CPS1_ISORU
ID CPS1_ISORU Reviewed; 798 AA.
AC A0A1X9IRQ7; A0A1W6QDI2; A0A516QJE3;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Copalyl diphosphate synthase 1, chloroplastic {ECO:0000303|PubMed:28381502, ECO:0000303|PubMed:28445526, ECO:0000303|Ref.3};
DE Short=IrCPS1 {ECO:0000303|PubMed:28381502};
DE EC=5.5.1.12 {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};
DE AltName: Full=Terpene synthase 3 {ECO:0000303|PubMed:28445526};
DE Short=IrTPS3 {ECO:0000303|PubMed:28445526};
DE Flags: Precursor;
GN Name=CPS1 {ECO:0000303|PubMed:28381502};
GN Synonyms=TPS3 {ECO:0000303|PubMed:28445526};
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PATHWAY, CATALYTIC ACTIVITY, AND
RP TISSUE SPECIFICITY.
RX PubMed=28445526; DOI=10.1371/journal.pone.0176507;
RA Pelot K.A., Hagelthorn L.M., Addison J.B., Zerbe P.;
RT "Biosynthesis of the oxygenated diterpene nezukol in the medicinal plant
RT Isodon rubescens is catalyzed by a pair of diterpene synthases.";
RL PLoS ONE 12:e0176507-e0176507(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Liu X.;
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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, ECO:0000269|PubMed:28445526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:24317;
CC Evidence={ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};
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, ECO:0000269|PubMed:28445526}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in roots, and, at low levels, in
CC stems and leaves. {ECO:0000269|PubMed:28381502,
CC ECO:0000269|PubMed:28445526}.
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: 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}.
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DR EMBL; KU180499; APJ36371.1; -; mRNA.
DR EMBL; KX831651; ARO38141.1; -; mRNA.
DR EMBL; MK344324; QDQ03535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9IRQ7; -.
DR SMR; A0A1X9IRQ7; -.
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; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isomerase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..72
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 73..798
FT /note="Copalyl diphosphate synthase 1, chloroplastic"
FT /id="PRO_0000452372"
FT MOTIF 383..386
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 385
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 469
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT CONFLICT 8
FT /note="H -> P (in Ref. 3; QDQ03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 23..25
FT /note="Missing (in Ref. 3; QDQ03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 23..24
FT /note="Missing (in Ref. 1; APJ36371)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="L -> M (in Ref. 1; APJ36371)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="T -> M (in Ref. 1; APJ36371)"
FT /evidence="ECO:0000305"
FT CONFLICT 139
FT /note="E -> Q (in Ref. 1; APJ36371)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="E -> Q (in Ref. 2; ARO38141)"
FT /evidence="ECO:0000305"
FT CONFLICT 247..249
FT /note="SRQ -> TRE (in Ref. 2; ARO38141)"
FT /evidence="ECO:0000305"
FT CONFLICT 498
FT /note="R -> S (in Ref. 3; QDQ03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 607
FT /note="N -> S (in Ref. 3; QDQ03535)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="V -> F (in Ref. 2; ARO38141)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 798 AA; 91716 MW; AB0F18683720B055 CRC64;
MASLSTMHLI NHSPASRRRI MSAAAAAAAK LHLPECFTIT KSAWMNNTEN LTLNYQLNHK
KISKVAGINR VATVDAPQVH DQDDSTENQG HDAVNNIEDP IEYIRTLLRT TGDGRISVSP
YDTAWVALIK DLNGRDAPEF PSSLEWIVRN QLDDGSWGDD KFFCVYDRLV NTIACVVALR
SWNVHDDKLK RGVTYIKENV EKLRDGNVEH MTCGFEVVFT ALLQRAKCLG IEDLPYDSPL
IQEIYHSRQQ KLNRIPMEMM HKVPTSLLFS LEGLENLEWE RLLKLQSADG SFLTSPSSTA
FAFMQTKDEK CYQFIKNTVE TFNGGAPHTY PVDVFGRLWA VDRLQRLGIS RFFESEIAEC
LAHIHKFWTE KGVFSGRESE FCDIDDTSMG IRLLRMHGYD VDPNVLRNFK KDDNFSCYGG
QMIESPSPIY NLYRASQLRF PGEEILEDAN KFAYNFLQEK LANNQILDKW VISKHLPDEI
KLGMEMPWYA TLPRVEARYY LQYYAGSGDV WIGKTLYRMP EISNDTYHEL AKTDFKRCQA
QHQFEWIYMQ EWYESCNVEE FGISRKELLL AYFLATASIF ELEKTKERIA WAKSQIISKM
ITSFFNNHNT SSEEKLAFLT DFRNSNGLNN TNMVLATLTQ FLEGFNRYTS HQLKNAWGEW
LAKLQQGEGD GAADAELLTN TLNICAGHIA FREEILSHNE YTTLSNLTSK ICQQLSQIQN
EKKMEIEGQM TAETSIKNKE LEQDMQTLVK LVLGKSSGIN RNIKKTFLAV AKTYYYRAYH
DAQTIDTHMF KVLFEPVV
