CPS3_ISOER
ID CPS3_ISOER Reviewed; 766 AA.
AC A0A3G1QTU5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Ent-copalyl diphosphate synthase 3 {ECO:0000303|PubMed:30496917};
DE Short=IeCPS3 {ECO:0000303|PubMed:30496917};
DE EC=5.5.1.13 {ECO:0000269|PubMed:30496917};
DE Flags: Precursor; Fragment;
GN Name=CPS3 {ECO:0000303|PubMed:30496917};
OS Isodon eriocalyx (Plectranthus eriocalyx).
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=662907;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=30496917; DOI=10.1016/j.phytochem.2018.11.015;
RA Du G., Gong H.-Y., Feng K.-N., Chen Q.-Q., Yang Y.-L., Fu X.-L., Lu S.,
RA Zeng Y.;
RT "Diterpene synthases facilitating production of the kaurane skeleton of
RT eriocalyxin B in the medicinal plant Isodon eriocalyx.";
RL Phytochemistry 158:96-102(2019).
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, and in the production of gibberellins
CC phytohormones (PubMed:30496917). Catalyzes the conversion of
CC (2E,6E,10E)-geranylgeranyl diphosphate (GGPP) to ent-copalyl
CC diphosphate (ent-CPP) (PubMed:30496917). {ECO:0000269|PubMed:30496917}.
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:30496917};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842;
CC Evidence={ECO:0000269|PubMed:30496917};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC -!- PATHWAY: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305|PubMed:30496917}.
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:30496917}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Accumulates in leaves, and, at low levels, in
CC germinating seeds. {ECO:0000269|PubMed:30496917}.
CC -!- DEVELOPMENTAL STAGE: Moslty expressed in leaves where ent-kaurane
CC diterpenoids accumulates but weakly expressed in germinating seeds in
CC which gibberellins are produced. {ECO:0000269|PubMed:30496917}.
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. Tpsc subfamily.
CC {ECO:0000305}.
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DR EMBL; KY937955; AWN06649.1; -; mRNA.
DR AlphaFoldDB; A0A3G1QTU5; -.
DR SMR; A0A3G1QTU5; -.
DR UniPathway; UPA00213; -.
DR UniPathway; UPA00390; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009905; F:ent-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:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
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..30
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 31..766
FT /note="Ent-copalyl diphosphate synthase 3"
FT /id="PRO_0000452380"
FT MOTIF 354..357
FT /note="DXDD motif"
FT /evidence="ECO:0000250|UniProtKB:G3E4M4"
FT BINDING 222
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 356
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 440
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT NON_TER 1
FT /evidence="ECO:0000305"
SQ SEQUENCE 766 AA; 87546 MW; 50232FABE369FE77 CRC64;
FRSTAAGRCL PVTCCVFPRH FRVSSSSILP SNAKVVGGCK KNRQIAVEAA QSLEVDSQQP
MNQEEVSEKM RQLREKIRWM LQNMDDGEIS VSPYDTAWVA MVEDIGGGGG PQFPTSLEWI
SNNQLDDGSW GDLRFLIYDR ILNTLACVAV LTQWKMHLHK CQKGLRFIRE NIDNLENGND
EMMPVGFEVA FPSLIQTAKK VGIKIPTDSP FMKNIYAKRD LKLRKIPMDI LHTKPTTLLH
SLEGMEGLDW EKLLNLRTDD GSFLMSPSST AYVFRHTKDE LCHQYLLKSV NKFNGGVPNV
YPVDMFEHLW CVDRLQRLGI SRYFQVEIQE CLDYVYKYWT NKGICWARNT NVQDVDDTAM
GFRLLRLHGY DVSTDAFKQF EKAGEFCSFP GQSTDALTGM YNLYRASQTM FNGEHILADA
KEYSTNFLHK KRLANAIVDK WIITKDLPGE VGYALDVPFY ASLPRLEARF FLEQYGGDDD
VWIGKTLYRM LYVNCDTHLE LAKLDYEKCQ AVHQLEWESI QKWYRDWNLV EFGLSERSLL
LAYYIAASTV FEPERSRERL AWAITAILVK TIASQRQLPL ETKGESLGSI LENEDGGRLI
EFLINTIHQL SSEIVVAEGR DITQQLSNTW QKWLKTCKEG GDDDLGEAEA RLIVHTLHLS
SGLDESSFSH PKYHQLLEAT SKVCGQLRLF QSRKQVDVDL ATGTTFQIEA GMQELVKLVF
TNSSEDLDSL TKQSFFSIAR SFYYTAYCDE GAINSHIDKV LFEKID