PC450_PENRW
ID PC450_PENRW Reviewed; 491 AA.
AC B6HFX9;
DT 29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Conidiogenone synthase PchP450 {ECO:0000303|PubMed:30343633};
DE EC=1.-.-.- {ECO:0000305|PubMed:30343633};
DE AltName: Full=Conidiogenone biosynthesis cluster protein PchP450 {ECO:0000303|PubMed:30343633};
DE AltName: Full=Cytochrome P450 monooxygenase PchP450 {ECO:0000303|PubMed:30343633};
GN Name=PchP450 {ECO:0000303|PubMed:30343633};
GN ORFNames=Pc20g10870, PCH_Pc20g10870;
OS Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin
OS 54-1255) (Penicillium chrysogenum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC Penicillium chrysogenum species complex.
OX NCBI_TaxID=500485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255;
RX PubMed=18820685; DOI=10.1038/nbt.1498;
RA van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A., van der Klei I.J.,
RA van Peij N.N.M.E., Veenhuis M., von Doehren H., Wagner C., Wortman J.R.,
RA Bovenberg R.A.L.;
RT "Genome sequencing and analysis of the filamentous fungus Penicillium
RT chrysogenum.";
RL Nat. Biotechnol. 26:1161-1168(2008).
RN [2]
RP FUNCTION.
RX PubMed=30343633; DOI=10.1080/09168451.2018.1536518;
RA Shiina T., Nakagawa K., Fujisaki Y., Ozaki T., Liu C., Toyomasu T.,
RA Hashimoto M., Koshino H., Minami A., Kawaide H., Oikawa H.;
RT "Biosynthetic study of conidiation-inducing factor conidiogenone:
RT heterologous production and cyclization mechanism of a key bifunctional
RT diterpene synthase.";
RL Biosci. Biotechnol. Biochem. 83:192-201(2019).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of conidiogenone, a diterpene known to induce
CC the conidiation (PubMed:30343633). The bifunctional terpene synthase
CC PrDS converts isopentenyl diphosphate (IPP) and dimethylallyl
CC diphosphate (DMAPP) into deoxyconidiogenol (PubMed:30343633). The C-
CC terminal prenyltransferase (PT) domain of PrDS catalyzes formation of
CC GGPP, whereas the N-terminal terpene cyclase (TC) domain catalyzes the
CC cyclization of GGPP into deoxyconidiogenol (PubMed:30343633). The
CC cytochrome P450 monooxygenase PrP450 then catalyzes two rounds of
CC oxidation to furnish conidiogenone (By similarity).
CC {ECO:0000250|UniProtKB:W6Q9B3, ECO:0000269|PubMed:30343633}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000250|UniProtKB:W6Q9B3}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AM920435; CAP86416.1; -; Genomic_DNA.
DR RefSeq; XP_002563576.1; XM_002563530.1.
DR SMR; B6HFX9; -.
DR EnsemblFungi; CAP86416; CAP86416; PCH_Pc20g10870.
DR GeneID; 8308897; -.
DR KEGG; pcs:Pc20g10870; -.
DR VEuPathDB; FungiDB:PCH_Pc20g10870; -.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_14_4_1; -.
DR OMA; NIVTHRE; -.
DR OrthoDB; 1247045at2759; -.
DR BioCyc; PCHR:PC20G10870-MON; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000000724; Contig Pc00c20.
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 Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..491
FT /note="Conidiogenone synthase PchP450"
FT /id="PRO_0000453713"
FT TRANSMEM 2..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 430
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; 55322 MW; EC03EA242E5F92B6 CRC64;
MLLLWFGFFS FVCGLVIYRL QFHPLSKFPG PKLAALTSLY EFYYNVVLGG RYLWEIERMH
EQYGPIVRIT PHELHVADPN FYTEIYAGPT RRRDKDPRLV RLAGQPTSMF ATVDHGLHSS
RRAILNNYFS KRSIAGLEDM IQGKVQKLVK RLNIACDQGT VVQLDAASSA LTADIISEYA
HGVSLDYLDD VNFNNEVADS ILSLASVVHV LKFFPFLLDL SKFIPDKVLE NLWSHAANIL
RLQKLVRAQA DVALQNGGKV NGQATMFGAL CDPSLPAQER TLDRLQDEGF SLIGGGTETT
TGTLKVIMFH LLNEKALLRK LRKELEESPS GTWAELEKLP YMRGVMNEGL RLSGVITRLP
RRAPDEALRY KQWTIPPNSL MSTSSHFVHT NSDLFPDPLV FDPERWIRAE AAGQRLEHMI
VTFSKGSRQC MGNHLALAEL YLVISTLVRE FDMDLYGVTA DNIVTHREYG FGVPKERGGG
LRVSISRVRT P
