CS_HELAN
ID CS_HELAN Reviewed; 555 AA.
AC Q4U3F6;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Alpha-copaene synthase;
DE EC=4.2.3.133;
DE AltName: Full=Alpha-humulene synthase;
DE EC=4.2.3.104;
DE AltName: Full=Alpha-muurolene synthase;
DE EC=4.2.3.125;
DE AltName: Full=Delta-cadinene synthase;
DE Short=HaCS;
DE AltName: Full=Terpene synthase 2;
DE Short=HaTPS2;
GN Name=CS;
OS Helianthus annuus (Common sunflower).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Helianthus.
OX NCBI_TaxID=4232;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Trichome gland;
RX PubMed=19580670; DOI=10.1186/1471-2229-9-86;
RA Goepfert J.C., Macnevin G., Ro D.-K., Spring O.;
RT "Identification, functional characterization and developmental regulation
RT of sesquiterpene synthases from sunflower capitate glandular trichomes.";
RL BMC Plant Biol. 9:86-86(2009).
RN [2]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of germacrene-derived
CC sesquiterpene lactones (PubMed:30468448). Catalyzes the cyclization of
CC farnesyl diphosphate to alpha-copaene, delta-cadinene, alpha-muurolene,
CC beta-caryophyllene and alpha-humulene (PubMed:19580670).
CC {ECO:0000269|PubMed:19580670, ECO:0000303|PubMed:30468448}.
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;
CC Evidence={ECO:0000269|PubMed:19580670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33992;
CC Evidence={ECO:0000269|PubMed:19580670};
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:19580670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33104;
CC Evidence={ECO:0000269|PubMed:19580670};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = alpha-humulene + diphosphate;
CC Xref=Rhea:RHEA:31895, ChEBI:CHEBI:5768, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:175763; EC=4.2.3.104;
CC Evidence={ECO:0000269|PubMed:19580670};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31896;
CC Evidence={ECO:0000269|PubMed:19580670};
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 -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000303|PubMed:30468448}.
CC -!- TISSUE SPECIFICITY: Mainly expressed in sunflower trichomes.
CC {ECO:0000269|PubMed:19580670}.
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; DQ016668; AAY41422.2; -; mRNA.
DR EMBL; EU443250; ACA33926.1; -; Genomic_DNA.
DR AlphaFoldDB; Q4U3F6; -.
DR SMR; Q4U3F6; -.
DR KEGG; ag:AAY41422; -.
DR OMA; YPISSDY; -.
DR OrthoDB; 360509at2759; -.
DR PhylomeDB; Q4U3F6; -.
DR BRENDA; 4.2.3.13; 2597.
DR BRENDA; 4.2.3.133; 2597.
DR UniPathway; UPA00213; -.
DR GO; GO:0047461; F:(+)-delta-cadinene synthase activity; IDA:UniProtKB.
DR GO; GO:0102877; F:alpha-copaene synthase activity; IDA:UniProtKB.
DR GO; GO:0080017; F:alpha-humulene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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..555
FT /note="Alpha-copaene synthase"
FT /id="PRO_0000422212"
FT MOTIF 312..316
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
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 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 316
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 452
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 555 AA; 64263 MW; 40238AF1FE40A842 CRC64;
MATTEANTMA QANSQTTIEP VRHLANFPPS IWGDQFLSFS LDNSQLEAYS KAMEQPKENV
RRMILNPAID TNEKLGLIYC VYRLGLTYNF SKDIDGQLDE LFKQLNLQSY NEADLYTISI
HFQVFRHFGY RFSCDVFNKF KDSSSGKFKE DMTRDVRGMI SLYESAQLRI RGESILDEAG
AFAESKLKTI EKTLDGTLAQ QVKHVLERPF NRGHQMVEAR KYLFLFEEEI SRYDSLLMLA
KVHFNYLQLL QKEELRSVSK WWKDLDLPAK TLYVRDRVPE LYVWILAFFL EPYYSEVRII
TTKIVLLVLV LDDTYDAYAT IEESRLLTHA INRWEVSAML QLPEYMKPLY EILLNEYDGF
YKHGRTNVIE TSKKAFQDLA RSYHQESEWR HAKEVPSFEE YMKIGTTTSA HNVLSKTALI
GMGNIVTREA LAWYESYPKI VQLSELIGRL EDDVVSVEFE RERAPTATSV DAYMKTYGVS
ENVAVKILKK LVENGWKDLN EACLKPTEVS LDLLAPIIGL TNMTDVAYRH NDGLTFPEKT
LKEYITLLFC VPVPM
