CPS5_SALMI
ID CPS5_SALMI Reviewed; 793 AA.
AC A0A0U3LQ20; A0A0A7ANR2; V9MGN6;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 16-MAR-2016, sequence version 1.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Ent-copalyl diphosphate synthase, chloroplastic {ECO:0000303|PubMed:26971881};
DE Short=SmCPSent {ECO:0000303|PubMed:26971881};
DE EC=5.5.1.13 {ECO:0000269|PubMed:26077765};
DE Flags: Precursor;
GN Name=CPS5 {ECO:0000303|PubMed:26077765};
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, 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=26971881; DOI=10.1038/srep23057;
RA Su P., Tong Y., Cheng Q., Hu Y., Zhang M., Yang J., Teng Z., Gao W.,
RA Huang L.;
RT "Functional characterization of ent-copalyl diphosphate synthase, kaurene
RT synthase and kaurene oxidase in the Salvia miltiorrhiza gibberellin
RT biosynthetic pathway.";
RL Sci. Rep. 6:23057-23057(2016).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Huang L., Gao W., He Y., Yuan Y., Shen Y., Cheng Q.;
RT "Functional identification of copalyl diphosphate synthase and its role in
RT initiating biosynthesis of diterpenoid natural products in Salvia
RT miltiorrhiza.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the conversion of geranylgeranyl diphosphate (GGPP)
CC to the gibberellin precursor ent-copalyl diphosphate (CPP).
CC {ECO:0000269|PubMed:26077765, ECO:0000269|PubMed:26971881}.
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:26077765, ECO:0000269|PubMed:26971881};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842;
CC Evidence={ECO:0000269|PubMed:26077765, ECO:0000269|PubMed:26971881};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
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. {ECO:0000305}.
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DR EMBL; KC814642; AHJ59324.1; -; mRNA.
DR EMBL; KT934789; ALX18648.1; -; mRNA.
DR EMBL; JX156302; AGF69544.1; -; mRNA.
DR AlphaFoldDB; A0A0U3LQ20; -.
DR SMR; A0A0U3LQ20; -.
DR UniPathway; UPA00390; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009905; F:ent-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:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
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..793
FT /note="Ent-copalyl diphosphate synthase, chloroplastic"
FT /id="PRO_0000449935"
FT MOTIF 372..375
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 372
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 374
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT CONFLICT 253
FT /note="P -> S (in Ref. 3; AGF69544)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="V -> A (in Ref. 3; AGF69544)"
FT /evidence="ECO:0000305"
FT CONFLICT 612
FT /note="T -> A (in Ref. 3; AGF69544)"
FT /evidence="ECO:0000305"
FT CONFLICT 699
FT /note="H -> Q (in Ref. 1; AHJ59324 and 3; AGF69544)"
FT /evidence="ECO:0000305"
FT CONFLICT 716
FT /note="H -> R (in Ref. 3; AGF69544)"
FT /evidence="ECO:0000305"
FT CONFLICT 732
FT /note="M -> T (in Ref. 1; AHJ59324 and 3; AGF69544)"
FT /evidence="ECO:0000305"
FT CONFLICT 738
FT /note="G -> E (in Ref. 1; AHJ59324)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 793 AA; 90130 MW; 3A8095E3C940F935 CRC64;
MPLASNPVAF LPSSTAHGDL PAAAFSRSSA GCLQLCRPLT PTSSLQCNAI SRPRTEEYID
VIQNGLPVIK WHEIVEDDAE KDSPKDKVGE LRDAVRSMLR SMGDGEISIS PYDTAWVALV
ADADGDRPQF PSSLHWISTN QLADGSWGDH ATFSIFDRII NTLACVVALT SWDLHPDKTH
KGILFIKKNI HRLEEENVEH MPIGFEVALP SLIDIAKQLQ IDIPSDTRGL REIYARREIK
LKKIPSDILH QMPTTLLHSL EGMPGLMWQK LLKLQSEDGS FLFSPSSTAF ALQQTKDHNC
LKYLTNHLIK FKGGVPNVYP VDLFEHLWAV DRLQRLGVSR YFQPEIEECV AYVYRYWTEK
GICWARNSEI QDIDDTAMGF RLLRLHGYEV SADVFKHFES GGEFFCFKGQ STQAVTGMYN
LYRAAQLIFP GENILEDAAT FSAKFLQQKR ANNELLDKWI ITKDLPGEVG YALDVPWYAS
LPRVETRFYL EQYGGEDDVW IGKTLYRMPY VNNNKYLELA KLDYNNCQAL HQQEWKDIQK
WYRNSSLGEF GLSEGSLVQA YYVAAASIFE PQKSQERLAW AKTAILMQTI TSHFHHSAEQ
KRVFLHEFQH ATGGRYKTTR TLVGTLLRTL NQLSLDILLA HGCHIHQPLK NAWHKWIKTW
EGGGGGAELL VQTLNLCGGG RRNRWESEEL LSSHPKYEHL LKATVGVCDK LRRFQHRKDC
NGCMGSDGGI RMLDIEAGMQ ELVKLVVTKS PGDLDSEIKQ NFFMIARSYY YAAYCNPGTI
NFHIAKVLFE RVQ
