ID   PTMC_PENSI              Reviewed;         342 AA.
AC   A0A140JWT3;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   11-MAY-2016, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Prenyl transferase ptmC {ECO:0000303|PubMed:25831977};
DE            EC=2.5.1.- {ECO:0000269|PubMed:25831977};
DE   AltName: Full=Penitrem biosynthesis cluster 1 protein C {ECO:0000303|PubMed:25831977};
GN   Name=ptmC {ECO:0000303|PubMed:25831977};
OS   Penicillium simplicissimum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=69488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=AK-40;
RX   PubMed=25831977; DOI=10.1002/anie.201501072;
RA   Liu C., Tagami K., Minami A., Matsumoto T., Frisvad J.C., Suzuki H.,
RA   Ishikawa J., Gomi K., Oikawa H.;
RT   "Reconstitution of biosynthetic machinery for the synthesis of the highly
RT   elaborated indole diterpene penitrem.";
RL   Angew. Chem. Int. Ed. 54:5748-5752(2015).
CC   -!- FUNCTION: Prenyl transferase; part of the gene cluster that mediates
CC       the biosynthesis of the indole diterpenes penitrems (PubMed:25831977).
CC       The geranylgeranyl diphosphate (GGPP) synthase ptmG catalyzes the first
CC       step in penitrem biosynthesis via conversion of farnesyl pyrophosphate
CC       and isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC       (PubMed:25831977). Condensation of indole-3-glycerol phosphate with
CC       GGPP by the prenyl transferase ptmC then forms 3-geranylgeranylindole
CC       (3-GGI) (PubMed:25831977). Epoxidation by the FAD-dependent
CC       monooxygenase ptmM leads to a epoxidized-GGI that is substrate of the
CC       terpene cyclase ptmB for cyclization to yield paspaline
CC       (PubMed:25831977). Paspaline is subsequently converted to 13-
CC       desoxypaxilline by the cytochrome P450 monooxygenase ptmP, the latter
CC       being then converted to paxilline by the cytochrome P450 monooxygenase
CC       ptmQ (PubMed:25831977). Paxilline is converted to beta-paxitriol via C-
CC       10 ketoreduction by the short-chain dehydrogenase ptmH which can be
CC       monoprenylated at the C-20 by the indole diterpene prenyltransferase
CC       ptmD (PubMed:25831977). A two-step elimination (acetylation and
CC       elimination) process performed by the O-acetyltransferase ptmV and ptmI
CC       leads to the production of the prenylated form of penijanthine
CC       (PubMed:25831977). 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 ptmE
CC       (PubMed:25831977). Five sequential oxidative transformations performed
CC       by the cytochrome P450 monooxygenases ptmK, ptmU, ptmL, ptmN and ptmJ
CC       yield the various penitrem compounds. PtmK, ptmU and ptmM are involved
CC       in the formation of the key bicyclic ring of penitrem C via the
CC       formation of the intermediates secopenitrem D and penitrem D. PtmL
CC       catalyzes the epoxidation of penitrem D and C to yield penitrem B and
CC       F, respectively. PtmJ catalyzes the last benzylic hydroxylation to
CC       convert penitrem B to prenitrem E and penitrem F to penitrem A
CC       (PubMed:25831977). {ECO:0000269|PubMed:25831977}.
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:25831977}.
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; LC027936; BAU61560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A140JWT3; -.
DR   SMR; A0A140JWT3; -.
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 ptmC"
FT                   /id="PRO_0000446550"
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   BINDING         211
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         240
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         247
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         257
FT                   /ligand="dimethylallyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:57623"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   SITE            146
FT                   /note="Important for determining product chain length"
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;  38790 MW;  C16539C08F427D0E CRC64;
     MTTMLTTPLS GWSQLSLSFL TLTVGALALI VVLYISIDRF PAPRWLSKKY QLIGQKDPAS
     TTSLECPYSY IRQIYGHYHW APFVHKLSPT LQYDDPAKYK MVLEIMDAIH LCLMLVDDIS
     DGSDFRKGRP AAHRIYGPSE TANRAYLRVT QILNQTTSGF PHLAPWLMRD LENILEGQDL
     SLVWRRDGLK NFPTAPLERA AAYQRMASLK TGSLFRLLGH LVLEDRSMDD TMTLVAWYSQ
     LQNDCKNVYS TEYAKMKGAI AEDLSNGELS YPIVLAMNAP DGHWVDLALQ SPSPWNVRNA
     LRVIRSDKVH QMCMAEMAES SSSIQDWLAL WGRKEKLDLK SV