COP_ELETR
ID COP_ELETR Reviewed; 556 AA.
AC H9L9E5;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2012, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Sesquiterpene synthase Cop {ECO:0000303|Ref.1};
DE AltName: Full=Alpha-copaene synthase {ECO:0000303|Ref.1};
DE Short=EtCop {ECO:0000303|Ref.1};
DE EC=4.2.3.133 {ECO:0000269|Ref.1};
GN Name=COP {ECO:0000303|Ref.1};
OS Eleutherococcus trifoliatus (Climbing ginseng) (Zanthoxylum trifoliatum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Araliaceae; Eleutherococcus.
OX NCBI_TaxID=46385;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX DOI=10.1515/HF.2011.135;
RA Wen C.-H., Tseng Y.-H., Chu F.-H.;
RT "Identification and functional characterization of a sesquiterpene synthase
RT gene from Eleutherococcus trifoliatus.";
RL Holzforschung 66:183-189(2012).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds (Ref.1). Mediates the conversion of (2E,6E)-farnesyl
CC diphosphate (FPP) into alpha-copaene (Ref.1). Not active with geranyl
CC diphosphate (GPP) as substrate (Ref.1). {ECO:0000269|Ref.1}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-copaene + diphosphate;
CC Xref=Rhea:RHEA:33991, ChEBI:CHEBI:10221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.133; Evidence={ECO:0000269|Ref.1};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33992;
CC Evidence={ECO:0000269|Ref.1};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|Ref.1}.
CC -!- TISSUE SPECIFICITY: Expressed in stems and leaves and, at low levels,
CC in rrots. {ECO:0000269|Ref.1}.
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|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; GU987104; ADK94034.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0102877; F:alpha-copaene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0010597; P:green leaf volatile biosynthetic process; IDA:UniProtKB.
DR GO; GO:0051762; P:sesquiterpene biosynthetic process; IDA:UniProtKB.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR InterPro; IPR001906; Terpene_synth_N.
DR InterPro; IPR036965; Terpene_synth_N_sf.
DR InterPro; IPR005630; Terpene_synthase_metal-bd.
DR InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
DR Pfam; PF01397; Terpene_synth; 1.
DR Pfam; PF03936; Terpene_synth_C; 1.
DR SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..556
FT /note="Sesquiterpene synthase Cop"
FT /id="PRO_0000454948"
FT MOTIF 308..312
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 308
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 556 AA; 64520 MW; E4EF5EE7B65F723D CRC64;
MATYLQASSG PCSTIVPEIT RRSANYHPNI WGDQFLKYNS FDLSKTDANT KEHFRQLKEE
VKKMLVDAGP NQQLNLIDDI QRLGVAYQFE AEIDAALQRM NVIFQGNDDD LHTISLRFRL
LRQHGYNVSS DVFRKFMDNN GKFKECLISD LRGVLSLYEA THFRVHGEDI LEDALEFTTS
HLERLKSHLK NPLAAQVIRA LKCPIHKGLN RLEAKHYISI YQQEDDSHNK VLLNFAKLDF
NLLQKMHQGE LSHITRWWKE LNFAKKLPFA RDRVVECYFW ILGVYFEPQY LIARRFLTKI
IAMASVADDI YDVYGTLEEL VILTDAIERW DMGALDQIPE CMRVYHRALL DVYTEMEEEM
AKTGRPSYRV HYAKEAYKEL VRQYLAEAKW FQEDYDPTLE EYLPVALISG GYKMLATHSF
VGMGDLATKE AFDWVSNNPL IVKASSVICR LSDDMVGHEV EHERGDVASA VECYMKQYGV
TKQEVYIEFQ KQISNAWKDM NQECLHPTTV TMPLLTVIFN MTRVINLLYD EEDGYTNSNT
RTKDFITSVL IDPVQI
