TPS1_XANST
ID TPS1_XANST Reviewed; 548 AA.
AC A0A142BX70;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 08-JUN-2016, sequence version 1.
DT 03-AUG-2022, entry version 21.
DE RecName: Full=Sesquiterpene synthase TPS1 {ECO:0000305};
DE AltName: Full=Beta-caryophyllene synthase {ECO:0000303|PubMed:26858282};
DE EC=4.2.3.57 {ECO:0000269|PubMed:26858282};
DE AltName: Full=Beta-copaene synthase {ECO:0000303|PubMed:26858282};
DE EC=4.2.3.127 {ECO:0000269|PubMed:26858282};
DE AltName: Full=Germacrene D synthase {ECO:0000303|PubMed:26858282};
DE EC=4.2.3.- {ECO:0000269|PubMed:26858282};
DE AltName: Full=Terpene synthase 1 {ECO:0000303|PubMed:26858282};
DE Short=XsTPS1 {ECO:0000303|PubMed:26858282};
GN Name=TPS1 {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 germacrene D, (-)-(E)-beta-
CC caryophyllene and beta-copaene (PubMed:26858282).
CC {ECO:0000269|PubMed:26858282}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene D;
CC Xref=Rhea:RHEA:68716, ChEBI:CHEBI:33019, ChEBI:CHEBI:49045,
CC ChEBI:CHEBI:175763; Evidence={ECO:0000269|PubMed:26858282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68717;
CC Evidence={ECO:0000269|PubMed:26858282};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (-)-(E)-beta-caryophyllene +
CC diphosphate; Xref=Rhea:RHEA:28294, ChEBI:CHEBI:10357,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.57;
CC Evidence={ECO:0000269|PubMed:26858282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28295;
CC Evidence={ECO:0000269|PubMed:26858282};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = beta-copaene + diphosphate;
CC Xref=Rhea:RHEA:33111, ChEBI:CHEBI:33019, ChEBI:CHEBI:64799,
CC ChEBI:CHEBI:175763; EC=4.2.3.127;
CC Evidence={ECO:0000269|PubMed:26858282};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33112;
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: Expressed in leaves and stems.
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; KT317705; AMP42987.1; -; mRNA.
DR BRENDA; 4.2.3.75; 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 TPS1"
FT /id="PRO_0000455106"
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 445
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 445
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
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; 64501 MW; F81A0E7633B87865 CRC64;
MEVKQEVLRP VSNFKPSIWG DQFLVYDEKE EDATVAQLIE CLKEEVRKEI MVALDDRNKH
ANLLKLVSDI QRLGISYCFK QEIEQALGHI YDVYGDEWEG GSLSIWFRLL RQQGFFVSCD
IFKKYKNNDG TFKDSLTRNV EGMLELYEAA YLRVRGEVIL DDALAFTKGQ LEKITKDPLQ
WNCNLSLSKH IKEALERPIW KRLPRLEVVR YIPFYEQQDS HNESLLRLAK LEFNRLQSLH
KRELSQLSKW WKDFEPTKNL HYVRDRLVEL YFWVLGVYFE PQYSRSRIFL TKVIKIATVL
DDTYDNYGVY DELEIFTDAI DRWSITCIDA LPDYMKFIYK ILLDTYGEME EIMASEGKAY
QVYYAKEALK ELSRNYMIEA KWTNEGYEPT LKEHETVSFI TAGYQMLTPS SFVGMGETVT
EEPFKWALTF PPLIKSASVV SRIMDDIIGH KEEGKRKHVV STVECYMKEH DVTEEYVYDL
FKERVEDAWK DMNLELLTCE NIPLALKMRT INLARVIESI YKYDDNLKNV GAEIQDNIKS
CFIISMSI
