CPS2_ISORU
ID CPS2_ISORU Reviewed; 419 AA.
AC A0A1X9IRP7;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2017, sequence version 1.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Copalyl diphosphate synthase 2, chloroplastic {ECO:0000303|PubMed:28381502};
DE Short=IrCPS2 {ECO:0000303|PubMed:28381502};
DE EC=5.5.1.12 {ECO:0000269|PubMed:28381502};
DE Flags: Fragment;
GN Name=CPS2 {ECO:0000303|PubMed:28381502};
OS Isodon rubescens (Rabdosia rubescens).
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=587669;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RX PubMed=28381502; DOI=10.1104/pp.17.00202;
RA Jin B., Cui G., Guo J., Tang J., Duan L., Lin H., Shen Y., Chen T.,
RA Zhang H., Huang L.;
RT "Functional diversification of kaurene synthase-like genes in Isodon
RT rubescens.";
RL Plant Physiol. 174:943-955(2017).
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:28381502). Catalyzes the conversion of
CC (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to (+)-copalyl
CC diphosphate ((+)-CPP) (PubMed:28381502). {ECO:0000269|PubMed:28381502}.
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:28381502};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24317;
CC Evidence={ECO:0000269|PubMed:28381502};
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:28381502}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000250|UniProtKB:G8GJ96}.
CC -!- TISSUE SPECIFICITY: Ubiquitous expression in roots, stems, leaves and
CC flowers. {ECO:0000269|PubMed:28381502}.
CC -!- MISCELLANEOUS: Abietane diterpenoids (e.g. miltiradiene, abietatriene
CC and ferruginol) accumulate specifically in the periderm of roots
CC (PubMed:28381502). The ent-kaurene diterpenoid oridonin, main
CC constituent of Isodon rubescens, accumulates in leaves
CC (PubMed:28381502). {ECO:0000269|PubMed:28381502}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsc subfamily.
CC {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; KU180500; APJ36372.1; -; mRNA.
DR AlphaFoldDB; A0A1X9IRP7; -.
DR SMR; A0A1X9IRP7; -.
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: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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isomerase; Magnesium; Metal-binding; Plastid.
FT CHAIN <1..419
FT /note="Copalyl diphosphate synthase 2, chloroplastic"
FT /id="PRO_0000452373"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 48375 MW; DD15CFD905D5B40B CRC64;
MGIRLLKMHG YDVDPNALKH FKQEDGKFSC YGGQMIESAS PIYNLYRASQ LRFPGEEILE
EATKFAYNFL QEKIANNQIQ EKWVISEHLI DEIKLGLKMP WYATLPRVEA AYYLQYYAGT
GDVWIGKTFY RMPEISNDTY KELAVLDFNR CQAQHQFEWI YMQEWYQSSS VKAFGISKKE
LLLAYFLAAA TIFEPERTQE RIMWAKTQIV SRMIKSFLSK ENTLSLEQKT TLLIDFGHDI
NGLNKINSVE KGNGLAGTLL TTFQQLLEEF DRYTTHQLKN AWSQWFVKLQ QGEGDGGADA
ELLANTLNIC AGHIAFNEDI LSHRDYTTLS SLTTKICQRL TQIQDKKILE IKDGSIKDKE
LEEEMQALVK LVLEENGGGI DRNIKQTFLS VFKTFYYCAY HHAETTDAHI FKVLFEPVV
