CPS1_SALMI
ID CPS1_SALMI Reviewed; 793 AA.
AC B8PQ84; A0A0A7AN31;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 52.
DE RecName: Full=Copalyl diphosphate synthase CPS1, chloroplastic {ECO:0000305};
DE Short=Copalyl diphosphate synthase 1 {ECO:0000303|PubMed:22291132};
DE Short=SmCPS {ECO:0000303|PubMed:19905026};
DE Short=SmCPS1 {ECO:0000303|PubMed:22291132};
DE EC=5.5.1.12 {ECO:0000269|PubMed:19905026};
DE Flags: Precursor;
GN Name=CPS1 {ECO:0000303|PubMed:22291132};
GN Synonyms=CPS {ECO:0000303|PubMed:19905026};
OS Salvia miltiorrhiza (Chinese sage).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Nepetoideae; Mentheae; Salviinae;
OC Salvia; Salvia incertae sedis.
OX NCBI_TaxID=226208;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION BY
RP JASMONATE.
RC TISSUE=Root hair;
RX PubMed=19905026; DOI=10.1021/ol902051v;
RA Gao W., Hillwig M.L., Huang L., Cui G., Wang X., Kong J., Yang B.,
RA Peters R.J.;
RT "A functional genomics approach to tanshinone biosynthesis provides
RT stereochemical insights.";
RL Org. Lett. 11:5170-5173(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26077765; DOI=10.1104/pp.15.00695;
RA Cui G., Duan L., Jin B., Qian J., Xue Z., Shen G., Snyder J.H., Song J.,
RA Chen S., Huang L., Peters R.J., Qi X.;
RT "Functional divergence of diterpene syntheses in the medicinal plant Salvia
RT miltiorrhiza.";
RL Plant Physiol. 169:1607-1618(2015).
RN [3]
RP FUNCTION.
RX PubMed=21082262; DOI=10.1007/s11033-010-0383-9;
RA Cui G., Huang L., Tang X., Zhao J.;
RT "Candidate genes involved in tanshinone biosynthesis in hairy roots of
RT Salvia miltiorrhiza revealed by cDNA microarray.";
RL Mol. Biol. Rep. 38:2471-2478(2011).
RN [4]
RP INDUCTION BY JASMONATE.
RX PubMed=22291132; DOI=10.1093/jxb/err466;
RA Ma Y., Yuan L., Wu B., Li X., Chen S., Lu S.;
RT "Genome-wide identification and characterization of novel genes involved in
RT terpenoid biosynthesis in Salvia miltiorrhiza.";
RL J. Exp. Bot. 63:2809-2823(2012).
CC -!- FUNCTION: Involved in tanshinone biosynthesis in hairy roots
CC (PubMed:19905026, PubMed:26077765, PubMed:21082262). Catalyzes the
CC conversion of geranylgeranyl diphosphate (GGPP) to copalyl diphosphate
CC (CPP) (PubMed:19905026, PubMed:26077765, PubMed:21082262).
CC {ECO:0000269|PubMed:19905026, ECO:0000269|PubMed:21082262,
CC ECO:0000269|PubMed:26077765}.
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:19905026};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24317;
CC Evidence={ECO:0000269|PubMed:19905026};
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:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- INDUCTION: Induced by jasmonate (MeJA) in roots.
CC {ECO:0000269|PubMed:19905026, ECO:0000269|PubMed:22291132}.
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 -!- MISCELLANEOUS: Plant silencing CPS1 are impaired in tanshinone
CC biosynthesis in hairy roots (PubMed:26077765). CPS1-silenced plants
CC exhibit an obvious white-color root phenotype compared with wild-type
CC roots, which have the characteristic reddish color associated with
CC tanshinones (PubMed:26077765). {ECO:0000269|PubMed:26077765}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {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; EU003997; ABV57835.1; -; mRNA.
DR EMBL; KC814639; AHJ59321.1; -; mRNA.
DR AlphaFoldDB; B8PQ84; -.
DR SMR; B8PQ84; -.
DR BRENDA; 5.5.1.12; 9850.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0050559; F: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:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..793
FT /note="Copalyl diphosphate synthase CPS1, chloroplastic"
FT /id="PRO_0000449933"
FT MOTIF 370..373
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 238
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 370
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 372
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 457
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT CONFLICT 56
FT /note="I -> L (in Ref. 2; AHJ59321)"
FT CONFLICT 250
FT /note="I -> M (in Ref. 2; AHJ59321)"
FT CONFLICT 597
FT /note="T -> A (in Ref. 2; AHJ59321)"
FT CONFLICT 602..605
FT /note="DKRA -> EKRD (in Ref. 2; AHJ59321)"
FT CONFLICT 611
FT /note="G -> E (in Ref. 2; AHJ59321)"
FT CONFLICT 733
FT /note="N -> S (in Ref. 2; AHJ59321)"
SQ SEQUENCE 793 AA; 90483 MW; 0D60AE289ABC59BC CRC64;
MASLSSTILS RSPAARRRIT PASAKLHRPE CFATSAWMGS SSKNLSLSYQ LNHKKISVAT
VDAPQVHDHD GTTVHQGHDA VKNIEDPIEY IRTLLRTTGD GRISVSPYDT AWVAMIKDVE
GRDGPQFPSS LEWIVQNQLE DGSWGDQKLF CVYDRLVNTI ACVVALRSWN VHAHKVKRGV
TYIKENVDKL MEGNEEHMTC GFEVVFPALL QKAKSLGIED LPYDSPAVQE VYHVREQKLK
RIPLEIMHKI PTSLLFSLEG LENLDWDKLL KLQSADGSFL TSPSSTAFAF MQTKDEKCYQ
FIKNTIDTFN GGAPHTYPVD VFGRLWAIDR LQRLGISRFF EPEIADCLSH IHKFWTDKGV
FSGRESEFCD IDDTSMGMRL MRMHGYDVDP NVLRNFKQKD GKFSCYGGQM IESPSPIYNL
YRASQLRFPG EEILEDAKRF AYDFLKEKLA NNQILDKWVI SKHLPDEIKL GLEMPWLATL
PRVEAKYYIQ YYAGSGDVWI GKTLYRMPEI SNDTYHDLAK TDFKRCQAKH QFEWLYMQEW
YESCGIEEFG ISRKDLLLSY FLATASIFEL ERTNERIAWA KSQIIAKMIT SFFNKETTSE
EDKRALLNEL GNINGLNDTN GAGREGGAGS IALATLTQFL EGFDRYTRHQ LKNAWSVWLT
QLQHGEADDA ELLTNTLNIC AGHIAFREEI LAHNEYKALS NLTSKICRQL SFIQSEKEMG
VEGEIAAKSS IKNKELEEDM QMLVKLVLEK YGGIDRNIKK AFLAVAKTYY YRAYHAADTI
DTHMFKVLFE PVA
