ID   IDTQ_CLAPA              Reviewed;         529 AA.
AC   J7FJH1;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Cytochrome P450 monooxygenase idtQ {ECO:0000303|PubMed:23468653};
DE            EC=1.-.-.- {ECO:0000305|PubMed:29457197};
DE   AltName: Full=Indole-diterpene biosynthesis cluster protein Q {ECO:0000303|PubMed:23468653};
GN   Name=idtQ {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: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:29457197}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; JN613321; AFO85417.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7FJH1; -.
DR   SMR; J7FJH1; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..529
FT                   /note="Cytochrome P450 monooxygenase idtQ"
FT                   /id="PRO_0000451437"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         469
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250|UniProtKB:P04798"
SQ   SEQUENCE   529 AA;  60321 MW;  FF80DDFC827B8CC5 CRC64;
     MLTEQFDPST FYSPKTVAIA GLILGCVLIY VYNDYPTNVN VPVIGVGVRY TKWLAAVRNV
     FYARDSVAEG YKKANFAFQI PTLNRMEIFI CDRKMTREYQ NLDSDRMSLD AVVVEEFEFD
     LLSPGHGHGH RRGPDSVPIP VVAKALAWQR RRTANTNDPF FQEFMAEVSY GFQQEVQRLS
     QDPRSSTTTP VFTVPCFSFA LQVVGRITTF ALFGRPMCRD RAFLDLCGKY SDGLPRGAML
     LRPWPKWMRP FIAKHMEAPQ VLAKLKEIIG AEIERRKASD GESPMENIMD YFVDWAYKGR
     DTVPADADDT VAHVLANLIF ASFHTTSQLL TDCLFEIAMR PEYVEPLREE IKDCFEKHGR
     ETRAVLDSLF KMDSFIKETH RWNPLDASAL ARIAMQDFTF SNGLHIPKGS FIFTPNAPIF
     QDERHYSNPK IFDGFRFAKM RDDPKLKLTC DLATVGEYSL NFGLGRHACP GRYLASDEVK
     LSLIHLLQNF DITVDPSELP LKRVRYGKFS LADMSAKVSL RRLRSEVKG