CPS4_SALMI
ID CPS4_SALMI Reviewed; 776 AA.
AC A0A0U2D9C5; H6VLG6; H6VLG7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 25.
DE RecName: Full=Ent-8-alpha-hydroxylabd-13-en-15-yl diphosphate synthase CPS4, chloroplastic {ECO:0000305};
DE EC=4.2.1.173 {ECO:0000269|PubMed:26077765};
DE AltName: Full=Copalyl diphosphate synthase 4 {ECO:0000303|PubMed:22291132};
DE Flags: Precursor;
GN Name=CPS4 {ECO:0000303|PubMed:22291132};
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 [GENOMIC DNA] OF 82-377 AND 386-776.
RX PubMed=22291132; DOI=10.1093/jxb/err466;
RA Ma Y., Yuan L., Wu B., Li X., Chen S., Lu S.;
RT "Genome-wide identification and characterization of novel genes involved in
RT terpenoid biosynthesis in Salvia miltiorrhiza.";
RL J. Exp. Bot. 63:2809-2823(2012).
CC -!- FUNCTION: Involved in diterpenoid biosynthesis (PubMed:26077765).
CC Catalyzes the conversion of all-trans-geranylgeranyl diphosphate to
CC ent-8alpha-hydroxylabd-13-en-15-yl diphosphate (PubMed:26077765).
CC {ECO:0000269|PubMed:26077765}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-8alpha-hydroxylabd-13-en-15-yl diphosphate = (2E,6E,10E)-
CC geranylgeranyl diphosphate + H2O; Xref=Rhea:RHEA:54648,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:58756, ChEBI:CHEBI:138223;
CC EC=4.2.1.173; Evidence={ECO:0000269|PubMed:26077765};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54650;
CC Evidence={ECO:0000269|PubMed:26077765};
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: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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AEZ55691.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; KP063138; AKN91186.1; -; mRNA.
DR EMBL; JN831120; AEZ55690.1; -; Genomic_DNA.
DR EMBL; JN831120; AEZ55691.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A0A0U2D9C5; -.
DR SMR; A0A0U2D9C5; -.
DR KEGG; ag:AKN91186; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..60
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 61..776
FT /note="Ent-8-alpha-hydroxylabd-13-en-15-yl diphosphate
FT synthase CPS4, chloroplastic"
FT /id="PRO_0000449934"
FT MOTIF 357..360
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 226
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT BINDING 357
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 359
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:C7BKP9"
FT BINDING 443
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q38802"
FT CONFLICT 338..339
FT /note="TF -> VY (in Ref. 1; AKN91186)"
FT CONFLICT 540
FT /note="I -> R (in Ref. 1; AKN91186)"
FT CONFLICT 564
FT /note="P -> A (in Ref. 1; AKN91186)"
SQ SEQUENCE 776 AA; 88151 MW; C50922F0F078EE9A CRC64;
MSFASNATGF RIPLTTCVYP SPILRFNAKV GSGSSYGTTE AQRNMKCVDG IGRSRVVAVA
ASGRTRDSNP EVESEKMKEM IRWMFRDMDD GEVSVSAYDT AWVALVEDIG GSGGPQFPTS
LDWISDNQLD DGSWGDRKFV LYDRILNTLA CVVALTTWKL HPHKCEKGLK FIRENIEKLD
NEDEELMLVG FEVALPSLID LAKKLGIEIS DDSPCIKNIY AKRDSKLKEI PMDLLHKEPT
SLLFSLEGME GLDWEKLLTL RSEGSFLSSP SSTAYALQHT KDELCLDYLL KPVNKFNGGV
PSTYPVDMFE HLWAVDRLQR LGISRYFQVE IGECLDYTFR YWTNEGISWA RYTNIKDSDD
TSMGFRLLRL HGYDISIDAF KAFEKGGEFW CMAGQMGHAV TGVYNLYRAS QLMFPQEHIL
LDARNFSANF LHHKRLTNAI VDKWIISKDL PAEVGYALDV PFYASLPRLE ARFFLEQYGG
DDDVWIGKTL YRMLYVNSNT YLELAKLDYK HCQSVHQLEW KSMQKWYTDC NLGEFGLSEI
SLLLAYYIAA STAFEPEKSG ERLPWATTII LVETIASQQL SNEQKREFVN EFENGSTINN
RNGGRYKPRS RLVDVLINAI TLVAQGRGIS QQLSNAWQKW LKTWEGGGHQ GEAEARLLIH
TLHLSSGLDE SSFSHPKYQQ LLEVTSKVCH QLRLFQNRKV YDAQGCTSRL VTGTTFQTEA
GMQELVKLVF PKTSDDMTSA TKQSFFNIAR SFYYTAYCHE GAIDSHIDKV LFEKIV
