KPS_SALDI
ID KPS_SALDI Reviewed; 787 AA.
AC A0A1S5RW73; A0A1L3THX5;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=(-)-kolavenyl diphosphate synthase, chloroplastic {ECO:0000303|PubMed:28204567};
DE Short=SdKPS {ECO:0000303|PubMed:28204567};
DE EC=5.5.1.28 {ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567};
DE AltName: Full=Clerodienyl diphosphate synthase {ECO:0000303|PubMed:27865008};
DE AltName: Full=Kolavenyl diphosphate synthase CPS2 {ECO:0000303|PubMed:27865008};
DE Short=SdCPS2 {ECO:0000303|PubMed:27865008};
DE Flags: Precursor;
GN Name=KPS {ECO:0000303|PubMed:28204567};
GN Synonyms=CPS2 {ECO:0000303|PubMed:27865008};
OS Salvia divinorum (Maria pastora) (Diviner's sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia subgen. Calosphace.
OX NCBI_TaxID=28513;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY,
RP DXDD MOTIF, AND MUTAGENESIS OF VAL-200; PHE-255; ALA-314; SER-369 AND
RP SER-402.
RC TISSUE=Peltate glandular trichome;
RX PubMed=28204567; DOI=10.1093/jxb/erw493;
RA Chen X., Berim A., Dayan F.E., Gang D.R.;
RT "A (-)-kolavenyl diphosphate synthase catalyzes the first step of
RT salvinorin A biosynthesis in Salvia divinorum.";
RL J. Exp. Bot. 68:1109-1122(2017).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF PHE-255; CYS-359 AND TRP-360.
RC TISSUE=Peltate glandular trichome;
RX PubMed=27865008; DOI=10.1111/tpj.13427;
RA Pelot K.A., Mitchell R., Kwon M., Hagelthorn D.M., Wardman J.F., Chiang A.,
RA Bohlmann J., Ro D.K., Zerbe P.;
RT "Biosynthesis of the psychotropic plant diterpene salvinorin A: Discovery
RT and characterization of the Salvia divinorum clerodienyl diphosphate
RT synthase.";
RL Plant J. 89:885-897(2017).
RN [3]
RP PATHWAY, AND REVIEW.
RX PubMed=30468448; DOI=10.1039/c8np00077h;
RA Liu Y., Jing S.-X., Luo S.-H., Li S.-H.;
RT "Non-volatile natural products in plant glandular trichomes: chemistry,
RT biological activities and biosynthesis.";
RL Nat. Prod. Rep. 36:626-665(2019).
CC -!- FUNCTION: Involved in the biosynthesis of clerodane diterpenoids
CC natural products, including salvinorin A with potent agonistic activity
CC on brain kappa-opioid receptors, thus confering hallucinogenic
CC properties (PubMed:30468448). Diterpene synthase that catalyzes the
CC formation of (-)-kolavenyl diphosphate from geranylgeranyl diphosphate
CC (GGPP) as the first reaction in salvinorin A biosynthesis
CC (PubMed:27865008, PubMed:28204567). {ECO:0000269|PubMed:27865008,
CC ECO:0000269|PubMed:28204567, ECO:0000303|PubMed:30468448}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate = (-)-kolavenyl
CC diphosphate; Xref=Rhea:RHEA:54684, ChEBI:CHEBI:58756,
CC ChEBI:CHEBI:138310; EC=5.5.1.28;
CC Evidence={ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:54685;
CC Evidence={ECO:0000269|PubMed:27865008, ECO:0000269|PubMed:28204567};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:28204567};
CC -!- ACTIVITY REGULATION: Inhibited by high concentrations of magnesium.
CC {ECO:0000269|PubMed:28204567}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.9 uM for geranylgeranyl diphosphate
CC {ECO:0000269|PubMed:28204567};
CC Note=kcat is 0.88 with geranylgeranyl diphosphate as substrate.
CC {ECO:0000269|PubMed:28204567};
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:28204567};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in peltate glandular trichomes of leaves
CC (PubMed:27865008). Highly expressed in the first leaf pair
CC (PubMed:28204567). {ECO:0000269|PubMed:27865008,
CC ECO:0000269|PubMed:28204567}.
CC -!- DOMAIN: The Asp-Xaa-Asp-Asp (DXDD) motif is important for the catalytic
CC activity through binding to Mg(2+). {ECO:0000305|PubMed:28204567}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. Tpsc subfamily.
CC {ECO:0000305}.
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DR EMBL; KX268505; AOZ15895.1; -; mRNA.
DR EMBL; KX424877; APH81400.1; -; mRNA.
DR AlphaFoldDB; A0A1S5RW73; -.
DR SMR; A0A1S5RW73; -.
DR KEGG; ag:AOZ15895; -.
DR BRENDA; 5.5.1.28; 15072.
DR BRENDA; 5.5.1.B7; 15072.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR GO; GO:0016102; P:diterpenoid 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 Chloroplast; Isomerase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..47
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 48..787
FT /note="(-)-kolavenyl diphosphate synthase, chloroplastic"
FT /id="PRO_0000447688"
FT MOTIF 368..371
FT /note="DXDD motif"
FT /evidence="ECO:0000305|PubMed:28204567"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 368
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 370
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 454
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT MUTAGEN 200
FT /note="V->I: No switch of product outcome."
FT /evidence="ECO:0000269|PubMed:28204567"
FT MUTAGEN 255
FT /note="F->H: Complete switch of product outcome from (-)-
FT kolavenyl diphosphate to ent-copalyl diphosphate."
FT /evidence="ECO:0000269|PubMed:27865008,
FT ECO:0000269|PubMed:28204567"
FT MUTAGEN 314
FT /note="A->V: No switch of product outcome."
FT /evidence="ECO:0000269|PubMed:28204567"
FT MUTAGEN 359
FT /note="C->F: Catalyzes the production of ent-7,13E-copalyl
FT diphosophate; when associated with S-360."
FT /evidence="ECO:0000269|PubMed:27865008"
FT MUTAGEN 360
FT /note="W->A: Catalyzes the production of ent-8alpha/beta-
FT labda-13-en-8-ol diphosphate."
FT /evidence="ECO:0000269|PubMed:27865008"
FT MUTAGEN 360
FT /note="W->S: Catalyzes the production of ent-8alpha/beta-
FT labda-13-en-8-ol diphosphate and of ent-7,13E-copalyl
FT diphosophate. Increased ability to produce ent-7,13E-
FT copalyl diphosophate; when associated with F-359."
FT /evidence="ECO:0000269|PubMed:27865008"
FT MUTAGEN 369
FT /note="S->V: No switch of product outcome."
FT /evidence="ECO:0000269|PubMed:28204567"
FT MUTAGEN 402
FT /note="S->C: No switch of product outcome."
FT /evidence="ECO:0000269|PubMed:28204567"
FT CONFLICT 308
FT /note="N -> H (in Ref. 2; APH81400)"
FT /evidence="ECO:0000305"
FT CONFLICT 643
FT /note="Q -> L (in Ref. 2; APH81400)"
FT /evidence="ECO:0000305"
FT CONFLICT 710
FT /note="K -> KQ (in Ref. 2; APH81400)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 787 AA; 89377 MW; 1015581F3C0DC1FA CRC64;
MSFATSLPRP TTTGAAGFGL PLATCISLSV SHSFSPKFGI CNNTSLRLKS KAGSGCYEGI
HRSQLAASTI LEGHTPINPE VESEKIRLIE RIRLMFRSMD DGEISVSPYD TAWVALVEDI
GGSGGPQFPT SLEWISNNQL DDGSWGDRKF VLYDRILNTL ACVVALTTWK MHPNKCEKGL
RFISDNIEKL ADEDEELMPV GFEIALPSLI DLAKRLCIEI PDNSASIKNI YAKRDSKLKR
IPMDLMHKKP TSLLFSLEGM EGLNWDKLLD FQSEGSFLSS PSSTAYALHH TKDELCLEYL
LKAVKKFNGG VPNAYPVDMF EHLWSVDRLR RLGISRYFQV EIDECLDYVY RYWTNKGICW
ARNMCVQDSD DSSMGFRLLR LYGYDVSIDV FKQFEEGGQF CSIPGQMTHA ITGMYNLYRA
SQLMFPQEHI LADARNFTAN LLHQKRVTNS IVDKWIITKD LPGEVAYALD VPFYASLPRL
EARFFLEQYG GDDDVWIGKT LYRMLYVNCN TYLELAKLDY KHCQTVHQLE WNSMQTWYRE
CNLGEFGLSE RSLLLAYYIA ASTAFEPEKS SERLAWAITT ILVETIMSQE LSDEQKREFV
DEFVNISIIN NQNGGRYKPG NRLVEVLINT VTLMAEGRGT DQQLSNAWKN WLKTWEEGGD
LGEAEARLLL HTIHLSSGLD ESSFSHPKYQ QLLEATSKVC HQLRLFQNLK ANDAQGSTSR
LVTVTTFQIE AGMQELVKLI FTKTLEDLTS ATKQSFFNIA RSFYYTAYCP ADTIDSHINK
VLFEKIV
