ID   CPS2_MARVU              Reviewed;         784 AA.
AC   A0A075F9Z3;
DT   22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT   29-OCT-2014, sequence version 1.
DT   03-AUG-2022, entry version 25.
DE   RecName: Full=ent-copalyl diphosphate synthase 2, chloroplastic {ECO:0000303|PubMed:24990389};
DE            Short=MvCPS2 {ECO:0000303|PubMed:24990389};
DE            EC=4.2.-.- {ECO:0000305|PubMed:24990389};
DE   Flags: Precursor;
GN   Name=CPS2 {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, PATHWAY, AND 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). May be involved in the conversion of
CC       geranylgeranyl diphosphate (GGPP) to ent-copalyl diphosphate (ent-CPP)
CC       and 8-hydroxycopalyl diphosphate (LPP, labda-13-en-8-ol diphosphate)
CC       (Probable). {ECO:0000305|PubMed:24990389}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:Q38802};
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC       {ECO:0000305|PubMed:24990389}.
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.
CC       {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}.
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; KJ584451; AIE77091.1; -; mRNA.
DR   AlphaFoldDB; A0A075F9Z3; -.
DR   SMR; A0A075F9Z3; -.
DR   UniPathway; UPA00213; -.
DR   UniPathway; UPA00390; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR   GO; GO:0009686; P:gibberellin 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   2: Evidence at transcript level;
KW   Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..57
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..784
FT                   /note="ent-copalyl diphosphate synthase 2, chloroplastic"
FT                   /id="PRO_0000449302"
FT   MOTIF           379..382
FT                   /note="DXDD motif"
FT                   /evidence="ECO:0000250|UniProtKB:A0A075FAK4"
FT   BINDING         242
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         466
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
SQ   SEQUENCE   784 AA;  89093 MW;  A5CA226176513B9B CRC64;
     MSMTLFASVT RPGLPGPTAL RFPETRHLFH SVTAFAASFS PSKSSVGSSQ CNATTPPAEY
     KEYTGNDLAK TTVDGIEKDI HSNKGLSDKT RELVMSIRSI LRTMEEGEIS MSPYDTAWVA
     MVEDIDGGGG PHFPSTLDWI SSNQLADGSW GDPIFLVYDR LINTFACVIA LTSWKMHPDK
     CDKAISFIRE NMYKLDDEKE ERMPIGFEMT FPPLVEKAKR LNINFPDDSP GLRKIYAQRD
     LKFKRIPWDK MHTVPTTLLY SLEGMALEAD VLDWQKLLKL QSPDGSLFYS PASTAFALQQ
     TGDHNCLQYL LKLVQTFNGG VPNLYPLDLY ERSWAVDRLQ RLGISRFFEP QIEECMKYVH
     RYWSNKNGVY AARHSDIQDI DDTSMGFRVL RLNGFDVSPD AFKQFEDDDG EFLCFIGQTN
     HSVSATYNLY RASQVMFPGE EILQRAKKFS TKFLQDKRAE NELLDKWVIT KDLPGEVGYA
     LDVPWYASLP RVEARFYIEQ YGGEDVAWIG KVLFRAPNVN NDNYLELAKL DYNDCQALHQ
     HEWKNIQQWY KSCGLRGFGL GEESLLLAYY IAAASVFEPE KSGERLAWAK TAALVKTITS
     QKLTKDQKHD FIREFEQGSI LENANGGRCG TSNKLVETIF TTVHKMSLET SSRDIHHQLL
     HAWRKWVVAW EVGGDGDAEL FVQTLNLTGG SSEPTPFCHP KYQQLLEVTT RICHQLRKST
     VKEIQVESDM QELVKLVVTK SSGDLDSDIK QKFLTIARSF YYAAHCSTEA IGFHIVKVLF
     ERLV