ID   TPS16_SOLHA             Reviewed;         405 AA.
AC   P0DO47;
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 16 {ECO:0000303|PubMed:21818683};
DE            Short=ShTPS16 {ECO:0000303|PubMed:21818683};
GN   Name=TPS16 {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], PATHWAY, AND GENE 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). 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}.
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; JN402398; -; NOT_ANNOTATED_CDS; mRNA.
DR   UniPathway; UPA00213; -.
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.
FT   CHAIN           1..405
FT                   /note="Sesquiterpene synthase 16"
FT                   /id="PRO_0000454688"
FT   MOTIF           155..159
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A1C9J6A7"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         155
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         159
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
SQ   SEQUENCE   405 AA;  47307 MW;  C4AE5FFD7AF22551 CRC64;
     MLSLYEAAQF RVHDEEILDE ALKFTTTHLK LILPELSNSL LAQQVGNALK FPIKDGVVRV
     EARKYISFYQ QNQNHNQVLL NFAKLDFNIL QMLHKKELCD ITRWWKELEI VKALPYVRDR
     LAEVYFWSLG VYFEPQYSTA RKILTKNISM ISLIDDTYDI YGTLDELTLF TEAIERWNID
     ASEQLQLPSY MKIIYCGLLD VYDEIKKDLA NENKSFLINY SIIEMKKMVM AYFQEATWYY
     GKTIPKMEQY MKNGISTSAY VQIAATSWLG MGNVATKDSF DWIVNEPPIL VASSIIARLL
     NDLLSHEEEQ KRGDAPSSVE CYMKEYGVTK EEAHIKIRNI IENSWKDLNE EYFKVNGTII
     PRVLLMCIIN LARVIEFIYK DEDAYTFSKN NLKDVVYRIL IDPII