DS_VALOF
ID DS_VALOF Reviewed; 556 AA.
AC U3KYL2;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2013, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=(-)-drimenol synthase {ECO:0000303|PubMed:25447532};
DE Short=VoDMS {ECO:0000303|PubMed:25447532};
DE EC=4.2.3.194 {ECO:0000269|PubMed:25447532};
DE AltName: Full=Drimenol cyclase {ECO:0000305};
DE AltName: Full=Sesquiterpene synthase 3 {ECO:0000303|PubMed:25447532};
DE Short=VoTPS3 {ECO:0000303|PubMed:25447532};
OS Valeriana officinalis (Valerian) (Garden heliotrope).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Dipsacales; Caprifoliaceae; Valeriana.
OX NCBI_TaxID=19953;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ASP-307.
RX PubMed=25447532; DOI=10.1016/j.febslet.2014.10.031;
RA Kwon M., Cochrane S.A., Vederas J.C., Ro D.K.;
RT "Molecular cloning and characterization of drimenol synthase from valerian
RT plant (Valeriana officinalis).";
RL FEBS Lett. 588:4597-4603(2014).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) into drimenol, a precursor of the sesquiterpenoid polygodial
CC (PubMed:25447532). Polygodial has been shown to be an antifeedant for a
CC number of herbivorous insects (Probable). {ECO:0000269|PubMed:25447532,
CC ECO:0000305|PubMed:25447532}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + H2O = (5S,9S,10S)-drim-7-en-11-
CC ol + diphosphate; Xref=Rhea:RHEA:28290, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:61148, ChEBI:CHEBI:175763;
CC EC=4.2.3.194; Evidence={ECO:0000269|PubMed:25447532};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28291;
CC Evidence={ECO:0000269|PubMed:25447532};
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=9.6 uM for (2E,6E)-farnesyl diphosphate
CC {ECO:0000269|PubMed:25447532};
CC Note=kcat is 0.025 sec (-1) with (2E,6E)-farnesyl diphosphate as
CC substrate. {ECO:0000269|PubMed:25447532};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000305}.
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:0000269|PubMed:25447532}.
CC -!- SIMILARITY: Belongs to the terpene synthase family. {ECO:0000305}.
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DR EMBL; JQ437841; AFR42419.1; -; mRNA.
DR AlphaFoldDB; U3KYL2; -.
DR SMR; U3KYL2; -.
DR KEGG; ag:AFR42419; -.
DR UniPathway; UPA00213; -.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0010333; F:terpene synthase activity; IEA:InterPro.
DR GO; GO:0016102; P:diterpenoid biosynthetic process; IEA:InterPro.
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; IPR034741; Terpene_cyclase-like_1_C.
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 SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR SUPFAM; SSF48239; SSF48239; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW Lyase; Magnesium; Metal-binding.
FT CHAIN 1..556
FT /note="(-)-drimenol synthase"
FT /id="PRO_0000449920"
FT MOTIF 307..311
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 307
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 311
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 453
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 457
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 461
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT MUTAGEN 307
FT /note="D->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:25447532"
SQ SEQUENCE 556 AA; 64840 MW; DA227AFBBEF28A24 CRC64;
MSTALNSEHE TVRPLASFQP STWGDLFISY SEDSQLKEVY GKEHECLKQQ VKTMLLDVTN
YRISEKIAFI NTLERLGVSH EFENEIEGLL HQMFDAHSKF QDGIQHFDLF TLGIYFRILR
QHGYRIYCDV FNKLKDSNNE FKKELKEDAI GLLSLYEATQ VRAHAEEILD EALIFTKAQL
ESIAATSSLS PFVEKQITHA LVQALHKGIP RVESRHFISV YEEDPDKNDL LLRFSKIDYN
IVQMLHKQEL CHISKWWRDS ELETKLTYAR NRVAECFLWT LCVYHEPKYS PARLLLGKLI
NIISCTDDTY DAYGTLEEVQ IFTDVIQRLD RSSMEQLPDY MKILYKAVLD LFDEVEVQLS
NQETNNTYRM AYAKEELKAI AKCYEKEHIW FRKCHVPPFE EYLENAVVSI GNRLAVTFSF
LGMDQVAAVE AFEWAKTDPK MVKSCGKVLR LVDDVMSHEE EDVRGHVATG VECYMKEHGV
SREEAVVEFY KRVEYAWKDV NEEFITPNHL HIDLLNRVLN LTRIADVVYK FEDGYTHPEK
TLKHHIMALF VDPVPI
