COX2_COPC7
ID COX2_COPC7 Reviewed; 526 AA.
AC A8NCK6;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 63.
DE RecName: Full=Cytochrome P450 monooxygenase COX2 {ECO:0000303|PubMed:19400802};
DE EC=1.-.-.- {ECO:0000269|PubMed:19400802};
DE AltName: Full=Alpha-cuprenene oxidase 2 {ECO:0000303|PubMed:19400802};
GN Name=COX2 {ECO:0000303|PubMed:19400802}; ORFNames=CC1G_03564;
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; EAU89299.1; -; Genomic_DNA.
DR RefSeq; XP_001832550.1; XM_001832498.2.
DR AlphaFoldDB; A8NCK6; -.
DR SMR; A8NCK6; -.
DR STRING; 5346.XP_001832550.1; -.
DR EnsemblFungi; EAU89299; EAU89299; CC1G_03564.
DR GeneID; 6009037; -.
DR KEGG; cci:CC1G_03564; -.
DR VEuPathDB; FungiDB:CC1G_03564; -.
DR eggNOG; KOG0156; Eukaryota.
DR InParanoid; A8NCK6; -.
DR OMA; FRHVFAI; -.
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..526
FT /note="Cytochrome P450 monooxygenase COX2"
FT /id="PRO_0000444638"
FT TRANSMEM 12..31
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 11
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"
SQ SEQUENCE 526 AA; 59361 MW; 0B5CF37B09D30EBD CRC64;
MNIVNSLDLS NITTNHVAAA VCAGIAVYAI VAGRNRGKKY PPGPKGHPLI GSLFEMPIQN
AHVVYKEWAK TYGDMIFFKV LGQPFLILSS EETITDLLDK RSTIYSSRPR MPMVVELMGW
DYTLGLLPYG ERWRFLRREF HRFMSPTAVS NYRQIQENSV YTFLNNLVES PEQFSKHLRL
FYGSISMKVS YGINVKSAED QYLLDAEGAM SGFMEAGIPG RFWVDLFPAL KYVPSWMPGA
EFKRKAARWA RLNDISLERP FKHVLDQLKK GVASQSVSAT LIEELPDQNS PDRKEKETIA
RNISATTFLA GIDTIHSTTQ AFFYAMAQFP EVQKKAQAEI DAVVGDKRLP TFEDRDQLPY
VNALVKELIR WSEVAPLGIY HSTTEDDEYK GYFIPKGTIV MTNAWSILTD PVTYPDPFAF
KPERYLKNGV MNPDAPRPED LAFGRGRRIC PGRYLADETL FMTSVGVLAG FNISPPLDKS
GKPIKLKNER VGTITLTPPK FECRIEPRSP AIRTMIHDTA ESISAL
