CPS2_ISOER
ID CPS2_ISOER Reviewed; 794 AA.
AC G3E4M4; G3E4M5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Ent-copalyl diphosphate synthase 2 {ECO:0000303|PubMed:22284743};
DE Short=IeCPS2 {ECO:0000303|PubMed:22284743};
DE EC=5.5.1.13 {ECO:0000269|PubMed:22284743};
DE Flags: Precursor;
GN Name=CPS2 {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] (ISOFORMS 1 AND 2), FUNCTION, PATHWAY, CATALYTIC
RP ACTIVITY, TISSUE 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 (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: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:22284743}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=G3E4M4-1; Sequence=Displayed;
CC Name=2; Synonyms=CPS2a;
CC IsoId=G3E4M4-2; Sequence=VSP_060989, VSP_060990;
CC -!- TISSUE SPECIFICITY: Expressed in leaves. {ECO:0000269|PubMed:22284743}.
CC -!- DEVELOPMENTAL STAGE: Accumulates in young and mature leaves where the
CC dominant ent-kaurane diterpenoid maoecrystal B accumulates.
CC {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; HQ455831; AEP03175.1; -; mRNA.
DR EMBL; HQ455832; AEP03176.1; -; mRNA.
DR AlphaFoldDB; G3E4M4; -.
DR SMR; G3E4M4; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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:1901946; P:miltiradiene biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IDA: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 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Isomerase; Magnesium; Metal-binding;
KW Plastid; Transit peptide.
FT TRANSIT 1..35
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 36..794
FT /note="Ent-copalyl diphosphate synthase 2"
FT /id="PRO_0000452379"
FT MOTIF 369..372
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 369
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 455
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT VAR_SEQ 42..48
FT /note="Missing (in isoform 2)"
FT /id="VSP_060989"
FT VAR_SEQ 95..98
FT /note="GTML -> ETIQ (in isoform 2)"
FT /id="VSP_060990"
FT CONFLICT 11
FT /note="P -> L (in Ref. 1; AEP03176)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="K -> E (in Ref. 1; AEP03176)"
FT /evidence="ECO:0000305"
FT CONFLICT 785
FT /note="I -> M (in Ref. 1; AEP03176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 794 AA; 90777 MW; 93D0C4A2F792FE65 CRC64;
MSSSSNVTSL PRLTTAGGVF PREMVRVHSS CNILRSKAKV GGINYFNPGN IKCVEVHKSR
QVAVAAVKSL EYETEKPTNQ DVVSEKMRVL SERIGTMLQN MNEGEISISP YDTAWVALVE
DTDGRPQFPT SLEWISNNQL ADGSWGDRKF VIYDRILNTL ACVVALTTWN MHPHKCNRGL
RFIRDNIEKL ENENEELMPI GFEVVFPSLI EAAQKLGIEI PHIDSPCIKK IQAMRDFKLK
RIPMELLHKK PTSLLHSLEG MQGLVWEKLL DFRSDGSFLC SPSSTAYALQ HTKDELCLQY
LLKAVKKFNG GVPNVYPVDM FEHLWCVDRL QRLGICRYFR AQIKEMLDYV YKYWTDKGIC
WARNTNVQDV DDTAMGFRLL RMHGYDVSTD VFKQFEKAGE FCCFPGQSTH AITGMYNVYR
TSQIMFDGED ILADAKNYSA TFLHQKRLAS ELVDKWIITK DLPGEVGYAL DVPFFASLPR
LEARFFLEQY GGDDDVWIGK TLYRMPYVNS DTYLELAKLD YKKCQAVHQL EWKSIQKWYR
DCKLGEFGLG EKRLLLAYFL AASTAFEPEK KGERLAWAKT AFLVETIASQ QLSHEQKREF
PNEFEHGSSL NMENGGRYKT RTRLVEILSN TVSQLSFETL VAEGRDIKQQ LSNTWQKWLK
TWEEGGNLGE AEAQLLLQTL HLSSGLDESS FSHPKYHQLL EATCKVCNQL RLFQNRKAHD
AQGGISDLVI GTTFQIEASM QELVKLVFTK SSEDLDSITK QSFFAIARSF YYTAYCDAGA
INSHIYKVLF ENID
