TPS17_SOLHA
ID TPS17_SOLHA Reviewed; 554 AA.
AC G8H5N0;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 1.
DT 03-AUG-2022, entry version 38.
DE RecName: Full=Terpene synthase 17 {ECO:0000303|PubMed:21818683};
DE Short=ShTPS17 {ECO:0000303|PubMed:21818683};
DE AltName: Full=(+)-valencene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.73 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(E)-beta-farnesene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.47 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(E)-beta-ocimene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.106 {ECO:0000269|PubMed:21818683};
DE AltName: Full=(E)-gamma-bisabolene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=(Z)-beta-ocimene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=(Z)-gamma-bisabolene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Alpha-bergamotene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.54 {ECO:0000269|PubMed:21818683};
DE EC=4.2.3.81 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-bisabolene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Beta-myrcene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.15 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Gamma-gurjunene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Gamma-terpinene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.114 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Limonene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Terpinolene synthase TPS17 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.113 {ECO:0000269|PubMed:21818683};
GN Name=TPS17 {ECO:0000303|PubMed:21818683};
OS Solanum habrochaites (Wild tomato) (Lycopersicon hirsutum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=62890;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND GENE
RP FAMILY.
RC STRAIN=cv. PI127826;
RX PubMed=21818683; DOI=10.1007/s11103-011-9813-x;
RA Bleeker P.M., Spyropoulou E.A., Diergaarde P.J., Volpin H., De Both M.T.J.,
RA Zerbe P., Bohlmann J., Falara V., Matsuba Y., Pichersky E., Haring M.A.,
RA Schuurink R.C.;
RT "RNA-seq discovery, functional characterization, and comparison of
RT sesquiterpene synthases from Solanum lycopersicum and Solanum habrochaites
RT trichomes.";
RL Plant Mol. Biol. 77:323-336(2011).
CC -!- FUNCTION: Sesquiterpene synthase involved in the biosynthesis of
CC volatile compounds (PubMed:21818683). Mediates the conversion of
CC (2E,6E)-farnesyl diphosphate (FPP) into gamma-gurjunene, (E)-beta-
CC farnesene and (+)-valencene, and of (2Z,6Z)-farnesyl diphosphate ((ZZ)-
CC FPP) into (E)-alpha-bergamotene and (Z)-gamma-bisabolene as well as
CC beta-bisabolene, (Z)-alpha-bergamotene and (E)-gamma-bisabolene to a
CC lower extent (PubMed:21818683). Can act with a low efficiency as a
CC monoterpene synthase with geranyl diphosphate (GPP) as substrate, thus
CC producing beta-myrcene, (E)-beta-ocimene, limonene, terpinolene, gamma-
CC terpinene and (Z)-beta-ocimene (PubMed:21818683).
CC {ECO:0000269|PubMed:21818683}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (+)-valencene + diphosphate;
CC Xref=Rhea:RHEA:29511, ChEBI:CHEBI:33019, ChEBI:CHEBI:61700,
CC ChEBI:CHEBI:175763; EC=4.2.3.73;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29512;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (E)-beta-farnesene +
CC diphosphate; Xref=Rhea:RHEA:27425, ChEBI:CHEBI:10418,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:175763; EC=4.2.3.47;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27426;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + gamma-gurjunene;
CC Xref=Rhea:RHEA:68400, ChEBI:CHEBI:33019, ChEBI:CHEBI:175763,
CC ChEBI:CHEBI:178033; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68401;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = beta-bisabolene + diphosphate;
CC Xref=Rhea:RHEA:68524, ChEBI:CHEBI:33019, ChEBI:CHEBI:49249,
CC ChEBI:CHEBI:60374; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68525;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (E)-gamma-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:68468, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49239, ChEBI:CHEBI:60374;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68469;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + limonene;
CC Xref=Rhea:RHEA:68640, ChEBI:CHEBI:15384, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68641;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = beta-myrcene + diphosphate;
CC Xref=Rhea:RHEA:16965, ChEBI:CHEBI:17221, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.15;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16966;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = (E)-beta-ocimene + diphosphate;
CC Xref=Rhea:RHEA:32691, ChEBI:CHEBI:33019, ChEBI:CHEBI:58057,
CC ChEBI:CHEBI:64280; EC=4.2.3.106;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32692;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + terpinolene;
CC Xref=Rhea:RHEA:25500, ChEBI:CHEBI:9457, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.113;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25501;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate = diphosphate + gamma-terpinene;
CC Xref=Rhea:RHEA:32559, ChEBI:CHEBI:10577, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58057; EC=4.2.3.114;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:32560;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (Z)-gamma-bisabolene +
CC diphosphate; Xref=Rhea:RHEA:68788, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:49238, ChEBI:CHEBI:60374;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68789;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = (1S,5S,6R)-alpha-bergamotene +
CC diphosphate; Xref=Rhea:RHEA:31427, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:62756, ChEBI:CHEBI:175763; EC=4.2.3.81;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31428;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2Z,6Z)-farnesyl diphosphate = (1S,5S,6S)-alpha-bergamotene +
CC diphosphate; Xref=Rhea:RHEA:30471, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:60374, ChEBI:CHEBI:61679; EC=4.2.3.54;
CC Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30472;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:A0A1C9J6A7};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1C9J6A7};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:21818683}.
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|UniProtKB:Q40577}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JN402391; AEM23828.1; -; mRNA.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid 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..554
FT /note="Terpene synthase 17"
FT /id="PRO_0000454689"
FT MOTIF 306..310
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 306
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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"
SQ SEQUENCE 554 AA; 64892 MW; AFCA0A1153820E4D CRC64;
MELCTQTVAA DHEVIITRRS GSHHPTLWGD HFLAYADLRG ANEGEEKQNE DLKEEVRKML
VMAPSNSLEK LELINTIQCL GLAYHFQSEI DESLSYMYTH YEEYSIGDLH AIALCFRLLR
QQGYYVSCDA FKKFTNDQGN FKEELVKDVE GMLSLYEAAQ FRVHGEQILD EALNFTITKL
KQILPKLSNS QLAQQITNAL KFPIKDGIVR VETRKYISFY QQNQNHNQVL LNFAKLDFNI
LQTLHKKELS DMTRWWKKME LVNTLPYARD RLVECYFWCL GTYFEPQYSV ARKMLTKISF
FISIIDDTYD IYGKLDELTL FTQAIERWNI DASEQLPLYM KIIYRDLLDV YDEIEKELAN
ENKSFLVNYS INEMKKVVRG YFQEAKWYYG KKVPKMEQYM KNAISTSAYI LLTTTSWLAM
GNVATKDVFD WVATEPKLVV ASCHIIRLLN DLVSHEEEQK RGNAASAVEC YMNEYSVTQE
EAHVKIRDII ENYWKDLNEE YFKVDMIIIP RVLLMCIINL TRVAEFIYKD EDAYTFSKNN
LKDVISDILV DPII