ID   CPS2_ISOJA              Reviewed;         800 AA.
AC   A0A5P8DHZ6;
DT   07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2020, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Copalyl diphosphate synthase 2, chloroplastic {ECO:0000303|Ref.1};
DE            Short=IjCPS2 {ECO:0000303|Ref.1};
DE            EC=5.5.1.12 {ECO:0000250|UniProtKB:A0A1X9IRP7};
DE   Flags: Precursor;
GN   Name=CPS2 {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 (+)-copalyl
CC       diphosphate ((+)-CPP) (By similarity).
CC       {ECO:0000250|UniProtKB:A0A1X9IRP7}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (+)-copalyl
CC         diphosphate; Xref=Rhea:RHEA:24316, ChEBI:CHEBI:58635,
CC         ChEBI:CHEBI:58756; EC=5.5.1.12;
CC         Evidence={ECO:0000250|UniProtKB:A0A1X9IRP7};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24317;
CC         Evidence={ECO:0000250|UniProtKB:A0A1X9IRP7};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q38802};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000250|UniProtKB:G8GJ95}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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; MK043034; QFP98578.1; -; mRNA.
DR   AlphaFoldDB; A0A5P8DHZ6; -.
DR   SMR; A0A5P8DHZ6; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050559; F: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:1901946; P:miltiradiene biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; ISS: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   2: Evidence at transcript level;
KW   Chloroplast; Isomerase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..38
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..800
FT                   /note="Copalyl diphosphate synthase 2, chloroplastic"
FT                   /id="PRO_0000452374"
FT   MOTIF           374..377
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000250|UniProtKB:G8GJ95"
FT   BINDING         242
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         374
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         376
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         461
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
SQ   SEQUENCE   800 AA;  91179 MW;  A0EE985F2B35D94E CRC64;
     MTSMSSLNLS NAPAVCRRSL PPAKLRLPEF STVYGWLNCS NKHEPLGYQI RRKQISKVTE
     CRVASLEASQ VGEKVGPAVR TPEEANKKIE ESIAYVKELL MTSGDGRISV APYDTSIVAL
     IKDKEGRDAP EFPSCLEWIA ENQMSDGSWG DEFFCIYDRV VNTLACVVAL KSWNVHADKI
     EKGVSYIKEN VHKLKDGNIE HMTSGFEIVI PAIIERAKAL GIQGLPYGDP IIKEIYTTKG
     RRLSKIPKDM IYKLPTTLLF SLEGLGDLDW EKILKLQSGD GSFLTSPSST AFAFMQTKDE
     KCYKFIENAV RNCNGGAPHT YPVDVFARLW AIDRLQRLGI SRFFQPEIKY FLDHINNVWT
     ENGVFSGRDS QFCDIDDTSM GIRLLKMHGY NIDPNALKHF KQEDGKFSCY GGQMIESASP
     IYNLYGAAQL RFPGEEILEE ATKFAYNFLQ EKIANNQIQE KWVISEHLID EIKLGLKMPW
     YATLPRVEAA YYFQYYAGTG DVWIGKTFYR MPEISNDTYK ELAVLDFNRC QAQHQFEWIY
     MQEWYQSSNV KAFGISKKEL LLAYFLAAAT IFEPERTQER IMWAKTQIVS RMIKSFLSEE
     NTLSLEQKTT LFVEFGHDIN GLNKINSVEK GNGLAGTLLT TFQQLLEEFD RYTTHQLKNA
     WSQWFVKLQQ GEGDGGADAE LLANTLNICA GHIAFNEDIL SHRDYTTLSS LTNKICRRLT
     QIQDKKILEI KDGSIKDKEM EEEMQALVKL VLEESESGGG IDRNIKQTFL SVFKTFYYCA
     YHHAETTDVH IFKVLFEPVV