COP3_COPC7
ID COP3_COPC7 Reviewed; 425 AA.
AC A8NE23;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Alpha-muurolene synthase;
DE EC=4.2.3.125 {ECO:0000269|PubMed:19400802, ECO:0000269|PubMed:20889795};
DE AltName: Full=Gamma-muurolene synthase;
DE EC=4.2.3.126 {ECO:0000269|PubMed:19400802, ECO:0000269|PubMed:20889795};
DE AltName: Full=Germacrene-A synthase;
DE EC=4.2.3.23 {ECO:0000269|PubMed:19400802, ECO:0000269|PubMed:20889795};
GN Name=COP3; ORFNames=CC1G_12294;
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, CATALYTIC ACTIVITY, AND MUTAGENESIS OF LYS-251; HIS-255 AND
RP ASN-256.
RX PubMed=20889795; DOI=10.1128/aem.01811-10;
RA Lopez-Gallego F., Wawrzyn G.T., Schmidt-Dannert C.;
RT "Selectivity of fungal sesquiterpene synthases: role of the active site's
RT H-1 alpha loop in catalysis.";
RL Appl. Environ. Microbiol. 76:7723-7733(2010).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of alpha-
CC muurolene, and at lower level (+)-(R)-germacrene A and gamma-muurolene.
CC {ECO:0000269|PubMed:19400802, ECO:0000269|PubMed:20889795}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-muurolene + diphosphate;
CC Xref=Rhea:RHEA:33103, ChEBI:CHEBI:33019, ChEBI:CHEBI:64797,
CC ChEBI:CHEBI:175763; EC=4.2.3.125;
CC Evidence={ECO:0000269|PubMed:19400802, ECO:0000269|PubMed:20889795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-muurolene;
CC Xref=Rhea:RHEA:33107, ChEBI:CHEBI:33019, ChEBI:CHEBI:64798,
CC ChEBI:CHEBI:175763; EC=4.2.3.126;
CC Evidence={ECO:0000269|PubMed:19400802, ECO:0000269|PubMed:20889795};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-(R)-germacrene A +
CC diphosphate; Xref=Rhea:RHEA:12516, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:41595, ChEBI:CHEBI:175763; EC=4.2.3.23;
CC Evidence={ECO:0000269|PubMed:19400802, ECO:0000269|PubMed:20889795};
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 -!- 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; AACS02000002; EAU88892.1; -; Genomic_DNA.
DR RefSeq; XP_001832925.1; XM_001832873.1.
DR AlphaFoldDB; A8NE23; -.
DR SMR; A8NE23; -.
DR STRING; 5346.XP_001832925.1; -.
DR EnsemblFungi; EAU88892; EAU88892; CC1G_12294.
DR GeneID; 6009414; -.
DR KEGG; cci:CC1G_12294; -.
DR VEuPathDB; FungiDB:CC1G_12294; -.
DR eggNOG; ENOG502S2X0; Eukaryota.
DR HOGENOM; CLU_042538_2_1_1; -.
DR InParanoid; A8NE23; -.
DR OMA; DLIEYAM; -.
DR OrthoDB; 1143139at2759; -.
DR BRENDA; 4.2.3.125; 1606.
DR BRENDA; 4.2.3.126; 1606.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0034005; F:germacrene-A synthase activity; IEA:UniProtKB-EC.
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..425
FT /note="Alpha-muurolene synthase"
FT /id="PRO_0000419683"
FT REGION 348..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 97..101
FT /note="DDXXD motif"
FT COMPBIAS 348..363
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 101
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 240
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT MUTAGEN 251
FT /note="K->I: Weak effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:20889795"
FT MUTAGEN 255
FT /note="H->P: Increased synthesis by of the cis pathway
FT product delta-cadinene 8."
FT /evidence="ECO:0000269|PubMed:20889795"
FT MUTAGEN 256
FT /note="N->L: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:20889795"
SQ SEQUENCE 425 AA; 47766 MW; 1CDFDB41EB11C49E CRC64;
MSTPSSSLTT DESPASFILP DLVSHCPFPL RYHPKGDEVA KQTVHWLDSN CPDLTAKERK
AMYGLQAGEL TGYCYPYTTP ERLRVVADFL NYLFHLDNIS DGMMTRETAV LADVVMNALW
FPEDYRPTKG QAAEELNPGK LARDFWSRCI PDCGPGTQAR FKETFGSFFE AVNIQARARD
EGVIPDLESY IDVRRDTSGC KPCWVLIEYA LGIDLPDFVV EHPVIAALNQ GTNDLVTWSN
DIFSYNVEQS KGDTHNMIII LMEHHGHTLQ SAVDYVGSLC QQTINTFCEN KQQLPSWGPE
IDDMVAKYVQ GLEDWIVGSL HWSFQTRRYF GDEGQEIKQH RLVKLLTVAP PPPPPPPTPP
PQSSDADTKK QKVKAQDGKG PVSDEEVWAL VRAEQSKGSI LESLFGFLTT SLSRIFFGYF
FAYSH
