ID   OLCB_PENCN              Reviewed;         491 AA.
AC   P9WEQ1;
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 olcB {ECO:0000303|PubMed:30090271};
DE            EC=1.-.-.- {ECO:0000269|PubMed:30090271};
DE   AltName: Full=15-deoxyoxalicine B biosynthesis cluster protein B {ECO:0000303|PubMed:30090271};
GN   Name=olcB {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 decaturin A. {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   SMR; P9WEQ1; -.
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; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
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..491
FT                   /note="Cytochrome P450 monooxygenase olcB"
FT                   /id="PRO_0000453886"
FT   TRANSMEM        5..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         435
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   491 AA;  56227 MW;  DE65C3E5B0BAD0B4 CRC64;
     MLNLLLLSLS VCLLYVFITA FWNLYIHPLH HIPGPRQWIA FPILRHLSAI RGTLDSDLRR
     WHFRYGSAVR FGPDEASFIT AEAWKDIYGS TRPQLPRVIS SGSNTSDIIN ANDANHARYR
     KALAHAFSTN GVRDQEPLVI DYIVKLVGRL KEVAESKLPT DMVKWYKLTT FDMIGDLAFG
     EHFGGLEKSE YHHWVATVGR FTRIIPFLKI MDAYPVLFKV FLAVMPQSFW KAQAEQAEYT
     KLTVQKRLNS SIAQDRPDFM DSMLRHRNEK DKLSEHELES NASVLVLAGS ETPADLLSGV
     TYWLLKTPEA LEKATGEVRS LMKAESEITF SSVEARLPYL LACVNEGLRL YPSLPGELQR
     MSPDTPMKIS GYDIPPRTRV SVHQYAAYSS PTNFHDPDRF IPERWLPEAK TNPSSPYLFD
     NREVFQPFSV GPRGCIGKSL AYPLMRTIIA RVLWNFDFDL CEESRSWHIQ KTFGLWEKPP
     LICKLTQRKQ S