ELS_MARVU
ID ELS_MARVU Reviewed; 580 AA.
AC A0A075FBG7;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 24.
DE RecName: Full=9,13-epoxylabda-14-ene synthase, chloroplastic {ECO:0000303|PubMed:24990389};
DE EC=4.2.3.189 {ECO:0000269|PubMed:24990389};
DE AltName: Full=Manoyl oxide synthase {ECO:0000303|PubMed:24990389};
DE EC=4.2.3.190 {ECO:0000269|PubMed:24990389};
DE AltName: Full=Miltiradiene synthase {ECO:0000303|PubMed:24990389};
DE EC=4.2.3.131 {ECO:0000269|PubMed:24990389};
DE Flags: Precursor;
GN Name=ELS {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 the catalyzes the conversion
CC of peregrinol diphosphate to 9,13(R)-epoxy-labd-14-ene, from (+)-
CC copalyl diphosphate ((+)-CPP) to miltiradiene and from 8-hydroxycopalyl
CC diphosphate (LPP, labda-13-en-8-ol diphosphate) to manoyl oxide
CC (PubMed:24990389). {ECO:0000269|PubMed:24990389,
CC ECO:0000305|PubMed:24990389}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=peregrinol diphosphate = (13R)-9,13-epoxylabd-14-ene +
CC diphosphate; Xref=Rhea:RHEA:54512, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:138232, ChEBI:CHEBI:138233; EC=4.2.3.189;
CC Evidence={ECO:0000269|PubMed:24990389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(+)-copalyl diphosphate = diphosphate + miltiradiene;
CC Xref=Rhea:RHEA:33983, ChEBI:CHEBI:33019, ChEBI:CHEBI:58635,
CC ChEBI:CHEBI:65037; EC=4.2.3.131;
CC Evidence={ECO:0000269|PubMed:24990389};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33984;
CC Evidence={ECO:0000269|PubMed:24990389};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-hydroxycopalyl diphosphate = (13R)-manoyl oxide +
CC diphosphate; Xref=Rhea:RHEA:54516, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:64283, ChEBI:CHEBI:138234; EC=4.2.3.190;
CC Evidence={ECO:0000269|PubMed:24990389};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q40577};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:Q40577};
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-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for
CC the catalytic activity, presumably through binding to Mg(2+).
CC {ECO:0000250|UniProtKB:G8GJ94}.
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; KJ584454; AIE77094.1; -; mRNA.
DR AlphaFoldDB; A0A075FBG7; -.
DR SMR; A0A075FBG7; -.
DR KEGG; ag:AIE77094; -.
DR BRENDA; 4.2.3.189; 15343.
DR BRENDA; 4.2.3.190; 15343.
DR UniPathway; UPA00213; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0106239; F:9,13-epoxylabda-14-ene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0062206; F:manoyl oxide synthase activity; IDA:UniProtKB.
DR GO; GO:0062205; F:miltiradiene synthase activity; IDA:UniProtKB.
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; 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; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Lyase; Magnesium; Metal-binding; Plastid; Transit peptide.
FT TRANSIT 1..32
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 33..580
FT /note="9,13-epoxylabda-14-ene synthase, chloroplastic"
FT /id="PRO_0000449305"
FT MOTIF 322..326
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:G8GJ94"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 322
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 326
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 466
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 474
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
SQ SEQUENCE 580 AA; 67098 MW; 3800598BFDCC5BE0 CRC64;
MSITFNLKIA PFSGPGIQRS KETFPATEIQ ITASTKSTMT TKCSFNASTD FMGKLREKVG
GKADKPPVVI HPVDISSNLC MIDTLQSLGV DRYFQSEINT LLEHTYRLWK EKKKNIIFKD
VSCCAIAFRL LREKGYQVSS DKLAPFADYR IRDVATILEL YRASQARLYE DEHTLEKLHD
WSSNLLKQHL LNGSIPDHKL HKQVEYFLKN YHGILDRVAV RRSLDLYNIN HHHRIPDVAD
GFPKEDFLEY SMQDFNICQA QQQEELHQLQ RWYADCRLDT LNYGRDVVRI ANFLTSAIFG
EPEFSDARLA FAKHIILVTR IDDFFDHGGS REESYKILDL VQEWKEKPAE EYGSKEVEIL
FTAVYNTVND LAEKAHIEQG RCVKPLLIKL WVEILTSFKK ELDSWTEETA LTLDEYLSSS
WVSIGCRICI LNSLQYLGIK LSEEMLSSQE CTDLCRHVSS VDRLLNDVQT FKKERLENTI
NSVGLQLAAH KGERAMTEED AMSKIKEMAD YHRRKLMQIV YKEGTVFPRE CKDVFLRVCR
IGYYLYSSGD EFTSPQQMKE DMKSLVYQPV KIHPLEAINV
