ID   GRA2_CLAGR              Reviewed;         570 AA.
AC   E9KMQ3;
DT   10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT   16-OCT-2013, sequence version 2.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=Grayanic acid biosynthesis cluster cytochrome P450 monooxygenase {ECO:0000303|PubMed:21289108};
DE            EC=1.-.-.- {ECO:0000305|PubMed:21289108};
GN   Name=P450 {ECO:0000303|PubMed:21289108};
OS   Cladonia grayi (Gray's cup lichen).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Lecanoromycetes;
OC   OSLEUM clade; Lecanoromycetidae; Lecanorales; Lecanorineae; Cladoniaceae;
OC   Cladonia.
OX   NCBI_TaxID=27339;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX   PubMed=21289108; DOI=10.3852/10-335;
RA   Armaleo D., Sun X., Culberson C.;
RT   "Insights from the first putative biosynthetic gene cluster for a lichen
RT   depside and depsidone.";
RL   Mycologia 103:741-754(2011).
RN   [2]
RP   FUNCTION.
RX   DOI=10.1016/0147-5975(92)90041-O;
RA   Culberson C., Armaleo D.;
RT   "Induction of a complete secondary-product pathway in a cultured lichen
RT   fungus.";
RL   Exp. Mycol. 16:52-63(1992).
CC   -!- FUNCTION: Non-reducing polyketide synthase; part of the gene cluster
CC       that mediates the biosynthesis of orcinol depsidone grayanic acid
CC       (GRA), the only major secondary metabolite known in C.grayi
CC       (PubMed:21289108). The first step consists in the ring and depside
CC       synthesis by PKS16 leading to 4-O-demethylsphaerophorin, involving
CC       different orcinol-like rings, one with acetyl CoA and the other with
CC       octanoyl CoA as the starter (Probable). Further depsidone formation by
CC       the GRA cluster-specific cytochrome P450 leads to 4-O-demethylgrayanic
CC       acid (Probable). Finally, the cluster specific O-methyltransferase
CC       probably converts the 4-O-demethylgrayanic acid into grayanic acid
CC       (Probable). {ECO:0000269|PubMed:21289108, ECO:0000305|PubMed:21289108,
CC       ECO:0000305|Ref.2}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000305|PubMed:21289108}.
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; GU930713; ADM79460.1; -; Genomic_DNA.
DR   BioCyc; MetaCyc:MON-21840; -.
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; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 2.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..570
FT                   /note="Grayanic acid biosynthesis cluster cytochrome P450
FT                   monooxygenase"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000445367"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         510
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        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   570 AA;  64899 MW;  7373423299DE5E43 CRC64;
     MLGVIQYSIL TIFWLPIAAA XLYGAGLAIY RLFLSPLAKF PGPKLAALTR KYESYYEAYQ
     NYEYYWKIKE LHKQYGELFT PLTASFXRXG PIVRVNPHEL HIDDKDFYYK LNSFQGAWNK
     DPYTAHQFAN PGSIVGTIDH DIHRKRRAAI MPFFSKQKIY ALESVIQGMV DKLCYRIEEY
     GKTGQPVNLR NASKCFAADV VGEYCFAESG GLXDKPDFAI EEMNQQQQGL KAGLRARYLP
     SWWMPVVRGA PAWIRASIDP AAKHFEVWHR VSDSLFVRLY DARKXGPVGR MEKRKNDEFY
     EKAGHRTIFH ELINSPHLPP EEKGTGRIIQ EAGAMVGAGG ESTSQVITAF VYCLLANPQV
     LSRLREELRS VIPNADSPAP TLRQLEALPY LVGPLLXSTY KYVGYLLTLV ARLRTGKIAR
     HQRVPRDRPL YFNEWEIPAG VSXHEDNIPM ASTDTAQTIC SMTPIFLQID PEVYPNPHAF
     MPERWLNLDE XQRQRLEHNL VPYSKGTRGC AGLTLANAEL YMLIPALVTR FDLELFDSDA
     WDTEMAVDSH HHSPRPDSKG VKVFVKKSTF