OLCD_PENCN
ID OLCD_PENCN Reviewed; 241 AA.
AC P9WEQ3;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 29-SEP-2021, sequence version 1.
DT 23-FEB-2022, entry version 2.
DE RecName: Full=Terpene cyclase olcD {ECO:0000303|PubMed:30090271};
DE EC=4.2.3.- {ECO:0000269|PubMed:30090271};
DE AltName: Full=15-deoxyoxalicine B biosynthesis cluster protein D {ECO:0000303|PubMed:30090271};
GN Name=olcD {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: Terpene cyclase; part of the gene cluster that mediates the
CC biosynthesis of 15-deoxyoxalicine B (PubMed:30090271). The first step
CC of the pathway is the synthesis of nicotinyl-CoA from nicotinic acid by
CC the nicotinic acid-CoA ligase olcI (PubMed:30090271). Nicotinyl-CoA is
CC then a substrate of polyketide synthase olcA to produce 4-hydroxy-6-(3-
CC pyridinyl)-2H-pyran-2-one (HPPO) which is further prenylated by the
CC polyprenyl transferase olcH to yield geranylgeranyl-HPPO
CC (PubMed:30090271). Geranylgeranyl pyrophosphate is provided by the
CC cluster-specific geranylgeranyl pyrophosphate synthase olcC
CC (PubMed:30090271). The FAD-dependent monooxygenase olcE catalyzes the
CC 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 -!- 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 paxB family. {ECO:0000305}.
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DR UniPathway; UPA00213; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR039020; PaxB-like.
DR PANTHER; PTHR42038; PTHR42038; 1.
PE 3: Inferred from homology;
KW Lyase; Membrane; Transmembrane; Transmembrane helix.
FT CHAIN 1..241
FT /note="Terpene cyclase olcD"
FT /id="PRO_0000453890"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..71
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 76..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..222
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 241 AA; 27028 MW; 2E260BEF4AEE0D81 CRC64;
MESLDFTKAP PEFQEVKYLS DILLVTLASG WLVCYFATIR TAFCDRACWM PLLPLSCNVA
WELVFITLYP PPGSPILGFW LLVNLGVIYS ALRFAPSKAS HLAVEKHYLP VLFVLAVGFW
AWGHLALIEQ LNPLPAFYYG GMACQLMTSA AALSGLVDQG STQGASYTIW LSRVIGTSSA
LAGLFFRAHY WPSLWAWADN ELMRWLAAAF GILDGVYGVQ FWRLRRSENQ LTIDHAHRKT
E
