ID   OLCH_PENCN              Reviewed;         330 AA.
AC   P9WEQ7;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   29-SEP-2021, sequence version 1.
DT   03-AUG-2022, entry version 4.
DE   RecName: Full=Polyprenyl transferase olcH {ECO:0000303|PubMed:30090271};
DE            EC=2.5.1.- {ECO:0000269|PubMed:30090271};
DE   AltName: Full=15-deoxyoxalicine B biosynthesis cluster protein H {ECO:0000303|PubMed:30090271};
GN   Name=olcH {ECO:0000303|PubMed:30090271};
OS   Penicillium canescens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5083;
RN   [1]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX   PubMed=30090271; DOI=10.1039/c5sc01965f;
RA   Yaegashi J., Romsdahl J., Chiang Y.M., Wang C.C.C.;
RT   "Genome mining and molecular characterization of the biosynthetic gene
RT   cluster of a diterpenic meroterpenoid, 15-deoxyoxalicine B, in Penicillium
RT   canescens.";
RL   Chem. Sci. 6:6537-6544(2015).
RN   [2]
RP   ERRATUM OF PUBMED:30090271.
RX   PubMed=30123464; DOI=10.1039/c6sc90012g;
RA   Yaegashi J., Romsdahl J., Chiang Y.M., Wang C.C.C.;
RT   "Correction: Genome mining and molecular characterization of the
RT   biosynthetic gene cluster of a diterpenic meroterpenoid, 15-deoxyoxalicine
RT   B, in Penicillium canescens.";
RL   Chem. Sci. 7:2440-2440(2016).
CC   -!- FUNCTION: Polyprenyl transferase; part of the gene cluster that
CC       mediates the biosynthesis of 15-deoxyoxalicine B (PubMed:30090271). The
CC       first step of the pathway is the synthesis of nicotinyl-CoA from
CC       nicotinic acid by the nicotinic acid-CoA ligase olcI (PubMed:30090271).
CC       Nicotinyl-CoA is then a substrate of polyketide synthase olcA to
CC       produce 4-hydroxy-6-(3-pyridinyl)-2H-pyran-2-one (HPPO) which is
CC       further prenylated by the polyprenyl transferase olcH to yield
CC       geranylgeranyl-HPPO (PubMed:30090271). Geranylgeranyl pyrophosphate is
CC       provided by the cluster-specific geranylgeranyl pyrophosphate synthase
CC       olcC (PubMed:30090271). The FAD-dependent monooxygenase olcE catalyzes
CC       the epoxidation of geranylgeranyl-HPPO and the terpene cyclase olcD
CC       catalyzes the cyclization of the terpenoid component, resulting in the
CC       formation of the tricyclic terpene moiety seen in predecaturin E
CC       (PubMed:30090271). The cytochrome P450 monooxygenase then catalyzes the
CC       allylic oxidation of predecaturin E, which is followed by
CC       spirocylization with concomitant loss of one molecule of water to form
CC       decaturin E (PubMed:30090271). Decaturin E is the substrate of the
CC       cytochrome P450 monooxygenase olcJ which hydroxylates it at the C-29
CC       position to form decaturin F (PubMed:30090271). The short-chain
CC       dehydrogenase/reductase olcF may catalyze the oxidation of decaturin F
CC       to generate the 29-hydroxyl-27-one intermediate, and subsequent
CC       hemiacetal formation probably leads to the formation of decaturin C
CC       (Probable). The dioxygenase olcK may be a peroxisomal enzyme that
CC       catalyzes the hydroxylation of decaturin C into decaturin A once
CC       decaturin C is shuttled into the peroxisome by the MFS transporter olcL
CC       (Probable). Finally the cytochrome P450 monooxygenase olcB catalyzes
CC       the oxidative rearrangement to yield 15-deoxyoxalicine B
CC       (PubMed:30090271). In the absence of olcJ, decaturin E may be shunted
CC       to a pathway in which it is oxidized to a ketone, possibly by olcF, to
CC       form decaturin D, which undergoes further allylic oxidation to yield
CC       decaturin G (PubMed:30090271). Moreover, in the absence of oclK or
CC       oclL, oclB can convert decaturin C into 15-deoxyoxalicine A
CC       (PubMed:30090271). {ECO:0000269|PubMed:30090271,
CC       ECO:0000305|PubMed:30090271}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P32378};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000269|PubMed:30090271}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Abolishes the production of 15-deoxyoxalicine B.
CC       {ECO:0000269|PubMed:30090271}.
CC   -!- MISCELLANEOUS: The 15-deoxyoxalicine B cluster is a rare cluster that
CC       contains its own geranylgeranyl pyrophosphate synthase (olcC), in
CC       contrast to other related clusters which rely on a FPP/GGPP synthase
CC       localized outside of the cluster. {ECO:0000269|PubMed:30090271}.
CC   -!- SIMILARITY: Belongs to the UbiA prenyltransferase family.
CC       {ECO:0000305}.
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DR   SMR; P9WEQ7; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd13959; PT_UbiA_COQ2; 1.
DR   Gene3D; 1.10.357.140; -; 1.
DR   InterPro; IPR039653; Prenyltransferase.
DR   InterPro; IPR000537; UbiA_prenyltransferase.
DR   InterPro; IPR030470; UbiA_prenylTrfase_CS.
DR   InterPro; IPR044878; UbiA_sf.
DR   PANTHER; PTHR11048; PTHR11048; 1.
DR   Pfam; PF01040; UbiA; 1.
DR   PROSITE; PS00943; UBIA; 1.
PE   3: Inferred from homology;
KW   Membrane; Transferase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..330
FT                   /note="Polyprenyl transferase olcH"
FT                   /id="PRO_0000453893"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        116..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        142..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        308..328
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   330 AA;  37469 MW;  7525B1AEE0B21E2D CRC64;
     MVTKCIDPCE QQNQKRPVGH LVWDLIRISR YDKYNSFLAL FSGVWSTLLA GALKLRNEPE
     STSVSFVLSR VVLCSLASYI FSGAGMVWND WVDRDIDAKV ARTKDRPLAS GRLHTMEAMA
     WLIIQVAAST GLLYWMMEGR HVWISLVPPA IGTLLYPYCK RPTAQKFGIY PQYVLGLTAA
     CPAVFGRAAI YNHEDSFQDL INASFPLCLF VFVWTLYFNT AYSYQDVKDD SKMKINSSYV
     FAGQHIHLFL VLLTGLVLAS IPWVLHPLQS GWLWVSWMGV WSVGCAEQLV RFNANDPHTG
     GLVWRRNILL ALWTIFACLV EVLLVWIHQI