ID   KSA_PEA                 Reviewed;         801 AA.
AC   O04408;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Ent-copalyl diphosphate synthase, chloroplastic;
DE            Short=Ent-CDP synthase;
DE            EC=5.5.1.13;
DE   AltName: Full=Ent-copalyl diphosphate synthase;
DE   AltName: Full=Ent-kaurene synthase A;
DE            Short=KSA;
DE   Flags: Precursor;
OS   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9107034; DOI=10.1046/j.1365-313x.1997.11030443.x;
RA   Ait-Ali T., Swain S.M., Reid J.B., Sun T.-P., Kamiya Y.;
RT   "The LS locus of pea encodes the gibberellin biosynthesis enzyme ent-
RT   kaurene synthase A.";
RL   Plant J. 11:443-454(1997).
CC   -!- FUNCTION: Catalyzes the conversion of geranylgeranyl diphosphate to the
CC       gibberellin precursor ent-copalyl diphosphate.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC   -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC       activity, presumably through binding to Mg(2+).
CC   -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR   EMBL; U63652; AAB58822.1; -; mRNA.
DR   PIR; T06783; T06783.
DR   AlphaFoldDB; O04408; -.
DR   SMR; O04408; -.
DR   UniPathway; UPA00390; -.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009905; F:ent-copalyl diphosphate synthase activity; IEA:UniProtKB-EC.
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   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   Chloroplast; Isomerase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..801
FT                   /note="Ent-copalyl diphosphate synthase, chloroplastic"
FT                   /id="PRO_0000033624"
FT   MOTIF           373..376
FT                   /note="DXDD motif"
FT   BINDING         241
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
FT   BINDING         373
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         375
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT   BINDING         459
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q38802"
SQ   SEQUENCE   801 AA;  92718 MW;  5CB88ADE00366844 CRC64;
     MFTHFSTHFH LPSSSSLFFL HPFYKSSSLG AVSFVAKDKE KRCRAISKSR TQEYEGVFQT
     NVATLKLSEI NVEDVIVIDD EEEQDIRVGL VNKIKSILSS LEDGEITISA YDTAWVALVE
     DVNAISTPQF PSSLEWIAKN QLQDGSWGDS RLFSAHDRII NTLACVIALR SWNMHSEKCD
     KGMIFFRENL SKLENENEEH MPIGFEVAFP SLLEGARGIK PLMCPNDSPI LKNIFEKRDE
     KLTRIPKEIM HKVPTTLLHS LEGMSGLDWK QLLKLQSQDG SFLFSPSSTA FALMQTKDGN
     CLKYLNNVVK KFNGGVPNVY PVDLFEHIWV VDRLERLGIS RFFRHEIKDC MNYVSKIWSE
     KGICWARNSN VQDIDDTAMA FRLLRLHGHQ VSAHVFKHFE RNGEFFCFAG QCTQAVTGMY
     NLFRASQVLF PGEKILEHAK HFSAKVLKEK REANELIDKW IIMKNLPEEV GYALDMPWYA
     NLDRIETRFY IDQYGAESDV WIGKTLYRMA YVNNNNYLEL AKLDYNNCQA QHLIEWNVIQ
     TWYLESRLGE FGLSKRDLLL AYFLATGSIF EPERSHERLA WAKTTALLET IKCYVRNEDL
     RKDFAKKFND HIDVRDYSIA RRMKRNKTEH ELVESLFATI GEISWDVRLS YGHEIGYDMH
     QCWKKWLSSW QSEGDKCEGE AELLIQIINL CSNHWISEGP SMQSTIQHLL QLTNSICHKL
     SCYQKDKELK GISCQENITN SEVESKMQEL VQMVFQKCPN DIDFNVKNTF FTIAKSFYYA
     AFCDSRTINF HIAKVLFEKV V