ID   TPS14_TRIWF             Reviewed;         815 AA.
AC   A0A0M5L832;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   09-DEC-2015, sequence version 1.
DT   03-AUG-2022, entry version 23.
DE   RecName: Full=(-)-kolavenyl diphosphate synthase TPS14, chloroplastic {ECO:0000305};
DE            EC=5.5.1.28 {ECO:0000269|PubMed:26749264};
DE   AltName: Full=Terpene synthase 14 {ECO:0000303|PubMed:26749264};
DE            Short=TwTPS14 {ECO:0000303|PubMed:26749264};
DE   Flags: Precursor;
GN   Name=TPS14 {ECO:0000303|PubMed:26749264};
OS   Tripterygium wilfordii (Thunder God vine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Celastrales; Celastraceae; Tripterygium.
OX   NCBI_TaxID=458696;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND DXDD MOTIF.
RX   PubMed=26749264; DOI=10.1002/anie.201510650;
RA   Andersen-Ranberg J., Kongstad K.T., Nielsen M.T., Jensen N.B., Pateraki I.,
RA   Bach S.S., Hamberger B., Zerbe P., Staerk D., Bohlmann J., Moeller B.L.,
RA   Hamberger B.;
RT   "Expanding the landscape of diterpene structural diversity through
RT   stereochemically controlled combinatorial biosynthesis.";
RL   Angew. Chem. Int. Ed. 55:2142-2146(2016).
CC   -!- FUNCTION: Diterpene synthase that catalyzes the formation of (-)-
CC       kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP).
CC       {ECO:0000269|PubMed:26749264}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (-)-kolavenyl
CC         diphosphate; Xref=Rhea:RHEA:54684, ChEBI:CHEBI:58756,
CC         ChEBI:CHEBI:138310; EC=5.5.1.28;
CC         Evidence={ECO:0000269|PubMed:26749264};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54685;
CC         Evidence={ECO:0000269|PubMed:26749264};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:A0A1S5RW73};
CC   -!- ACTIVITY REGULATION: Inhibited by high concentrations of magnesium.
CC       {ECO:0000250|UniProtKB:A0A1S5RW73}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC       activity through binding to Mg(2+). {ECO:0000305|PubMed:26749264}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsc 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; KP889111; ALE19956.1; -; mRNA.
DR   AlphaFoldDB; A0A0M5L832; -.
DR   SMR; A0A0M5L832; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   Gene3D; 1.10.600.10; -; 1.
DR   Gene3D; 1.50.10.130; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
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; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Chloroplast; Isomerase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..51
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           52..815
FT                   /note="(-)-kolavenyl diphosphate synthase TPS14,
FT                   chloroplastic"
FT                   /id="PRO_0000447690"
FT   MOTIF           379..382
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000305|PubMed:26749264"
FT   BINDING         247
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         379
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         381
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         465
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
SQ   SEQUENCE   815 AA;  93935 MW;  9AB385D08694F490 CRC64;
     MFMSSSSSSH ARRPQLSSFS YLHPPLPFPG LSFFNTRDKR VNFDSTRIIC IAKSKPARTT
     PEYSDVLQTG LPLIVEDDIQ EQEEPLEVSL ENQIRQGVDI VKSMLGSMED GETSISAYDT
     AWVALVENIH HPGSPQFPSS LQWIANNQLP DGSWGDPDVF LAHDRLINTL ACVIALKKWN
     IHPHKCKRGL SFVKENISKL EKENEEHMLI GFEIAFPSLL EMAKKLGIEI PDDSPALQDI
     YTKRDLKLTR IPKDIMHNVP TTLLYSLEGL PSLDWEKLVK LQCTDGSFLF SPSSTACALM
     HTKDGNCFSY INNLVHKFNG GVPTVYPVDL FEHIWCVDRL QRLGISRFFH PEIKECLGYV
     HRYWTKDGIC WARNSRVQDI DDTAMGFRLL RLHGYEVSPD VFKQFRKGDE FVCFMGQSNQ
     AITGIYNLYR ASQMMFPEET ILEEAKKFSV NFLREKRAAS ELLDKWIITK DLPNEVGFAL
     DVPWYACLPR VETRLYIEQY GGQDDVWIGK TLYRMPYVNN NVYLELAKLD YNNCQSLHRI
     EWDNIQKWYE GYNLGGFGVN KRSLLRTYFL ATSNIFEPER SVERLTWAKT AILVQAIASY
     FENSREERIE FANEFQKFPN TRGYINGRRL DVKQATKGLI EMVFATLNQF SLDALVVHGE
     DITHHLYQSW EKWVLTWQEG GDRREGEAEL LVQTINLMAG HTHSQEEELY ERLFKLTNTV
     CHQLGHYHHL NKDKQPQQVE DNGGYNNSNP ESISKLQIES DMRELVQLVL NSSDGMDSNI
     KQTFLAVTKS FYYTAFTHPG TVNYHIAKVL FERVV