OLCG_PENCN
ID OLCG_PENCN Reviewed; 493 AA.
AC P9WEQ6;
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=Cytochrome P450 monooxygenase olcG {ECO:0000303|PubMed:30090271};
DE EC=1.-.-.- {ECO:0000269|PubMed:30090271};
DE AltName: Full=15-deoxyoxalicine B biosynthesis cluster protein G {ECO:0000303|PubMed:30090271};
GN Name=olcG {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: Cytochrome P450 monooxygenase; 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=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:30090271}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Abolishes the production of 15-deoxyoxalicine B
CC and accumulates predecaturin E. {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 cytochrome P450 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:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.10.630.10; -; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..493
FT /note="Cytochrome P450 monooxygenase olcG"
FT /id="PRO_0000453887"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 429
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:P04798"
SQ SEQUENCE 493 AA; 56196 MW; DCB1FBBD748184C0 CRC64;
MLQGVIDTHQ ASLRGILATG ALVIFVALFL ATFQFQVLCL PLINGRKRFE LSLTNSKKRY
YADAKGFIQS GFSQSKNGFY AITENGRELI LAPKFADDIR NDKRFNFHTY REHTMLPNVA
GLDLFQLNDL GKKILSHVIG YRLTHNLEWH EVPLRNSLLA VISQQSSRVF LGKKFCRDPT
WLKINTDITV LAFRAVQELR VYPNLLRPVV GWFLPACRVL RSEVRKARKI VEPIVQKRRD
YKAACLREQT NPEQFLDTIE WAEECAGSQA YDPTVTQLTI ALSAMHNTSD FLTQLVFDLC
ERPNLIEDLR QEIISVRKKH PWGKATIHHL KLMDSVMKES QRLKPIGLVN MRRRAENSVE
LADGLIIRKG DLLMISSANQ WNPAIYPDPD QFDGYRFYNM RQTPDKKNLS HFVSTNVNHI
GFGHGRHACP GRFFAAAETK VALCHILLKY DFKLVGEAPP KILAIGSITS ANPFAKIAIR
RREEEVSLGV SEP
