CPS4_ISORU
ID CPS4_ISORU Reviewed; 796 AA.
AC A0A1W6QDJ1; A0A1X9IRR5;
DT 07-APR-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2017, sequence version 1.
DT 03-AUG-2022, entry version 20.
DE RecName: Full=Ent-copalyl diphosphate synthase 4 {ECO:0000303|PubMed:28381502, ECO:0000303|PubMed:28445526};
DE EC=5.5.1.13 {ECO:0000269|PubMed:28381502, ECO:0000269|PubMed:28445526};
DE AltName: Full=Terpene synthase 5 {ECO:0000303|PubMed:28445526};
DE Short=IrTPS5 {ECO:0000303|PubMed:28445526};
DE Flags: Precursor;
GN Name=CPS4 {ECO:0000303|PubMed:28381502};
GN Synonyms=TPS5 {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] (ISOFORM 2), 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, PATHWAY, CATALYTIC
RP ACTIVITY, AND 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).
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:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=A0A1W6QDJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A0A1W6QDJ1-2; Sequence=VSP_060981, VSP_060982, VSP_060983,
CC VSP_060984, VSP_060985, VSP_060986,
CC VSP_060987, VSP_060988;
CC -!- TISSUE SPECIFICITY: Highly expressed in leaves, and, at low levels, in
CC stems, but barely in roots and flowers. {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; KU180502; APJ36374.1; -; mRNA.
DR EMBL; KX831653; ARO38143.1; -; mRNA.
DR AlphaFoldDB; A0A1W6QDJ1; -.
DR SMR; A0A1W6QDJ1; -.
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; 2.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Isomerase; Magnesium; Metal-binding;
KW Plastid; Transit peptide.
FT TRANSIT 1..23
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 24..796
FT /note="Ent-copalyl diphosphate synthase 4"
FT /id="PRO_0000452375"
FT MOTIF 371..374
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 240
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 371
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 373
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 VAR_SEQ 544..555
FT /note="CKLGEFGLGEKR -> WNLVEFGLSERS (in isoform 2)"
FT /id="VSP_060981"
FT VAR_SEQ 561..574
FT /note="FLAASTAFEPEKKG -> YIAASTVFEPERSR (in isoform 2)"
FT /id="VSP_060982"
FT VAR_SEQ 581..587
FT /note="KTAFLVE -> ITAILVK (in isoform 2)"
FT /id="VSP_060983"
FT VAR_SEQ 593..641
FT /note="QLSHEQKREFADEFEHGSSLNMENGGSYKTRTRLVEILSNTVSQLSFET ->
FT RQLPLEQKGEFLGSILENEDGGRLIEFLINTISQLSSEI (in isoform 2)"
FT /id="VSP_060984"
FT VAR_SEQ 664..669
FT /note="WEEGGN -> CKEGGDDD (in isoform 2)"
FT /id="VSP_060985"
FT VAR_SEQ 676..682
FT /note="QLLLQTL -> RLILHTQ (in isoform 2)"
FT /id="VSP_060986"
FT VAR_SEQ 704..710
FT /note="VTCKVCN -> ATSKVCG (in isoform 2)"
FT /id="VSP_060987"
FT VAR_SEQ 717..732
FT /note="NRKAHDAQGGISDLVI -> SRKQVDVDLAT (in isoform 2)"
FT /id="VSP_060988"
FT CONFLICT 6
FT /note="I -> N (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 26..27
FT /note="AQ -> VR (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="V -> A (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 94
FT /note="E -> K (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 196
FT /note="N -> D (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="V -> A (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 386
FT /note="G -> S (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 524
FT /note="K -> E (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="K -> E (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 650
FT /note="K -> T (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 741
FT /note="S -> G (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 760
FT /note="I -> L (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="A -> S (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 780
FT /note="A -> E (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 788
FT /note="Y -> D (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
FT CONFLICT 794
FT /note="N -> K (in Ref. 1; APJ36374)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 796 AA; 91115 MW; 6011B334880C205A CRC64;
MSSSSIVTSL LRPTTAADGV LPRQMAQVNS SCNIWRSKAK VGGINYFNPG NIKCVEEVHK
SRQVVVAALK SLEYETEKPT NQDVVSEKMR VLSERIETML QNMDEGEISI SPYDTAWVAL
VEDTDGRPQF PTSLEWISNN QLADGSWGDR KFVIYDRILN TLACVVALTT WNMHPHKCNR
GLRFIRDNME KLENENEELM PIGFEVVFPS LIEAAQKLGI EIPHIDSPCI KKIQAMRDFK
LKRIPMELLH KKPTSLLHSL EGMQGLVWEK LLDFRSDGSF LCSPSSTAYA LQHTKDELCL
QYLLKAVKKF NGGVPNVYPV DMFEHLWCVD RLQRLGICRY FRVQIKEMLD YVYKYWTDKG
ICWARNTNVQ DVDDTAMGFR LLRMHGYDVS TDVFKQFEKA GEFCCFPGQS THAITGMYNV
YRTSQIMFDG EDILADAKNY SATFLHQKRL ANELVDKWII TKDLPGEVGY ALDVPFFASL
PRLEARFFLE QYGGDDDVWI GKTLYRMPYV NSDTYLELAK LDYKKCQAVH QLEWKSIQKW
YRDCKLGEFG LGEKRLLLAY FLAASTAFEP EKKGERLAWA KTAFLVETIA SQQLSHEQKR
EFADEFEHGS SLNMENGGSY KTRTRLVEIL SNTVSQLSFE TLVAEGRDIK QQLSNTWQKW
LKTWEEGGNL GEAEAQLLLQ TLHLSSGLDE SSFSHPKYHQ LLEVTCKVCN QLRLFQNRKA
HDAQGGISDL VIGTTFQIEA SMQELVKLVF TKSSEDLDSI TKQSFFAIAR SFYYTAYCDA
GAINSHIYKV LFENID
