PAXC_PENPX
ID PAXC_PENPX Reviewed; 317 AA.
AC Q9C448;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Prenyl transferase paxC {ECO:0000303|PubMed:11169115};
DE EC=2.5.1.- {ECO:0000305};
DE AltName: Full=Paxilline synthesis protein C {ECO:0000303|PubMed:11169115};
GN Name=paxC {ECO:0000303|PubMed:11169115};
OS Penicillium paxilli.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=70109;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=PN2013;
RX PubMed=11169115; DOI=10.1046/j.1365-2958.2001.02265.x;
RA Young C., McMillan L., Telfer E., Scott B.;
RT "Molecular cloning and genetic analysis of an indole-diterpene gene cluster
RT from Penicillium paxilli.";
RL Mol. Microbiol. 39:754-764(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=PN2013;
RX PubMed=23949005; DOI=10.3390/toxins5081422;
RA Scott B., Young C.A., Saikia S., McMillan L.K., Monahan B.J., Koulman A.,
RA Astin J., Eaton C.J., Bryant A., Wrenn R.E., Finch S.C., Tapper B.A.,
RA Parker E.J., Jameson G.B.;
RT "Deletion and gene expression analyses define the paxilline biosynthetic
RT gene cluster in Penicillium paxilli.";
RL Toxins 5:1422-1446(2013).
RN [3]
RP FUNCTION.
RX PubMed=16494875; DOI=10.1016/j.febslet.2006.02.008;
RA Saikia S., Parker E.J., Koulman A., Scott B.;
RT "Four gene products are required for the fungal synthesis of the indole-
RT diterpene, paspaline.";
RL FEBS Lett. 580:1625-1630(2006).
CC -!- FUNCTION: Prenyl transferase; part of the gene cluster that mediates
CC the biosynthesis of paxalline, a mycotoxin that acts as an inhibitor of
CC mammalian maxi-K channels (PubMed:11169115, PubMed:23949005,
CC PubMed:16494875). PaxG, the geranylgeranyl diphosphate (GGPP) synthase
CC is proposed to catalyze the first step in paxilline biosynthesis
CC (PubMed:23949005 PubMed:16494875). Condensation of indole-3-glycerol
CC phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI),
CC followed by epoxidation and cyclization of this intermediate (by paxM
CC and paxB) to form paspaline (PubMed:23949005, PubMed:16494875).
CC Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the
CC latter being then converted to paxilline by paxQ (PubMed:23949005).
CC Finally paxilline can be mono- and di-prenylated by paxD
CC (PubMed:23949005). {ECO:0000269|PubMed:11169115,
CC ECO:0000269|PubMed:16494875, ECO:0000269|PubMed:23949005}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000269|PubMed:16494875, ECO:0000305|PubMed:11169115,
CC ECO:0000305|PubMed:23949005}.
CC -!- DISRUPTION PHENOTYPE: Impairs the production of paxilline
CC (PubMed:23949005). {ECO:0000269|PubMed:23949005}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; HM171111; AAK11529.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9C448; -.
DR SMR; Q9C448; -.
DR BioCyc; MetaCyc:MON-18635; -.
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 Magnesium; Metal-binding; Transferase.
FT CHAIN 1..317
FT /note="Prenyl transferase paxC"
FT /id="PRO_0000436117"
FT BINDING 53
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 93
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 102
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 187
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 216
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 223
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 233
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
SQ SEQUENCE 317 AA; 35924 MW; 48D54AC8093D9710 CRC64;
MGVAGSGVLY FLFNNVPSPR FWLKKTQLIG TENPEGITGY ECPYEYLRKS YGKHHWAAFV
DKLSPNLQNE DPAKYRMVLE TMDVIHLCLM MVDDISDGSE YRKGKPAAHK IYGAPETANR
AYYRVTQILA QTATEFPRLS PWLMTDLRDI LEGQDMSLVW RRDGVNGFPG TASERTAAYK
RMVLLKTGGL FRLLGHLTLE NNSMDEAFST LGWHSQLQND CKNVYSSEYA KMKGVVAEDL
LNREMTYPIV LALDASGGHW VEAALKSPSR RNVGNALKII QCDYVRDVCM AELARSGAPV
KEWLKLWKRE EKLDLKA
