ID   CPS3_MARVU              Reviewed;         785 AA.
AC   A0A075FA51;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=(+)-copalyl diphosphate synthase 3, chloroplastic {ECO:0000303|PubMed:24990389};
DE            Short=MvCPS3 {ECO:0000303|PubMed:24990389};
DE            EC=5.5.1.12 {ECO:0000269|PubMed:24990389};
DE   Flags: Precursor;
GN   Name=CPS3 {ECO:0000303|PubMed:24990389};
OS   Marrubium vulgare (White horehound).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Lamiaceae; Lamioideae; Marrubieae; Marrubium.
OX   NCBI_TaxID=41230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=24990389; DOI=10.1111/tpj.12589;
RA   Zerbe P., Chiang A., Dullat H., O'Neil-Johnson M., Starks C., Hamberger B.,
RA   Bohlmann J.;
RT   "Diterpene synthases of the biosynthetic system of medicinally active
RT   diterpenoids in Marrubium vulgare.";
RL   Plant J. 79:914-927(2014).
CC   -!- FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid
CC       including marrubiin and other labdane-related furanoid diterpenoids
CC       with potential applications as anti-diabetics, analgesics or
CC       vasorelaxants (Probable). Terpene synthase that produces (+)-copalyl
CC       diphosphate ((+)-CPP) from geranylgeranyl diphosphate (GGPP)
CC       (PubMed:24990389). {ECO:0000269|PubMed:24990389,
CC       ECO:0000305|PubMed:24990389}.
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:0000269|PubMed:24990389};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24317;
CC         Evidence={ECO:0000269|PubMed:24990389};
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:0000305|PubMed:24990389}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Present in both leaves and flowers, with higher
CC       levels in leaves. {ECO:0000269|PubMed:24990389}.
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. {ECO:0000305}.
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DR   EMBL; KJ584452; AIE77092.1; -; mRNA.
DR   AlphaFoldDB; A0A075FA51; -.
DR   SMR; A0A075FA51; -.
DR   BRENDA; 5.5.1.12; 15343.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0050559; F:copalyl diphosphate synthase activity; IDA:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..785
FT                   /note="(+)-copalyl diphosphate synthase 3, chloroplastic"
FT                   /id="PRO_0000449303"
FT   MOTIF           371..374
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A075FAK4"
FT   BINDING         238
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         371
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         373
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         457
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
SQ   SEQUENCE   785 AA;  90197 MW;  6F5A85BCE60EA537 CRC64;
     MGSLSTLNLI KTCVTLASSE KLNQPSQCYT ISTCMKSSNN PPFNYYQING RKKMSTAIDS
     SVNAPPEQKY NSTALEHDTE IIEIEDHIEC IRRLLRTAGD GRISVSPYDT AWIALIKDLD
     GHDSPQFPSS MEWVADNQLP DGSWGDEHFV CVYDRLVNTI ACVVALRSWN VHAHKCEKGI
     KYIKENVHKL EDANEEHMTC GFEVVFPALL QRAQSMGIKG IPYNAPVIEE IYNSREKKLK
     RIPMEVVHKV ATSLLFSLEG LENLEWEKLL KLQSPDGSFL TSPSSTAFAF IHTKDRKCFN
     FINNIVHTFK GGAPHTYPVD IFGRLWAVDR LQRLGISRFF ESEIAEFLSH VHRFWSDEAG
     VFSGRESVFC DIDDTSMGLR LLRMHGYHVD PNVLKNFKQS DKFSCYGGQM MECSSPIYNL
     YRASQLQFPG EEILEEANKF AYKFLQEKLE SNQILDKWLI SNHLSDEIKV GLEMPWYATL
     PRVETSYYIH HYGGGDDVWI GKTLYRMPEI SNDTYRELAR LDFRRCQAQH QLEWIYMQRW
     YESCRMQEFG ISRKEVLRAY FLASGTIFEV ERAKERVAWA RSQIISHMIK SFFNKETTSS
     DQKQALLTEL LFGNISASET EKRELDGVVV ATLRQFLEGF DIGTRHQVKA AWDVWLRKVE
     QGEAHGGADA ELCTTTLNTC ANQHLSSHPD YNTLSKLTNK ICHKLSQIQH QKEMKGGIKA
     KCSINNKEVD IEMQWLVKLV LEKSGLNRKA KQAFLSIAKT YYYRAYYADQ TMDAHIFKVL
     FEPVV