLL GTPDCSYLPC
     SQIAERQARL RQINEMTGTS SGFFLAVALF SQHLEMNGAR LGAGLLARLF FVSLIAGPAA
     GAADALLLRS AFMRTRRST