STS2_THAGA
ID STS2_THAGA Reviewed; 561 AA.
AC K4LMW2;
DT 13-NOV-2013, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Sesquiterpene synthase 2;
DE EC=4.2.3.143;
DE AltName: Full=Kunzeaol synthase STS2;
GN Name=STS2;
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, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 kunzeaol. Produces mainly
CC (-)-germacrene D along with gamma-cadinene.
CC {ECO:0000269|PubMed:22938155}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + kunzeaol;
CC Xref=Rhea:RHEA:36063, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:72776, ChEBI:CHEBI:175763; EC=4.2.3.143;
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.6 uM for farnesyl diphosphate (at pH 7.5 and 28 degrees Celsius)
CC {ECO:0000269|PubMed:22938155};
CC Note=kcat is 0.03 sec(-1) with farnesyl diphosphate as substrate (at
CC pH 7.5 and 28 degrees Celsius).;
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; JQ290345; AFV09099.1; -; mRNA.
DR AlphaFoldDB; K4LMW2; -.
DR SMR; K4LMW2; -.
DR KEGG; ag:AFV09099; -.
DR BRENDA; 4.2.3.143; 13957.
DR UniPathway; UPA00213; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; 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 2"
FT /id="PRO_0000424293"
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; 64663 MW; 5D5B073CA628CB50 CRC64;
MAVYVNSTTG PPSSVVRNSA GFHPSIWGDT FIPSGNSAVQ KTDVDRKEEE NLQLLKQEVK
KMLTAGDTCQ QDLICLIDDI QRLGLSYHFE AEIDTLLQHV KDSYLEYYGT KNHDNLHDVA
LSFRLLRQEG HNISSDVFSK FQDSDGKFNE KLVKDVRGML SLFEAAHLSV HGENILEDAL
EFTTSHLNSY LNSNPNAPLA DLVRRALKYP LRKSFNRMVA RHYISIYHKY YWHKQVLLDL
AKCDFNLVQK VHQKELGYIT RWWKDLDFTN KLPFARDRVV ECYFWITGVY FEPRYAAPRK
FLTKVISLTS IIDDIYDVYG TPEELVQLTD AIDKWDINIL DQLPEYMRHA YKPLLDVFAE
GEEEMAKEGL PTYGVDYAKE AFKRLTVTYL HEAKWLQAQY FPTFEEYMSV ALVSGAVKML
SVSSFVRMGN IATREAFEWL SKDPLIVNGL SVICRLSDDI VGHEFENQRP HIPSAVECYM
KSHHVTKETA YAELRKPIIN AWKDMNEECL QPEAPPKPLL ERVFNLARVI NFLYDGHDGY
THSSTRTKDM ITSVLINPIP A
