ID   CPS1_ISOJA              Reviewed;         711 AA.
AC   A0A5P8DI15;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   03-AUG-2022, entry version 10.
DE   RecName: Full=Ent-copalyl diphosphate synthase 1 {ECO:0000303|Ref.1};
DE            Short=IjCPS1 {ECO:0000303|Ref.1};
DE            EC=5.5.1.13 {ECO:0000250|UniProtKB:G3E4M6};
GN   Name=CPS1 {ECO:0000303|Ref.1};
OS   Isodon japonicus (Scutellaria japonica).
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=425908;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Ide Y., Yamamura Y., Lee J.-B.;
RL   Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the biosynthesis of ent-kaurene diterpenoids
CC       natural products such as oridonin, miltiradiene, eriocalyxin B and
CC       nezukol, known to exhibit antitumor, anti-inflammatory and
CC       antibacterial activities (By similarity). Catalyzes the conversion of
CC       (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl
CC       diphosphate (ent-CPP) (By similarity). {ECO:0000250|UniProtKB:G3E4M6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = ent-copalyl
CC         diphosphate; Xref=Rhea:RHEA:14841, ChEBI:CHEBI:58553,
CC         ChEBI:CHEBI:58756; EC=5.5.1.13;
CC         Evidence={ECO:0000250|UniProtKB:G3E4M6};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842;
CC         Evidence={ECO:0000250|UniProtKB:G3E4M6};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q40577};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000250|UniProtKB:G3E4M6}.
CC   -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC       activity, presumably through binding to Mg(2+). {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsc subfamily.
CC       {ECO:0000305}.
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DR   EMBL; MK043033; QFP98577.1; -; mRNA.
DR   AlphaFoldDB; A0A5P8DI15; -.
DR   SMR; A0A5P8DI15; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; ISS:UniProtKB.
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; ISS:UniProtKB.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; ISS: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; 2.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   2: Evidence at transcript level;
KW   Isomerase; Magnesium; Metal-binding.
FT   CHAIN           1..711
FT                   /note="Ent-copalyl diphosphate synthase 1"
FT                   /id="PRO_0000452378"
FT   MOTIF           277..280
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000250|UniProtKB:G3E4M6"
FT   BINDING         145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         277
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
SQ   SEQUENCE   711 AA;  81749 MW;  670A04637DCF15A9 CRC64;
     MLQSMGDGEI SISPYDTAWV ALVEDDGGGR RQPQFPSSLE WISSNQLADG SWGDAGTFSI
     FDRILNTLAC VVALRSWNIH PHKTEKGIWF MKKNMCRIDE ENLEHMPIGF EVALPSLIDI
     AKKLGIDIPT QTRGLQEIYA RREIKLKKIP RDIMHQAPTT LLHSLEGMAG LKWEKLLKLQ
     SEDGSFLFSP ASTAFALQQT RDHNCLKYLT NHIHKFNGGV PNVYPVDLFE HLWAVDRLQR
     LGLSRYFEPE IEECIAYVHR QWTEKGICWA RNSQVEDIDD TAMGFRLLRL HGYEVSADVF
     RHFKSDGGEF FCFKGQSTQA VTGMYNLYRA SQLMFPGENI LVDAARFSAN FLQLKRANND
     LFDKWIITKD LPGEVGYALD VPWYASLPRV ETRFYLDQYG GDDDVWIGKT LYRMPYVNNN
     KYLELAKLDY NNCQALHQQE WQNIQKWYRS CSLGEFGMTE RSLLQTYYVA AASVFEPEKS
     QERLAWAKTA ILMETITSHF EFQQLSRDQK RAFITEFEHD SILKYTNGGR YKRRSSLVGT
     LVRTLNHLSL DILLAHGRDI HQPLKNAWCK WLNSWEEGGD AELLVRTLNL MISGGGRRRR
     WASEELLSSN PKHEQLLKAT IGVCDKLRLF QRRKVQGGNG CMNATGITTV EIESEMRELV
     KLVVTRSSSE DLDSEIKQNF LTIARSFYYA AYCNQGTINF HIAKVLFEKV L