ID   TPS6_ISORU              Reviewed;         681 AA.
AC   A0A1W6QDI6;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2017, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=Terpene synthase 6, chloroplastic {ECO:0000303|PubMed:28445526};
DE            Short=IrTPS6 {ECO:0000303|PubMed:28445526};
DE            EC=4.2.3.- {ECO:0000250|UniProtKB:A0A1Z3GBK8};
DE   Flags: Fragment;
GN   Name=TPS6 {ECO:0000303|PubMed:28445526};
OS   Isodon rubescens (Rabdosia rubescens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Ocimeae; Isodoninae;
OC   Isodon.
OX   NCBI_TaxID=587669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, AND TISSUE SPECIFICITY.
RX   PubMed=28445526; DOI=10.1371/journal.pone.0176507;
RA   Pelot K.A., Hagelthorn L.M., Addison J.B., Zerbe P.;
RT   "Biosynthesis of the oxygenated diterpene nezukol in the medicinal plant
RT   Isodon rubescens is catalyzed by a pair of diterpene synthases.";
RL   PLoS ONE 12:e0176507-e0176507(2017).
CC   -!- FUNCTION: May be involved in the biosynthesis of ent-kaurene
CC       diterpenoids natural products such as oridonin, miltiradiene,
CC       eriocalyxin B and nezukol, known to exhibit antitumor, anti-
CC       inflammatory and antibacterial activities.
CC       {ECO:0000305|PubMed:28445526}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q40577};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:28445526}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC       {ECO:0000250|UniProtKB:A0A0U4CDK4}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:28445526}.
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:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; KY661362; ARO38145.1; -; mRNA.
DR   AlphaFoldDB; A0A1W6QDI6; -.
DR   SMR; A0A1W6QDI6; -.
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   GO; GO:1901946; P:miltiradiene biosynthetic process; IDA:UniProtKB.
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; 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   2: Evidence at transcript level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid.
FT   CHAIN           <1..681
FT                   /note="Terpene synthase 6, chloroplastic"
FT                   /id="PRO_0000452383"
FT   MOTIF           433..437
FT                   /note="DDXXD motif"
FT                   /evidence="ECO:0000305"
FT   BINDING         433
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         433
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         437
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         437
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         577
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   BINDING         585
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250|UniProtKB:Q40577"
FT   NON_TER         1
FT                   /evidence="ECO:0000312|EMBL:ARO38145.1"
SQ   SEQUENCE   681 AA;  78191 MW;  4E3F611F61AA3D29 CRC64;
     LLNKDVLSST LASILALHKW GLGQHHIAKG LHFLELNFAS ATDNSQITPL GFDIVFPAML
     DHAADLSLNL RLDPTTLNDL MNRRDLELQR CTENGSAETE VYMAYIGEGM GKLHDWESVM
     KYQRKNGSLF NSPSTTAAAF IALRNSDCLN YLYSALNKFG SAVPAVYPLD IYSQLCIVDN
     LERLGISRFF STEIQSVLDE TYRCWLQGDE EIFMDASTCG LAFRTLRMNG YNVTSDPITK
     ILQECFSSSF RGNMTDINTT LEIYRASELI LYPEERDLDQ HNLRLKTFLE QELSSNGFIQ
     SCQLGRNINA EVNQAIEYPF YAIMDRMAKR KNIENYNIDN TRILKTSYRS PNFGNKDFLS
     LSVEDFNRCQ VIHREELREL ERWVIENRLD ELKFARSKAA YCYFSAAATI FSPELSDARM
     SWAKNALMTT MVDDLFDVTG SVEEMKNLIQ LVELWDVDVS TECCSHKVQI LFSALKRTIC
     EVGDRAYQLQ GRSIRSHIIV IWLDTLHSMM KEVEWTRDKF VPTMDEYVSN AYVSFALGPI
     VLPALYLVGP KLSEEMVNHS EYHNLFKLMS TCGRLMNDIR GYEREHDDGK LNAMSLYIMN
     NGGEITPEVA ILEIKSWNDR QRRDLLSLVL EEKSVIPKAC KDLFWHMCSV VHLFYNKDDG
     FWSQELIEVV NQVIHQPILL N