CPS1_ISOER
ID CPS1_ISOER Reviewed; 710 AA.
AC G3E4M6;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Ent-copalyl diphosphate synthase 1 {ECO:0000303|PubMed:22284743};
DE Short=IeCPS1 {ECO:0000303|PubMed:22284743};
DE EC=5.5.1.13 {ECO:0000269|PubMed:22284743};
GN Name=CPS1 {ECO:0000303|PubMed:22284743};
OS Isodon eriocalyx (Plectranthus eriocalyx).
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=662907;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22284743; DOI=10.1016/j.phytochem.2011.12.021;
RA Li J.-L., Chen Q.-Q., Jin Q.-P., Gao J., Zhao P.-J., Lu S., Zeng Y.;
RT "IeCPS2 is potentially involved in the biosynthesis of pharmacologically
RT active Isodon diterpenoids rather than gibberellin.";
RL Phytochemistry 76:32-39(2012).
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, and in the production of gibberellins
CC phytohormones (PubMed:22284743). Catalyzes the conversion of
CC (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl
CC diphosphate (ent-CPP) (PubMed:22284743). {ECO:0000269|PubMed:22284743}.
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:0000269|PubMed:22284743};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842;
CC Evidence={ECO:0000269|PubMed:22284743};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000269|PubMed:22284743}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:22284743}.
CC -!- TISSUE SPECIFICITY: Expressed in germinating seeds and leaves.
CC {ECO:0000269|PubMed:22284743}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in germinating seeds as well as in
CC leaves. {ECO:0000269|PubMed:22284743}.
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; HQ455833; AEP03177.1; -; mRNA.
DR AlphaFoldDB; G3E4M6; -.
DR SMR; G3E4M6; -.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00390; -.
DR GO; GO:0009905; F:ent-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:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:1901946; P:miltiradiene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA: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 1: Evidence at protein level;
KW Isomerase; Magnesium; Metal-binding.
FT CHAIN 1..710
FT /note="Ent-copalyl diphosphate synthase 1"
FT /id="PRO_0000452377"
FT MOTIF 277..280
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
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 710 AA; 81645 MW; 7C22C641C0F862A4 CRC64;
MLQSMGDGEI SISPYDTAWV ALVEDDGGGR RQPQFPSSLE WISSNQLADG SWGDAGTFSI
FDRILNTLAC VVALRSWNIH PHKTDKGIWF MKKNMCRIDE ENLEHMPIGF EVALPSLIDI
AKKLEIDIPT QTRGLQEIYA RREIKLKKIP RDIMHQVPTT LLHSLEGMAG LKWEKLLKLQ
SQDGSFLFSP SSTAFALQQT RDHGCLKYLT NHIHKFNGGV PNVYPVDLFE HLWAVDRLQR
LGLSRYFQPE IEECIAYVHR QWTEKGICWA RNSQVEDIDD TAMGFRLLRL HGYEVSADVF
RHFKSDGGEF FCFKGQSTQA VTGMYNLYRA SQLMFPGENI LVDAARFSAN FLQLKRANND
LLDKWIITKD LPGEVGYALD VPWYASLPRV ETRFYLDQYG GDDDVWIGKT LYRMPYVNNN
KYLELAKLDY NNCQALHQQE WQNIQKWYRS CSLGEFGMTE RSLLQTYYVA AASVFEPEKS
QERLAWAKTA ILMETISSHF EFQQLSRDQK RAFITEFEHD SILKYTNGGR YKRRSSLVGT
LVRTLNHLSL DILLAHGRDI HQPLKNAWCK WLNSWEEGGD AELLLRTLNL MSGGGRRRRW
ASEELLSSNP KHEQLLKATI GVCDKLRLFQ RRKVQGGNGC MNATGITTVE IESEMRELVK
LVVTRSSSED LDSEIKQNFL TIARSFYYAA YCNQGTINFH IAKVLFEKVL
