ID   JANQ_PENJA              Reviewed;         501 AA.
AC   A0A0E3D8N7;
DT   10-APR-2019, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 16.
DE   RecName: Full=Cytochrome P450 monooxygenase janQ {ECO:0000303|PubMed:26213965};
DE            EC=1.-.-.- {ECO:0000305|PubMed:26213965};
DE   AltName: Full=Janthitremanes biosynthesis cluster protein Q {ECO:0000303|PubMed:26213965};
GN   Name=janQ {ECO:0000303|PubMed:26213965};
OS   Penicillium janthinellum (Penicillium vitale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], IDENTIFICATION, FUNCTION, AND PATHWAY.
RC   STRAIN=PN2408;
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 janthitremanes such
CC       as shearinine K or shearinine A (PubMed:26213965). The geranylgeranyl
CC       diphosphate (GGPP) synthase janG catalyzes the first step in
CC       janthitremane biosynthesis via conversion of farnesyl pyrophosphate and
CC       isopentyl pyrophosphate into geranylgeranyl pyrophosphate (GGPP)
CC       (PubMed:26213965). Condensation of indole-3-glycerol phosphate with
CC       GGPP by the prenyl transferase janC then forms 3-geranylgeranylindole
CC       (3-GGI) (PubMed:26213965). Epoxidation by the FAD-dependent
CC       monooxygenase janM leads to a epoxidized-GGI that is substrate of the
CC       terpene cyclase janB for cyclization to yield paspaline
CC       (PubMed:26213965). Paspaline is subsequently converted to 13-
CC       desoxypaspaline by the cytochrome P450 monooxygenase janP, via beta-PC-
CC       M6 in a series of alpha-face oxidations (Probable). The cytochrome P450
CC       monooxygenase janQ is proposed to carry out sequential beta-face
CC       oxidation steps at C-7 and C-13 of 13-desoxypaspaline to form
CC       paspalicine and paspalinine respectively (Probable). The indole
CC       diterpene prenyltransferase janD may then convert paspalinine into
CC       shearinine K which is substrate of janO and/or additional enzymes for
CC       oxidation and cyclization to generate shearinine A (Probable).
CC       {ECO:0000269|PubMed:26213965, 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; KF280651; AGZ20487.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0E3D8N7; -.
DR   SMR; A0A0E3D8N7; -.
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..501
FT                   /note="Cytochrome P450 monooxygenase janQ"
FT                   /id="PRO_5002410105"
FT   TRANSMEM        1..16
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         439
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        132
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   501 AA;  57297 MW;  1DFB330945B372D3 CRC64;
     MVLGLLAFIW LMRAWRQSLK IWVDVPSIGK DGILGQWITA LQWQQKARSL IQEGYEKHGH
     YAFKIATPSR WEIFICNEKM IKEYKNLMDD KFSANAVTAD MFQTKWTAPG AAEGVHKIPI
     PLLAKALTWQ RNRSSVTGDT YFKEFVTEFL HAWEVETKIT SEGPYEFCCF ETGTRIVAHL
     TAKSLVGHPL CRDPEIIDLF AGYGNAVPSS GFLIAMFPGI LKPLVAKFCE APKMSDRLDR
     IFLSEMKERQ LQTGSDASDI MSWLWHWTQE NEPGKYSEVD IVRSITSAVF GAIHTTTQVL
     VHCLFELATR PEYVEPLRQE VQQAVENHGG WEKEGIESML KLDSFIKECQ RFNPLDSGSL
     ARCATNDFTF SNGLKVAKGT YVFAPNAPVL FDERFYPNPH QFDGYRFYRL GQQTGKPQGF
     RFVATNSNYL QFGDGRHTCP GRYMAADEIR LMLGHILLHY DITTKENEGR PKNWFFKKIL
     FPDMKGVIVL KKRAEVRAVN K