PENQ_PENCR
ID PENQ_PENCR Reviewed; 510 AA.
AC A0A0E3D8P8;
DT 10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT 24-JUN-2015, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Cytochrome P450 monooxygenase penQ {ECO:0000303|PubMed:26213965};
DE EC=1.-.-.- {ECO:0000305|PubMed:26213965};
DE AltName: Full=Penitrem biosynthesis cluster protein Q {ECO:0000303|PubMed:26213965};
GN Name=penQ {ECO:0000303|PubMed:26213965};
OS Penicillium crustosum (Blue mold fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36656;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC STRAIN=PN2402;
RX PubMed=26213965; DOI=10.3390/toxins7082701;
RA Nicholson M.J., Eaton C.J., Starkel C., Tapper B.A., Cox M.P., Scott B.;
RT "Molecular cloning and functional analysis of gene clusters for the
RT biosynthesis of indole-diterpenes in Penicillium crustosum and P.
RT janthinellum.";
RL Toxins 7:2701-2722(2015).
CC -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC mediates the biosynthesis of the indole diterpenes penitrems
CC (PubMed:26213965). The geranylgeranyl diphosphate (GGPP) synthase penG
CC catalyzes the first step in penitrem biosynthesis via conversion of
CC farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl
CC pyrophosphate (GGPP) (Probable). Condensation of indole-3-glycerol
CC phosphate with GGPP by the prenyl transferase penC then forms 3-
CC geranylgeranylindole (3-GGI) (Probable). Epoxidation by the FAD-
CC dependent monooxygenase penM leads to a epoxidized-GGI that is
CC substrate of the terpene cyclase penB for cyclization to yield
CC paspaline (Probable). Paspaline is subsequently converted to 13-
CC desoxypaxilline by the cytochrome P450 monooxygenase penP, the latter
CC being then converted to paxilline by the cytochrome P450 monooxygenase
CC penQ (PubMed:26213965). Paxilline is converted to beta-paxitriol via C-
CC 10 ketoreduction by the short-chain dehydrogenase PC-15 which can be
CC monoprenylated at the C-20 by the indole diterpene prenyltransferase
CC penD (Probable). A two-step elimination (acetylation and elimination)
CC process performed by the O-acetyltransferase PC-16 and the
CC P.simplicissimum ptmI-ortholog not yet identified in P.crustosum, leads
CC to the production of the prenylated form of penijanthine (Probable).
CC The FAD-linked oxidoreductase ptmO then converts the prenylated form of
CC penijanthine into PC-M5 which is in turn transformed into PC-M4 by the
CC aromatic dimethylallyltransferase PC-22 (Probable). A series of
CC oxidation steps involving 4 cytochrome P450 monooxygenases (PC-21, PC-
CC 05, PC-23, PC-20) and a FAD-dependent monooxygenase (PC-14) are
CC required for the transformation of PC-M4 to penitrems A and E.
CC Synthesis of these final products is proposed to proceed via penitrems
CC D and C (PC-21, PC-05, PC-14) and penitrems B and F (PC-21, PC-05, PC-
CC 14, PC-23) (Probable). {ECO:0000269|PubMed:26213965,
CC ECO:0000305|PubMed:26213965}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- PATHWAY: Secondary metabolite biosynthesis.
CC {ECO:0000305|PubMed:26213965}.
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; KC963408; AGZ20192.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0E3D8P8; -.
DR SMR; A0A0E3D8P8; -.
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 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 SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..510
FT /note="Cytochrome P450 monooxygenase penQ"
FT /id="PRO_0000446574"
FT TRANSMEM 9..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 448
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"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 482
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 510 AA; 58211 MW; 97AC174F2C464196 CRC64;
MDYVTQSPWI VTLIVAATTY CTLRWVQYWR SWVNVPVVGR RGFLGSWIST ILWTWEARGC
IQKGYEKNKD FAFQVSTPNG WEVCICNDDM IKEYKNLMDD QMSALAVTSE TFQAKYTLPG
ADWDAVHKLV PQPALAKSLM WLRNRAANDT DPYFADFVKT FQRAFKEEIQ VEQDGAPFPC
FPRYSRIVAA LTVKALLGSL ENRPELIDLL CEYAEAIPLD GFFIALFPAV LKPIVAFFCK
APRLSDRLVK VITEEIARRE LENKHRIPED MTDWMAQWVK DNPGYCIESA VVRVIATFFG
GIHTTTQLTV HTLLEIATRP EYVDPLRQEI TTALKTHGGW NKSAIESMTK LDSFIKEAQR
FNPLDAASLA RQATRDFQFS NGLKLPRGTW VFAPNGPMLF DESLYPAGSQ FDGLRFWKLA
EQTQKPHDYR LVTASSKYLQ FGDGRHTCPG RFMAADEIRL IVAHTLFHFD IAIKNHGPRP
RNTTFKKICF PDMAAEIMLR PRKPHGSDGN
