ID   STS1_THAGA              Reviewed;         561 AA.
AC   K4L9M2;
DT   13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   03-AUG-2022, entry version 30.
DE   RecName: Full=Sesquiterpene synthase 1;
DE            EC=4.2.3.13;
DE   AltName: Full=D-cadinene synthase STS1;
GN   Name=STS1;
OS   Thapsia garganica (Deadly carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Thapsia.
OX   NCBI_TaxID=79022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   TISSUE=Root;
RX   PubMed=22938155; DOI=10.1042/bj20120654;
RA   Pickel B., Drew D.P., Manczak T., Weitzel C., Simonsen H.T., Ro D.-K.;
RT   "Identification and characterization of a kunzeaol synthase from Thapsia
RT   garganica: implications for the biosynthesis of the pharmaceutical
RT   thapsigargin.";
RL   Biochem. J. 448:261-271(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of delta-cadinene.
CC       {ECO:0000269|PubMed:22938155}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (1S,8aR)-delta-cadinene +
CC         diphosphate; Xref=Rhea:RHEA:19525, ChEBI:CHEBI:15385,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.13;
CC         Evidence={ECO:0000269|PubMed:22938155};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 manganese or magnesium ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; JQ290344; AFV09098.1; -; mRNA.
DR   AlphaFoldDB; K4L9M2; -.
DR   SMR; K4L9M2; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047461; F:(+)-delta-cadinene synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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   Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding.
FT   CHAIN           1..561
FT                   /note="Sesquiterpene synthase 1"
FT                   /id="PRO_0000424292"
FT   MOTIF           313..317
FT                   /note="DDXXD motif"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         458
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
FT   BINDING         466
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:O81192"
SQ   SEQUENCE   561 AA;  64339 MW;  B2D1ACA8C1F3420C CRC64;
     MAVYVNSTTG PPPSVGRNSA GFHPSIWGDK FITSSNSAVQ KTDVDRKEEE KLQLLKQEVK
     KMLTAGDTSQ QDLICLIDDI QRLGLSYHFE AEIDTLLQHV KHSYVEHYGK KNHDNLHDVA
     LSFRLLRQEG HNISSDVFSK FQDSDGKFKE ELVEDVRGML SLFEAAHLRV HGENILEDAL
     EFTTTHLNSY LNSNPSSSLA DLVRRALKYP LRKSFNRMVA RHYISVYHKF DWHKQVLLDM
     AKCDFNLVQK VHQNELGYIT RWWKDLDFTN KLPFARDRVV ECYFWITGVY FEPRYAAPRK
     FLTEVMSLTS IIDDIYDVYG TPDELVQLAD AIDKWDISIL DQLPEYVRHA YKPLLDTFAE
     AEEEMANEGL PTYGVDYAKE AFKRLAVAYL QETKWLQAQY IPTFEEYLSV ALVSAGGNML
     SVSSFVRMGN IATREAFEWL SKDPLIANGL SVIIRLSDDI VGHEFESQRP HIPSAVECYM
     KSHDVTKETA YAELQKPIIK AWKDMNEGCL HPEAPPKPLL ERVLNLARVL NFLYDGHDGY
     THSSTRTKDI ITTAFINPIP L