PENC_PENCR
ID PENC_PENCR Reviewed; 342 AA.
AC A0A0E3D8N1;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 14.
DE RecName: Full=Prenyl transferase penC {ECO:0000303|PubMed:26213965};
DE EC=2.5.1.- {ECO:0000305|PubMed:26213965};
DE AltName: Full=Penitrem biosynthesis cluster protein C {ECO:0000303|PubMed:26213965};
GN Name=penC {ECO:0000303|PubMed:26213965};
OS Penicillium crustosum (Blue mold fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC STRAIN=PN2402;
RX PubMed=26213965; DOI=10.3390/toxins7082701;
RA Nicholson M.J., Eaton C.J., Starkel C., Tapper B.A., Cox M.P., Scott B.;
RT "Molecular cloning and functional analysis of gene clusters for the
RT biosynthesis of indole-diterpenes in Penicillium crustosum and P.
RT janthinellum.";
RL Toxins 7:2701-2722(2015).
CC -!- FUNCTION: Prenyl transferase; part of the gene cluster that mediates
CC the biosynthesis of the indole diterpenes penitrems (PubMed:26213965).
CC The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first
CC step in penitrem biosynthesis via conversion of farnesyl pyrophosphate
CC and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC (Probable). Condensation of indole-3-glycerol phosphate with GGPP by
CC the prenyl transferase penC then forms 3-geranylgeranylindole (3-GGI)
CC (Probable). Epoxidation by the FAD-dependent monooxygenase penM leads
CC to a epoxidized-GGI that is substrate of the terpene cyclase penB for
CC cyclization to yield paspaline (Probable). Paspaline is subsequently
CC converted to 13-desoxypaxilline by the cytochrome P450 monooxygenase
CC penP, the latter being then converted to paxilline by the cytochrome
CC P450 monooxygenase penQ (PubMed:26213965). Paxilline is converted to
CC beta-paxitriol via C-10 ketoreduction by the short-chain dehydrogenase
CC PC-15 which can be monoprenylated at the C-20 by the indole diterpene
CC prenyltransferase penD (Probable). A two-step elimination (acetylation
CC and elimination) process performed by the O-acetyltransferase PC-16 and
CC the P.simplicissimum ptmI-ortholog not yet identified in P.crustosum,
CC leads to the production of the prenylated form of penijanthine
CC (Probable). The FAD-linked oxidoreductase ptmO then converts the
CC prenylated form of penijanthine into PC-M5 which is in turn transformed
CC into PC-M4 by the aromatic dimethylallyltransferase PC-22 (Probable). A
CC series of oxidation steps involving 4 cytochrome P450 monooxygenases
CC (PC-21, PC-05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14)
CC are required for the transformation of PC-M4 to penitrems A and E.
CC Synthesis of these final products is proposed to proceed via penitrems
CC D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC-
CC 14, PC-23) (Probable). {ECO:0000269|PubMed:26213965,
CC ECO:0000305|PubMed:26213965}.
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26213965}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; KC963408; AGZ20189.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3D8N1; -.
DR SMR; A0A0E3D8N1; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; Membrane; Metal-binding; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..342
FT /note="Prenyl transferase penC"
FT /id="PRO_0000446549"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 110
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 121
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 126
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 210
FT /ligand="dimethylallyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:57623"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT CARBOHYD 154
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 342 AA; 38675 MW; EF3834AEC1DBFB3F CRC64;
MTTMLTTPLS GWSQLSLSYL TLTVGALALV VVLYISIDRF PAPRWLSKKY QLIGQKDPAS
TTSLECPYSY IRQIYGHHHW APFVHKLSPT LQHDDPAKYK MVLEIMDAIH LCLMLVDDIS
DGSDFRKGRP AAHRIYGPSE TANRAYFRVT QILNQTTTGF PHLAPWLMQD LENILEGQDL
SLVWRRDGLK NFPTAPSERA AAYQRMASLK TGSLFRLLGH LVLEDRSMDD TMTLVAWYSQ
LQNDCKNVYS TEYAKMKGAI AEDLCNGELS YPIVLAMNAP DGHWVELALQ SPSPRNVRNA
LRAIRSDNVH QMCMAELAES SSSIQDWLAL WGRKEKLDLK ST
