TPS9_SOLLC
ID TPS9_SOLLC Reviewed; 548 AA.
AC O64961; G1JUH6; O64962;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Sesquiterpene synthase 9 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE Short=SlTPS9 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
DE Short=Terpene synthase 9 {ECO:0000303|PubMed:21813655};
DE AltName: Full=Beta-myrcene synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.15 {ECO:0000269|PubMed:21818683};
DE AltName: Full=Germacrene C synthase TPS9 {ECO:0000303|PubMed:21818683, ECO:0000303|PubMed:9482865};
DE EC=4.2.3.60 {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865};
DE AltName: Full=Limonene synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.- {ECO:0000269|PubMed:21818683};
DE AltName: Full=Sesquiterpene synthase 1 {ECO:0000303|PubMed:11090225};
DE AltName: Full=Terpinolene synthase TPS9 {ECO:0000303|PubMed:21818683};
DE EC=4.2.3.113 {ECO:0000269|PubMed:21818683};
GN Name=TPS9 {ECO:0000303|PubMed:21813655, ECO:0000303|PubMed:21818683};
GN Synonyms=SSTLE1 {ECO:0000303|PubMed:11090225};
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
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=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND
RP PATHWAY.
RC STRAIN=cv. VFNT Cherry; TISSUE=Epidermis;
RX PubMed=9482865; DOI=10.1073/pnas.95.5.2216;
RA Colby S.M., Crock J., Dowdle-Rizzo B., Lemaux P.G., Croteau R.;
RT "Germacrene C synthase from Lycopersicon esculentum cv. VFNT cherry tomato:
RT cDNA isolation, characterization, and bacterial expression of the multiple
RT product sesquiterpene cyclase.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:2216-2221(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. E6203;
RX PubMed=11090225; DOI=10.1105/tpc.12.11.2283;
RA van Der Hoeven R.S., Monforte A.J., Breeden D., Tanksley S.D.,
RA Steffens J.C.;
RT "Genetic Control and Evolution of Sesquiterpene Biosynthesis in
RT Lycopersicon esculentum and Lycopersicon hirsutum.";
RL Plant Cell 12:2283-2294(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. M82;
RX PubMed=21813655; DOI=10.1104/pp.111.179648;
RA Falara V., Akhtar T.A., Nguyen T.T.H., Spyropoulou E.A., Bleeker P.M.,
RA Schauvinhold I., Matsuba Y., Bonini M.E., Schilmiller A.L., Last R.L.,
RA Schuurink R.C., Pichersky E.;
RT "The tomato terpene synthase gene family.";
RL Plant Physiol. 157:770-789(2011).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE SPECIFICITY, AND GENE FAMILY.
RC STRAIN=cv. Moneymaker;
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: Involved in the biosynthesis of germacrene C, one of the most
CC abundant sesquiterpene in the leaf oil of tomato (PubMed:11090225).
CC Produces mainly germacrene C, but also smaller amounts of germacrene A,
CC B and D when used with farnesyl diphosphate (FPP) as substrate; able to
CC use both (2E,6E)-farnesyl diphosphate ((EE)-FPP) and (2Z,6Z)-farnesyl
CC diphosphate ((ZZ)-FPP) (PubMed:9482865, PubMed:21818683). No or low
CC activity with geranylgeranyl diphosphate (GGPP) (PubMed:9482865). Can
CC act with a low efficiency as a monoterpene synthase with geranyl
CC diphosphate (GPP) as substrate, thus producing beta-myrcene, limonene
CC and terpinolene (PubMed:21818683, PubMed:9482865).
CC {ECO:0000269|PubMed:11090225, ECO:0000269|PubMed:21818683,
CC ECO:0000269|PubMed:9482865}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate = diphosphate + germacrene C;
CC Xref=Rhea:RHEA:28302, ChEBI:CHEBI:33019, ChEBI:CHEBI:61478,
CC ChEBI:CHEBI:175763; EC=4.2.3.60;
CC Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28303;
CC Evidence={ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865};
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 + 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=(2Z,6Z)-farnesyl diphosphate = diphosphate + germacrene C;
CC Xref=Rhea:RHEA:68772, ChEBI:CHEBI:33019, ChEBI:CHEBI:60374,
CC ChEBI:CHEBI:61478; Evidence={ECO:0000269|PubMed:21818683};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68773;
CC Evidence={ECO:0000269|PubMed:21818683};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:9482865};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:9482865};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit.
CC {ECO:0000305|PubMed:9482865};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:21818683, ECO:0000269|PubMed:9482865}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Mostly expressed in stem and trichomes, to a lower
CC extent in roots, leaves and flowers and, at low levels, in fruits.
CC {ECO:0000269|PubMed:21813655, 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:A0A1C9J6A7}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC {ECO:0000305}.
CC -!- CAUTION: It is unclear whether AAC39431 and AAC39432 represent
CC different alleles or different products derived from two germacrene C
CC synthase loci. {ECO:0000305}.
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DR EMBL; AF035630; AAC39431.1; -; mRNA.
DR EMBL; AF035631; AAC39432.1; -; mRNA.
DR EMBL; AF279453; AAG41889.1; -; mRNA.
DR EMBL; JN408289; AEM05858.1; -; Genomic_DNA.
DR PIR; T06265; T06265.
DR PIR; T06266; T06266.
DR RefSeq; NP_001234055.1; NM_001247126.2.
DR AlphaFoldDB; O64961; -.
DR SMR; O64961; -.
DR PRIDE; O64961; -.
DR EnsemblPlants; Solyc06g059885.1.1; Solyc06g059885.1.1; Solyc06g059885.1.
DR GeneID; 543549; -.
DR Gramene; Solyc06g059885.1.1; Solyc06g059885.1.1; Solyc06g059885.1.
DR KEGG; sly:543549; -.
DR InParanoid; O64961; -.
DR OMA; PSKMKID; -.
DR OrthoDB; 360509at2759; -.
DR BioCyc; MetaCyc:MON-13579; -.
DR UniPathway; UPA00213; -.
DR Proteomes; UP000004994; Chromosome 6.
DR ExpressionAtlas; O64961; baseline.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0102904; F:germacrene C synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0050551; F:myrcene synthase activity; IEA:RHEA.
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 Cytoplasm; Lyase; Magnesium; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..548
FT /note="Sesquiterpene synthase 9"
FT /id="PRO_0000412239"
FT MOTIF 300..304
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 300
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 304
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
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"
FT CONFLICT 497
FT /note="F -> S (in Ref. 1; AAC39432)"
FT /evidence="ECO:0000305"
FT CONFLICT 528..529
FT /note="TN -> ST (in Ref. 1; AAC39432)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="S -> P (in Ref. 1; AAC39432)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 64115 MW; 8D3DC5336AF0B127 CRC64;
MAASSADKCR PLANFHPSVW GYHFLSYTHE ITNQEKVEVD EYKETIRKML VETCDNSTQK
LVLIDAMQRL GVAYHFDNEI ETSIQNIFDA SSKQNDNDNN LYVVSLRFRL VRQQGHYMSS
DVFKQFTNQD GKFKETLTND VQGLLSLYEA SHLRVRNEEI LEEALTFTTT HLESIVSNLS
NNNNSLKVEV GEALTQPIRM TLPRMGARKY ISIYENNDAH HHLLLKFAKL DFNMLQKFHQ
RELSDLTRWW KDLDFANKYP YARDRLVECY FWILGVYFEP KYSRARKMMT KVLNLTSIID
DTFDAYATFD ELVTFNDAIQ RWDANAIDSI QPYMRPAYQA LLDIYSEMEQ VLSKEGKLDR
VYYAKNEMKK LVRAYFKETQ WLNDCDHIPK YEEQVENAIV SAGYMMISTT CLVGIEEFIS
HETFEWLMNE SVIVRASALI ARAMNDIVGH EDEQERGHVA SLIECYMKDY GASKQETYIK
FLKEVTNAWK DINKQFFRPT EVPMFVLERV LNLTRVADTL YKEKDTYTNA KGKLKNMINS
ILIESVKI
