ID   TPS15_SOLLC             Reviewed;         430 AA.
AC   P0DO46;
DT   23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT   23-FEB-2022, sequence version 1.
DT   03-AUG-2022, entry version 3.
DE   RecName: Full=Sesquiterpene synthase 15 {ECO:0000303|PubMed:21818683};
DE            Short=SlTPS15 {ECO:0000303|PubMed:21818683};
GN   Name=TPS15 {ECO:0000303|PubMed:21818683};
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], PATHWAY, 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: Sesquiterpene synthase involved in the biosynthesis of
CC       volatile compounds (PubMed:21818683). No activity detected with geranyl
CC       diphosphate (GPP) and farnesyl diphosphate (FPP) as substrates
CC       (PubMed:21818683). {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; JN402399; -; NOT_ANNOTATED_CDS; mRNA.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000004994; Unplaced.
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   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   2: Evidence at transcript level;
KW   Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..430
FT                   /note="Sesquiterpene synthase 15"
FT                   /id="PRO_0000454692"
FT   MOTIF           182..186
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         182
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         186
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         335
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   430 AA;  50184 MW;  635AD8841D1F0852 CRC64;
     MSHLDVFRKF TDDQGNYNKE LVNDTHGLLS LYEAAQFRVH DEEILDEAIN FTTTHLKLLL
     PKLSNSLSMQ VSYALKYPIN KTIARVATRK YISFYQEEES SCDQVLINFA KLDFSILQKM
     HKRELCDITR WWKELDLANE LAFARDRVVE LYFWCLGVYF EPQYKVARNI LTKVLCFVSI
     TDDIYDTYGT LHELTLLTNA IERWNLDATE NLTSYMKLFY TGLLHFYNEV EKELEKENKS
     FRVNFAISEM KKLVRAYFQE AKWYHGNTVP KMEEEYMKNG IQSSANPTLA TASWLGMGDE
     ATKEAFEWIS TEPPILVASS NIARLLNDIV SHEREIERGD VASSIECYMN EYGATKEEAY
     MEIRKIIENN WKDLNRGCLK PTTVPRVLLM PVLNLTRVAE FVYKDEDAYT FSKNNLKEVI
     SMVLDDPIEE