COP4_COPC7
ID COP4_COPC7 Reviewed; 345 AA.
AC A8NU13;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Linoleate 10R-lipoxygenase COP4;
DE EC=4.2.3.91;
DE AltName: Full=(+)-sativene synthase;
DE EC=4.2.3.129;
DE AltName: Full=Beta-copaene synthase;
DE EC=4.2.3.127;
DE AltName: Full=Beta-cubebene synthase;
DE EC=4.2.3.128;
DE AltName: Full=Sesquiterpene synthase COP4;
GN Name=COP4; ORFNames=CC1G_06441;
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, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
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: Sesquiterpene synthase that catalyzes the cyclization of
CC farnesyl diphosphate (FPP) into multiple products, including germacrene
CC D, beta-copaene, beta-cubebene, (+)-sativene and cubebol, a natural
CC sesquiterpene alcohol used in the food industry for its cooling and
CC refreshing taste. Terpenoid hydrocarbons resulting from cyclization of
CC farnesyl diphosphate are intermediates in the biosynthesis of
CC biologically active compounds such as antibiotics, toxins and
CC pheromones. {ECO:0000269|PubMed:20419721}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = cubebol + diphosphate;
CC Xref=Rhea:RHEA:31823, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:63446, ChEBI:CHEBI:175763; EC=4.2.3.91;
CC Evidence={ECO:0000269|PubMed:20419721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate;
CC Xref=Rhea:RHEA:33111, ChEBI:CHEBI:33019, ChEBI:CHEBI:64799,
CC ChEBI:CHEBI:175763; EC=4.2.3.127;
CC Evidence={ECO:0000269|PubMed:20419721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-cubebene + diphosphate;
CC Xref=Rhea:RHEA:32019, ChEBI:CHEBI:10363, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.128;
CC Evidence={ECO:0000269|PubMed:20419721};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-sativene + diphosphate;
CC Xref=Rhea:RHEA:33119, ChEBI:CHEBI:33019, ChEBI:CHEBI:64800,
CC ChEBI:CHEBI:175763; EC=4.2.3.129;
CC Evidence={ECO:0000269|PubMed:20419721};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11 uM for all-trans-farnesyl diphosphate
CC {ECO:0000269|PubMed:20419721};
CC KM=20 uM for cis-trans-farnesyl diophosphate
CC {ECO:0000269|PubMed:20419721};
CC KM=24 uM for trans-geranyl diphosphate {ECO:0000269|PubMed:20419721};
CC -!- DOMAIN: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; AACS02000004; EAU85540.1; -; Genomic_DNA.
DR RefSeq; XP_001836356.1; XM_001836304.1.
DR AlphaFoldDB; A8NU13; -.
DR SMR; A8NU13; -.
DR EnsemblFungi; EAU85540; EAU85540; CC1G_06441.
DR GeneID; 6012899; -.
DR KEGG; cci:CC1G_06441; -.
DR VEuPathDB; FungiDB:CC1G_06441; -.
DR eggNOG; ENOG502SJ7W; Eukaryota.
DR HOGENOM; CLU_042538_2_1_1; -.
DR InParanoid; A8NU13; -.
DR OMA; AMETWVI; -.
DR OrthoDB; 1143139at2759; -.
DR BRENDA; 4.2.3.127; 1606.
DR BRENDA; 4.2.3.128; 1606.
DR BRENDA; 4.2.3.129; 1606.
DR SABIO-RK; A8NU13; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034686; Terpene_cyclase-like_2.
DR SFLD; SFLDG01020; Terpene_Cyclase_Like_2; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..345
FT /note="Linoleate 10R-lipoxygenase COP4"
FT /id="PRO_0000416224"
FT MOTIF 87..91
FT /note="DDXXD motif"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 91
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 222
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 230
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 345 AA; 39693 MW; 0BF4A6A95B74A29E CRC64;
MRPTARQFTL PDLFSICPLQ DATNPWYKQA AAESRAWINS YNIFTDRKRA FFIQGSNELL
CSHVYAYAGY EQFRTCCDFV NLLFVVDEIS DDQNGQDARA TGRIFVNAMR DAHWDDGSIL
AKITHEFRER FVRLAGPKTV RRFADLCESY TDCVAREAEL RERNQVLGLN DFIALRRQNS
AVLLCYSLVE YILGIDLDDE VYEDPTFAKA YWAACDFVCW ANDVYSYDME QAKGHTGNNV
VTVLMKEKDL SLQEASDYIG RECEKQMRDY LEAKSQLLQS TDLPQEAVRY IEALGYWMVG
NLVWSFESQR YFGAQHERVK ATHVVHLRPS SVLEASCDSD SDSDC
