TPS1_INUHU
ID TPS1_INUHU Reviewed; 563 AA.
AC A0A1L2D3T3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 03-AUG-2022, entry version 23.
DE RecName: Full=10-epi-juneol synthase {ECO:0000303|PubMed:27231873};
DE EC=4.2.3.172 {ECO:0000269|PubMed:27231873};
DE AltName: Full=Tau-cadinol synthase {ECO:0000303|PubMed:27231873};
DE EC=4.2.3.173 {ECO:0000269|PubMed:27231873};
DE AltName: Full=Terpene synthase 1 {ECO:0000303|PubMed:27231873};
DE Short=IhsTPS1 {ECO:0000303|PubMed:27231873};
GN Name=TPS1 {ECO:0000303|PubMed:27231873};
OS Inula hupehensis (Inula helianthus-aquatilis subsp. hupehensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Asterales; Asteraceae; Asteroideae; Inuleae;
OC Inulinae; Inula.
OX NCBI_TaxID=1805964;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RX PubMed=27231873; DOI=10.1016/j.plaphy.2016.05.023;
RA Gou J.B., Li Z.Q., Li C.F., Chen F.F., Lv S.Y., Zhang Y.S.;
RT "Molecular cloning and functional analysis of a 10-epi-junenol synthase
RT from Inula hupehensis.";
RL Plant Physiol. Biochem. 106:288-294(2016).
CC -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC sesquiterpenes and sesquiterpenoid alcohols (PubMed:27231873). Converts
CC farnesyl diphosphate (FPP) to 10-epi-juneol (PubMed:27231873). Converts
CC FPP to tau-cadinol (PubMed:27231873). 10-epi-juneol is the major
CC product (PubMed:27231873). {ECO:0000269|PubMed:27231873}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = 10-epi-juneol +
CC diphosphate; Xref=Rhea:RHEA:14485, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:138037, ChEBI:CHEBI:175763;
CC EC=4.2.3.172; Evidence={ECO:0000269|PubMed:27231873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14486;
CC Evidence={ECO:0000269|PubMed:27231873};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = diphosphate + tau-
CC cadinol; Xref=Rhea:RHEA:54052, ChEBI:CHEBI:15377, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:138042, ChEBI:CHEBI:175763; EC=4.2.3.173;
CC Evidence={ECO:0000269|PubMed:27231873};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54053;
CC Evidence={ECO:0000269|PubMed:27231873};
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 -!- TISSUE SPECIFICITY: Highly expressed in leaves (PubMed:27231873).
CC Expressed in roots and flowers (PubMed:27231873).
CC {ECO:0000269|PubMed:27231873}.
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}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; KT218680; AMQ26035.1; -; mRNA.
DR AlphaFoldDB; A0A1L2D3T3; -.
DR SMR; A0A1L2D3T3; -.
DR KEGG; ag:AMQ26035; -.
DR BRENDA; 4.2.3.172; 15335.
DR BRENDA; 4.2.3.173; 15335.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010334; F:sesquiterpene synthase activity; IDA:UniProtKB.
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..563
FT /note="10-epi-juneol synthase"
FT /id="PRO_0000452460"
FT MOTIF 314..318
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 277
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 318
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 318
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 455
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 458
FT /ligand="(2E,6E)-farnesyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:175763"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 458
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 462
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 563 AA; 65177 MW; 85C1915C1214F019 CRC64;
MATQKSTTAL DAKSKMTTDL VRPLANFPSS IWGDRFMSLS IDKSELKTYD KVIEKQKQEL
RRLIIDPSMD SNKKLSLINS VYRLGLTYLF EEEIEGQLDK LFKEIDMQEA CNEADLYTIS
VNFQVFRQHG YKLSCNVFNK FKDYTSDHKF KEYIMADVRG MLGLYESTQL RIRGETILEE
AFAFTESQLK GVLDTLEGNI ARQVKHALTS PFHRGLRTVE ARIYFSNYEE ECSTYDSLQK
LANAHFNYLQ LQHKEELASV IKWGEDMDFK TITPYARDRI PDLYLWGLGL FSEPHYSQAR
ILISKMAQLI CVLDDTYDAY ATIDELHLLT NAINRWELSA TEQLPEYMKP LYKVLLNEHV
ELEKQLSSKG KSNFVNASKK AFQELAMGYL QEAEWRHNGK VPSFQEYLKN GLITSTYNVF
AKSSLICMSD IVTEEACTWY DSDPIILQAT GLLGRVYNDI STFQFERKRA QQQITSIEAY
MKTFGVPENV ALEELKKMVE IAWNDINKGC LNTNEISKKL LAPIVNLARM TDVIYRYNDK
FTFPEKTIEE YITLLFCESI PKN
