TPS2_XANST
ID TPS2_XANST Reviewed; 548 AA.
AC A0A142BX74;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 03-AUG-2022, entry version 22.
DE RecName: Full=Sesquiterpene synthase TPS2 {ECO:0000305};
DE AltName: Full=Guaia-4,6-diene synthase {ECO:0000303|PubMed:26858282};
DE EC=4.2.3.179 {ECO:0000269|PubMed:26858282};
DE AltName: Full=Terpene synthase 2 {ECO:0000303|PubMed:26858282};
DE Short=XsTPS2 {ECO:0000303|PubMed:26858282};
GN Name=TPS2 {ECO:0000303|PubMed:26858282};
OS Xanthium strumarium (Rough cocklebur).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae;
OC Heliantheae alliance; Heliantheae; Xanthium.
OX NCBI_TaxID=318068;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND MOTIF.
RC TISSUE=Leaf;
RX PubMed=26858282; DOI=10.1093/pcp/pcw019;
RA Li Y., Chen F., Li Z., Li C., Zhang Y.;
RT "Identification and functional characterization of sesquiterpene synthases
RT from Xanthium strumarium.";
RL Plant Cell Physiol. 57:630-641(2016).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds (PubMed:26858282). Mediates the conversion of
CC (2E,6E)-farnesyl diphosphate (FPP) into guaia-4,6-diene
CC (PubMed:26858282). {ECO:0000269|PubMed:26858282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + guaia-4,6-diene;
CC Xref=Rhea:RHEA:54108, ChEBI:CHEBI:33019, ChEBI:CHEBI:138049,
CC ChEBI:CHEBI:175763; EC=4.2.3.179;
CC Evidence={ECO:0000269|PubMed:26858282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54109;
CC Evidence={ECO:0000269|PubMed:26858282};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q40577}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in glandular trichomes
CC (PubMed:26858282). Expressed in leaves and stems (PubMed:26858282).
CC {ECO:0000269|PubMed:26858282}.
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:0000305|PubMed:26858282}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
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DR EMBL; KT317709; AMP42991.1; -; mRNA.
DR SMR; A0A142BX74; -.
DR KEGG; ag:AMP42991; -.
DR BRENDA; 4.2.3.179; 15340.
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 GO; GO:0046246; P:terpene biosynthetic process; IEA:UniProt.
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; Metal-binding.
FT CHAIN 1..548
FT /note="Sesquiterpene synthase TPS2"
FT /id="PRO_0000455107"
FT MOTIF 301..305
FT /note="DDXXD motif"
FT /evidence="ECO:0000305|PubMed:26858282"
FT BINDING 264
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 301
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 301
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 442
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
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"
SQ SEQUENCE 548 AA; 63782 MW; 2C77588500D47005 CRC64;
MSTKQLEVVR PTAKFPPSVW GDQFLIYEEN TAEQLEVEEK VKKLIEVVRK DIKSSLEVQT
EHANLLKLID AIQRLGIAYH FEQEIEQALQ HIYGAYGDNW KGGNPSLWFR ILRQQGFYVS
CDIFNELKDE NGSFKESLTS DVQGLLDLYE ATYLRVQGEA VLEDAQVFTR THLNKLTNSL
TKTNSTLSTH IQDALEEPIR KRLPRLEALR YIPFYGQQEF HNKSLLKLAK LGFILLQSLH
KKELSQVSRW WKRLDITKDL PYVRDRMVES YFWALGVYFE PKYSHARMFL AKVFTVTAVI
DDTYDSYGTY EELMIFTEAV QRWSVSCIDM LPEYMKPMYQ VLMGVYEEME EILLKDGKEY
QLSYAIESMK ELTRNYMMEA KWAHEGYVPT TEEHLSVSYV SSGYVMLTTT CFVGMGDLVT
DESFKWALSK PPLVKASCII ARLMNDFVSQ KEEKEKMHVV SNVDSYMKQY GVTKEYAHNV
LKNKIEDAWM DLTLESLTCK NVPMHVKIRV INLTQVLTVM YKGKDNYTEV GEELIHHIRS
LLIHGMSI
