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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}.
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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
 
 
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