CPS5_ISORU
ID CPS5_ISORU Reviewed; 664 AA.
AC A0A1X9ISN9; A0A1W6QDI5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 19.
DE RecName: Full=Ent-copalyl diphosphate synthase 5 {ECO:0000303|PubMed:28381502};
DE EC=5.5.1.13 {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};
DE AltName: Full=Putative ent-copalyl diphosphate synthase {ECO:0000303|PubMed:28445526};
DE Short=IrTPS1 {ECO:0000303|PubMed:28445526};
DE Flags: Fragment;
GN Name=CPS5 {ECO:0000303|PubMed:28381502};
GN Synonyms=TPS1 {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] OF 1-357, FUNCTION, PATHWAY, AND CATALYTIC
RP ACTIVITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-664, FUNCTION, PATHWAY, CATALYTIC
RP ACTIVITY, AND 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).
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 ent-copalyl
CC diphosphate (ent-CPP) (PubMed:28381502). {ECO:0000269|PubMed:28381502}.
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:28381502, ECO:0000269|PubMed:28445526};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14842;
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:0000305}.
CC -!- TISSUE SPECIFICITY: Ubiquitous expression in roots, stems, leaves and
CC flowers. {ECO:0000269|PubMed:28381502}.
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; KY661361; ARO38144.1; -; mRNA.
DR EMBL; KU180503; APJ36375.1; -; mRNA.
DR AlphaFoldDB; A0A1X9ISN9; -.
DR SMR; A0A1X9ISN9; -.
DR UniPathway; UPA00213; -.
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: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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Isomerase; Magnesium; Metal-binding; Plastid.
FT CHAIN <1..>664
FT /note="Ent-copalyl diphosphate synthase 5"
FT /id="PRO_0000452376"
FT MOTIF 233..236
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 101
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 233
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 235
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 320
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT CONFLICT 314
FT /note="K -> N (in Ref. 1; ARO38144)"
FT /evidence="ECO:0000305"
FT NON_TER 1
FT /evidence="ECO:0000305"
FT NON_TER 664
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 76698 MW; EA5C6454B83783A2 CRC64;
NQLADGSWGD AGTFSIFDRI LNTLACVVAL RSWNIHPHKT DKGIWFMKKN MCRIDEENLE
HMPIGFEVAL PSLIDIAKKL EIDIPTQTRG LQEIYARREI KLKKIPRDIM HQVPTTLLHS
LEGMAGLKWE KLLKLQSEDG SFLFSPSSTA FALQQTRDHN CLKYLTNHIH KFNGGVPNVY
PVDLFEHLWA VDRLQRLGLS RYFEPEIEEC IAYVHRQWTE KGICWARNSQ VEDIDDTAMG
FRLLRLHGYE VSADVFRHFK SDGGEFFCFK GQSTQAVTGM YNLYRASQLM FPGENILVDA
ARFSANFLQL KRAKNDLLDK WIITKDLPGE VGYALDVPWY ASLPRVETRF YLDQYGGDDD
VWIGKTLYRM PYVNNNKYLE LAKLDYNNCQ ALHQQEWQNI LKWYRSCSLG EFGMTERSLL
QTYYVAAASV FEPEKSQERL AWAKTAILME TITSHFEFQQ LSRDQKRAFI TEFEHDSILK
YTNGGRYKRR SSLVGTLVRT LNHLSLDILL AHGRDIHQPL KNAWCKWLNS WEEGGDAELL
VRTLNLMSGG GRRRRWASEE LLSSNPKHEQ LLKATIGVCD KLRLFLRRKV QGGNGCMNAT
GMTTVEIESE MRELVKLVVT RSSSEDLDSE IKQNFLTIAR SFYYAAYCNQ GTINFHIAKV
LFEK
