CPS1_MARVU
ID CPS1_MARVU Reviewed; 776 AA.
AC A0A075FAK4;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Peregrinol diphosphate synthase CPS1, chloroplastic {ECO:0000303|PubMed:24990389};
DE EC=4.2.1.174 {ECO:0000269|PubMed:24990389};
DE AltName: Full=(+)-copalyl diphosphate synthase 1 {ECO:0000303|PubMed:24990389};
DE Short=MvCPS1 {ECO:0000303|PubMed:24990389};
DE Flags: Precursor;
GN Name=CPS1 {ECO:0000303|PubMed:24990389};
OS Marrubium vulgare (White horehound).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lamiaceae; Lamioideae; Marrubieae; Marrubium.
OX NCBI_TaxID=41230;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX PubMed=24990389; DOI=10.1111/tpj.12589;
RA Zerbe P., Chiang A., Dullat H., O'Neil-Johnson M., Starks C., Hamberger B.,
RA Bohlmann J.;
RT "Diterpene synthases of the biosynthetic system of medicinally active
RT diterpenoids in Marrubium vulgare.";
RL Plant J. 79:914-927(2014).
CC -!- FUNCTION: Involved in the biosynthesis of labdane-type diterpenoid
CC including marrubiin and other labdane-related furanoid diterpenoids
CC with potential applications as anti-diabetics, analgesics or
CC vasorelaxants (Probable). Terpene synthase that produces peregrinol
CC diphosphate from geranylgeranyl diphosphate (GGPP) (PubMed:24990389).
CC {ECO:0000269|PubMed:24990389, ECO:0000305|PubMed:24990389}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peregrinol diphosphate = (2E,6E,10E)-geranylgeranyl
CC diphosphate + H2O; Xref=Rhea:RHEA:54652, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:138232; EC=4.2.1.174;
CC Evidence={ECO:0000269|PubMed:24990389};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54654;
CC Evidence={ECO:0000269|PubMed:24990389};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q38802};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305|PubMed:24990389}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Present in both leaves and flowers, with higher
CC levels in leaves. {ECO:0000269|PubMed:24990389}.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ584450; AIE77090.1; -; mRNA.
DR AlphaFoldDB; A0A075FAK4; -.
DR SMR; A0A075FAK4; -.
DR KEGG; ag:AIE77090; -.
DR BRENDA; 4.2.1.174; 15343.
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:0106238; F:peregrinol diphosphate synthase activity; IDA:UniProtKB.
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..17
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 18..776
FT /note="Peregrinol diphosphate synthase CPS1, chloroplastic"
FT /id="PRO_0000449301"
FT MOTIF 371..374
FT /note="DXDD motif"
FT /evidence="ECO:0000305"
FT BINDING 238
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"
SQ SEQUENCE 776 AA; 89510 MW; E4A70BB7C56C505E CRC64;
MASTPTLNLS ITTPFVRTKI PAKISLPACS WLDRSSSRHV ELNHKFCRKL ELKVAMCRAS
LDVQQVRDEV YSNAQPHELV DKKIEERVKY VKNLLSTMDD GRINWSAYDT AWISLIKDFE
GRDCPQFPST LERIAENQLP DGSWGDKDFD CSYDRIINTL ACVVALTTWN VHPEINQKGI
RYLKENMRKL EETPTVLMTC AFEVVFPALL KKARNLGIHD LPYDMPIVKE ICKIGDEKLA
RIPKKMMEKE TTSLMYAAEG VENLDWERLL KLRTPENGSF LSSPAATVVA FMHTKDEDCL
RYIKYLLNKF NGGAPNVYPV DLWSRLWATD RLQRLGISRY FESEIKDLLS YVHSYWTDIG
VYCTRDSKYA DIDDTSMGFR LLRVQGYNMD ANVFKYFQKD DKFVCLGGQM NGSATATYNL
YRAAQYQFPG EQILEDARKF SQQFLQESID TNNLLDKWVI SPHIPEEMRF GMEMTWYSCL
PRIEASYYLQ HYGATEDVWL GKTFFRMEEI SNENYRELAI LDFSKCQAQH QTEWIHMQEW
YESNNVKEFG ISRKDLLFAY FLAAASIFET ERAKERILWA RSKIICKMVK SFLEKETGSL
EHKIAFLTGS GDKGNGPVNN AMATLHQLLG EFDGYISIQL ENAWAAWLTK LEQGEANDGE
LLATTINICG GRVNQDTLSH NEYKALSDLT NKICHNLAQI QNDKGDEIKD SKRSERDKEV
EQDMQALAKL VFEESDLERS IKQTFLAVVR TYYYGAYIAA EKIDVHMFKV LFKPVG
