IDTC_CLAPA
ID IDTC_CLAPA Reviewed; 367 AA.
AC J7FJH2;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Prenyltransferase idtC {ECO:0000303|PubMed:23468653};
DE EC=2.5.1.- {ECO:0000305|PubMed:29457197};
DE AltName: Full=Indole-diterpene biosynthesis cluster protein C {ECO:0000303|PubMed:23468653};
DE Flags: Precursor;
GN Name=idtC {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: Prenyltransferase; 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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q12051};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q12051};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:29457197}.
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 FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; JN613321; AFO85422.1; -; Genomic_DNA.
DR AlphaFoldDB; J7FJH2; -.
DR SMR; J7FJH2; -.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Magnesium; Metal-binding; Signal; Transferase.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..367
FT /note="Prenyltransferase idtC"
FT /id="PRO_0000451433"
FT REGION 32..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 139
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 143
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 264
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT CARBOHYD 67
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 367 AA; 40020 MW; 42DBFDD614893041 CRC64;
MTTLAWFAGR SMVLDLAALT SAFTVGYLLK STSTPTSTPT STDKAGTPPG STIHHYGYPQ
GSVTKPNNSK TEKENGSPKD SKGNVPDCPY KYLVGLYGHH HFAGFVEALQ PTLKDEDPEK
YTLVLDIMDA VHLCLILVDD ICDDSPKRKN QTTAHLLFGS CETANRAYLV LTKVINRAMR
TRPVLGAELV RALELILEGQ DLSLVWRRDG LAAFDAEEGG DKVSVYKKMA QLKTGTLFVL
LGRLLNDGGA QLDDVLLRLG WYSQLQNDCK NIYSGEYANN KGAIAEDLRN GEMSFPVVVA
LGDQTTSSQI RKAFGSHSDG DIFDALDALQ SSCIKNKCSQ ALQEAGRGLE NLLAIWGRRE
HMDSLGS
