ID   TPSD_OCIBA              Reviewed;         601 AA.
AC   Q5SBP0;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=Terpinolene synthase, chloroplastic;
DE            EC=4.2.3.113;
DE   Flags: Precursor;
GN   Name=TES;
OS   Ocimum basilicum (Sweet basil).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Ociminae;
OC   Ocimum.
OX   NCBI_TaxID=39350;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=15516500; DOI=10.1104/pp.104.051318;
RA   Iijima Y., Davidovich-Rikanati R., Fridman E., Gang D.R., Bar E.,
RA   Lewinsohn E., Pichersky E.;
RT   "The biochemical and molecular basis for the divergent patterns in the
RT   biosynthesis of terpenes and phenylpropenes in the peltate glands of three
RT   cultivars of basil.";
RL   Plant Physiol. 136:3724-3736(2004).
CC   -!- FUNCTION: Monoterpene synthase that catalyzes the formation of
CC       terpinolene and other monoterpenes from geranyl diphosphate.
CC       {ECO:0000269|PubMed:15516500}.
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:15516500};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsd 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; AY693650; AAV63792.1; -; mRNA.
DR   AlphaFoldDB; Q5SBP0; -.
DR   SMR; Q5SBP0; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; 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   SUPFAM; SSF48239; SSF48239; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..32
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           33..601
FT                   /note="Terpinolene synthase, chloroplastic"
FT                   /id="PRO_0000399255"
FT   MOTIF           354..358
FT                   /note="DDXXD motif"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         358
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         498
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         502
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         506
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   601 AA;  70000 MW;  0FBC6D323C29DB14 CRC64;
     MSTFVISNSM HVGISFSFLH KLPQTPPPQV VCCSGGLRLR PSCSLQLQPP PTTRRSGNYE
     PSAWDFNYLQ SLNNYHHKEE RYLRRQADLI EKVKMILKEE KMEALQQLEL IDDLRNLGLS
     YCFDDQINHI LTTIYNQHSC FHYHEAATSE EANLYFTALG FRLLREHGFK VSQEVFDRFK
     NEKGTDFRPD LVDDTQGLLQ LYEASFLLRE GEDTLEFARQ FATKFLQKKV EEKMIEEENL
     LSWTLHSLEL PLHWRIQRLE AKWFLDAYAS RPDMNPIIFE LAKLEFNIAQ ALQQEELKDL
     SRWWNDTGIA EKLPFARDRI VESHYWAIGT LEPYQYRYQR SLIAKIIALT TVVDDVYDVY
     GTLDELQLFT DAIRRWDIES INQLPSYMQL CYLAIYNFVS ELAYDIFRDK GFNSLPYLHK
     SWLDLVEAYF QEAKWYHSGY TPSLEQYLNI AQISVASPAI LSQIYFTMAG SIDKPVIESM
     YKYRHILNLS GILLRLPDDL GTASDELGRG DLAKAMQCYM KERNVSEEEA RDHVRFLNRE
     VSKQMNPARA ADDCPFTDDF VVAAANLGRV ADFMYVEGDG LGLQYPAIHQ HMAELLFHPY
     A