EKS_MARVU
ID EKS_MARVU Reviewed; 756 AA.
AC A0A075FBT3;
DT 22-APR-2020, integrated into UniProtKB/Swiss-Prot.
DT 29-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 26.
DE RecName: Full=Ent-kaurene synthase, chloroplastic {ECO:0000303|PubMed:24990389};
DE EC=4.2.3.19 {ECO:0000269|PubMed:24990389};
DE Flags: Fragment;
GN Name=EKS {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 ent-kaurene
CC from ent-copalyl diphosphate (ent-CPP) (PubMed:24990389).
CC {ECO:0000269|PubMed:24990389, ECO:0000305|PubMed:24990389}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene;
CC Xref=Rhea:RHEA:22220, ChEBI:CHEBI:15415, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:58553; EC=4.2.3.19;
CC Evidence={ECO:0000269|PubMed:24990389};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22221;
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: Plant hormone biosynthesis; gibberellin biosynthesis.
CC {ECO:0000305|PubMed:24990389}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC Single-pass membrane protein {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Present in both leaves and flowers.
CC {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}.
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DR EMBL; KJ584453; AIE77093.1; -; mRNA.
DR AlphaFoldDB; A0A075FBT3; -.
DR SMR; A0A075FBT3; -.
DR UniPathway; UPA00390; -.
DR GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0009899; F:ent-kaurene synthase activity; IDA:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0009686; P:gibberellin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00684; Terpene_cyclase_plant_C1; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR Gene3D; 1.50.10.130; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR044814; Terpene_cyclase_plant_C1.
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; Membrane; Metal-binding; Plastid;
KW Transmembrane; Transmembrane helix.
FT CHAIN <1..756
FT /note="Ent-kaurene synthase, chloroplastic"
FT /id="PRO_0000449304"
FT TRANSMEM 606..622
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 507..511
FT /note="DDXXD motif"
FT /evidence="ECO:0000250|UniProtKB:G8GJ94"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 507
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 511
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 651
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 655
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 659
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT NON_TER 1
SQ SEQUENCE 756 AA; 86373 MW; 22333C9A744082EC CRC64;
IDESQTSLDT GVQRFTSSKI ASSVQCFEDT KARIVKLIHK PELSVSTYDT AWVAMVPSPN
SSNEPCFPDC LAWLLENQCC DGSWACPHHH PFLKKDVLSS TLACILALKK WGVGEEQINK
GARFIEVNFA SATEKSQISP TGFDIIFPAM LDYARDLFLD LRLEPTTFDN LIFRRDLELK
RCYESHREAY LAYIAEGMGK LQDWESVMKY QRKNGSLFNS PSTTAAAFIA LPNSGCLSYL
HSALKKFGNA VPAAYPLDVY SRLRTVDNLE SLGISRYFQK EIQQVLDETY RWWLQGSEEI
FLDASTCALA FRTLRMNGYN VTSDAITKLL PDSFCGNMKD IGTTLELYRA SEFILYPDEK
DLEQQNLRLK DILEQELSSG FIHSEVNRAL NYPFYAIMDR VAKRRNIEHY NFDNTRILKT
SYCSPNFANK DFLFLSVEDF NNCQAMHREE LKGKMRWVTE NRLDELKFAR SKSAYCYFSA
AATFFAPDLS DARMSWAKNG VLTTVVDDFF DVGGSEEELK QLIRLVEIWD LDAITECSSQ
NVQIIFSSLK RTISEIGDKG FKLQGRSVTN HIIEIWLDLL YSMMKEAEWA RDNHAPPMDD
YISNAYVSFA LGPIVLPCLY LVGPKLSEEM VRHSECHTLF RLMSTCGRLL NDIQTCEREL
KDGKLNAIPL YMINSGGETS KEAATQEMKS LIDRQRQELL RLVLTREGSL LPKPCKELFW
HMSTVLHLFY CKDDGFTSQD LIKVVNEVIH EPVVLN
