ID   COX1_COPC7              Reviewed;         518 AA.
AC   A8NCK4;
DT   18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   03-AUG-2022, entry version 62.
DE   RecName: Full=Cytochrome P450 monooxygenase COX1 {ECO:0000303|PubMed:19400802};
DE            EC=1.-.-.- {ECO:0000269|PubMed:19400802};
DE   AltName: Full=Alpha-cuprenene oxidase 1 {ECO:0000303|PubMed:19400802};
GN   Name=COX1 {ECO:0000303|PubMed:19400802}; ORFNames=CC1G_03562;
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003;
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canbaeck B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kuees U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.-J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=19400802; DOI=10.1111/j.1365-2958.2009.06717.x;
RA   Agger S., Lopez-Gallego F., Schmidt-Dannert C.;
RT   "Diversity of sesquiterpene synthases in the basidiomycete Coprinus
RT   cinereus.";
RL   Mol. Microbiol. 72:1181-1195(2009).
RN   [3]
RP   FUNCTION.
RX   PubMed=20419721; DOI=10.1002/cbic.200900671;
RA   Lopez-Gallego F., Agger S.A., Abate-Pella D., Distefano M.D.,
RA   Schmidt-Dannert C.;
RT   "Sesquiterpene synthases Cop4 and Cop6 from Coprinus cinereus: catalytic
RT   promiscuity and cyclization of farnesyl pyrophosphate geometric isomers.";
RL   ChemBioChem 11:1093-1106(2010).
CC   -!- FUNCTION: Cytochrome P450 monooxygenase; part of the gene cluster that
CC       mediates the biosynthesis of alpha-cuprenene and oxidized derivatives
CC       (PubMed:19400802). The alpha-cuprenene synthase COP6 is the only
CC       sesquiterpene synthase identified in C.cinereus that appears to be part
CC       of a biosynthetic gene cluster and is highly specific since it
CC       catalyzes the cyclization of (2E,6E)-farnesyl diphosphate into only one
CC       product, alpha-cuprenene (PubMed:19400802, PubMed:20419721). The
CC       cytochrome P450 monooxygenase COX2 then oxidizes the cyclohexadiene
CC       ring of alpha-cuprenene at positions 1 and 4, yielding first alpha-
CC       cuparene, followed by alpha-cuparophenol and a further yet unidentified
CC       compound resulting from one additional oxidation step
CC       (PubMed:19400802). The cytochrome P450 monooxygenase COX1 then likely
CC       catalyzes the oxidation at position 9 of the pentane ring of alpha-
CC       cuprenene to give the corresponding hydroxy or ketone derivatives
CC       (PubMed:19400802). {ECO:0000269|PubMed:19400802,
CC       ECO:0000269|PubMed:20419721}.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:P04798};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000269|PubMed:19400802}.
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; AACS02000009; EAU89297.2; -; Genomic_DNA.
DR   RefSeq; XP_001832548.2; XM_001832496.2.
DR   AlphaFoldDB; A8NCK4; -.
DR   SMR; A8NCK4; -.
DR   STRING; 5346.XP_001832548.2; -.
DR   EnsemblFungi; EAU89297; EAU89297; CC1G_03562.
DR   GeneID; 6009035; -.
DR   KEGG; cci:CC1G_03562; -.
DR   VEuPathDB; FungiDB:CC1G_03562; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   HOGENOM; CLU_001570_2_3_1; -.
DR   InParanoid; A8NCK4; -.
DR   OMA; FNDYWKE; -.
DR   OrthoDB; 702827at2759; -.
DR   Proteomes; UP000001861; Unassembled WGS sequence.
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   1: Evidence at protein level;
KW   Glycoprotein; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW   Oxidoreductase; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..518
FT                   /note="Cytochrome P450 monooxygenase COX1"
FT                   /id="PRO_0000444637"
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         450
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        48
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        100
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        292
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        457
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   518 AA;  58438 MW;  CC1C4B857CAB9AF2 CRC64;
     MTSTTQVLIA LSSIVVAYFV KTALAKRKLN PRGLPYPPGP KGLPVIGNLT QLPQHKPWLV
     YKEWGRTYGD LMYLEAMGQP MIIINSLSRA LDLLDKRAVN YSDRPHVPTM DLCVLMKLDW
     VFAFMQYGAD WRNHRRAFHQ YLNHNMVHNY HPIQEQETQE FLRALIARPK DFLAHTRHLF
     GSIIIRISYG FEDEEYNKVL VEEAEALASG FSESIIPGRY LVNAFPFLRH VPSWLPGAGF
     QRTMQYLRKI SEKTLSEPFD NVKEALKTGN RQVGPSLAVG LIESLPDETH ANRTSLEVVA
     RNTSALSYIA GADTTVSSAQ ALILALAMHP EVQRKAQKEI DSVVGTDRLP NMSDKPNMPY
     VQAIVKEAGR WHTVLPLGFI HVSAKEDEYD GYFIPKGSFI FVNTWAIMHD PDVFKNPLQF
     NPERYLKNGQ IDTSVLDPEA ATFGFGRRIC PGRWLSNDSL FLMAASLLAT FNIAAPKDRT
     GKPIPLSLDT SSHLITAPLP YDCEFQLRSP KYAALLQK