ID   TPS10_TRIWF             Reviewed;         815 AA.
AC   A0A1C7AAN2;
DT   31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 20.
DE   RecName: Full=(-)-kolavenyl diphosphate synthase TPS10, chloroplastic {ECO:0000305};
DE            EC=5.5.1.28 {ECO:0000269|PubMed:27801964};
DE   AltName: Full=Terpene synthase 10 {ECO:0000303|PubMed:27801964};
DE            Short=TwTPS10 {ECO:0000303|PubMed:27801964};
DE   Flags: Precursor;
GN   Name=TPS10 {ECO:0000303|PubMed:27801964};
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=27801964; DOI=10.1111/tpj.13410;
RA   Hansen N.L., Heskes A.M., Hamberger B., Olsen C.E., Hallstroem B.M.,
RA   Andersen-Ranberg J., Hamberger B.;
RT   "The terpene synthase gene family in Tripterygium wilfordii harbors a
RT   labdane-type diterpene synthase among the monoterpene synthase TPS-b
RT   subfamily.";
RL   Plant J. 89:429-441(2017).
CC   -!- FUNCTION: Diterpene synthase that catalyzes the formation of (-)-
CC       kolavenyl diphosphate from geranylgeranyl diphosphate (GGPP).
CC       {ECO:0000269|PubMed:27801964}.
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:27801964};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54685;
CC         Evidence={ECO:0000269|PubMed:27801964};
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:27801964}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsc subfamily.
CC       {ECO:0000305}.
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DR   EMBL; KU948708; ANO43021.1; -; mRNA.
DR   AlphaFoldDB; A0A1C7AAN2; -.
DR   SMR; A0A1C7AAN2; -.
DR   KEGG; ag:ANO43021; -.
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; IDA:UniProtKB.
DR   GO; GO:0016102; P:diterpenoid biosynthetic process; IDA:UniProtKB.
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..50
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           51..815
FT                   /note="(-)-kolavenyl diphosphate synthase TPS10,
FT                   chloroplastic"
FT                   /id="PRO_0000447689"
FT   MOTIF           379..382
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000305|PubMed:27801964"
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;  93441 MW;  F44EC6D66A9D3115 CRC64;
     MFMSSSSSSH ARRPQLSSFS YLHPPLPFPG LSFSSTRDKR VNFDSTRIIS IAKSKPARTT
     PEYSDVLQTG LPLIVEDDIQ EQEEPLEVSL ENQIRQGVDI VKSMLGSIED GEISISAYDT
     AWVALVENIH HPGSPQFPST LQWIANNQLP DSSWGDPDMF LTHDRLINTL ACVIALKKWN
     IHPRKCKRGL SFVKENISKL AKEDEEHMLI GFEIAFPSLL EMAKKLGIEI PDDCPAMQDI
     YTKKDLKLTR IPRDIMHNVP TTLLYSLEGL PSLDWEKLVK LQCQDGSFLF SPSSTACALM
     HTKDGNCFSY LNNLVHKFNG GVPNVYPVDL FEHIWSVDRL LRLGISRFFR PEIKECLEYV
     HRYWTKDGIC WARNSNVQDI DDTSMGFRLL RLHGYEVSPD VFKQFKKGNE FVCVVGQSDQ
     AITGIYNLYR ASQLMFPKET ILHGAKEFAG NFLRKKRTAN ELLDKWIITK DLPGEVGFAL
     DVPWYACLPR VETRLYIEQY GGQDDVWIGK TLYRMPYVNN NVYLELAKLD YNNCQSLHRI
     EWDNIQKWYE EYNVGGFGVS KRGLLKTYFV ATASIFEPER SVERLAWAKT AILVETIRSY
     FGNSREERIA FPNEFQKAKT RGYINGRRLD GKQATKGLIE MVFATLNHLS QDALVVHGQD
     ITPHLYQSWE KWVLTWQEGG DRGEGEAELL VQTINLMAGH THSQEEELLY ERLFKLTNTV
     CHQLGHYHHL NKDKQPQQVQ DNGGYNNSNP ESISKLQIES DMRELVQLVL NSSDGMDSNI
     KQTFLTVTKS FYYTAFTHPG TVNYHIAKVL FERVV