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IDTB_CLAPA
ID   IDTB_CLAPA              Reviewed;         239 AA.
AC   J7FIJ6;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2012, sequence version 1.
DT   25-MAY-2022, entry version 10.
DE   RecName: Full=Terpene cyclase idtB {ECO:0000303|PubMed:23468653};
DE            EC=4.2.3.- {ECO:0000305|PubMed:29457197};
DE   AltName: Full=Indole-diterpene biosynthesis cluster protein B {ECO:0000303|PubMed:23468653};
GN   Name=idtB {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.
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: Terpene cyclase; part of the gene cluster that mediates the
CC       biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that
CC       are potent 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   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:29457197}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Simultaneous disruption of idtB, idtC, idtF and
CC       idtG eliminates the biosynthesis of the whole spectrum of indole-
CC       diterpenes reported to be produced by C.paspali, including paspaline,
CC       paxilline, paspalinine, paspalitrem A and paspalitrem B.
CC       {ECO:0000269|PubMed:29457197}.
CC   -!- SIMILARITY: Belongs to the paxB family. {ECO:0000305}.
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DR   EMBL; JN613321; AFO85421.1; -; Genomic_DNA.
DR   AlphaFoldDB; J7FIJ6; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR039020; PaxB-like.
DR   PANTHER; PTHR42038; PTHR42038; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Lyase; Membrane; Transmembrane; Transmembrane helix.
FT   CHAIN           1..239
FT                   /note="Terpene cyclase idtB"
FT                   /id="PRO_0000451432"
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        75..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        113..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        138..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        164
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   239 AA;  26633 MW;  39330615C16D2A93 CRC64;
     MDGFSILHEP PAAYKEVKWM ADTFVAGMGL GWIVNYALMI RFSWKGRPHC MALLPLCNNI
     AWELTYTIVY PSANRVELLV FAIGLTLNFF IMVGARRSAR VEWRHSPLLS EHAGFILLVG
     TLLCFTGHVA LAMEIGPGLA YSWGAVVCQL ALSIGGLFQL LQRNSTAGTS WTLWSSRFLG
     SCCTVAFAGL RCKYWPEVFG WLASPLVLWS LVTFLLADSA YGFCLYRVSH AETKARKKH
 
 
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