DS_PERHD
ID DS_PERHD Reviewed; 559 AA.
AC W0FFD7;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 19-MAR-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=(-)-drimenol synthase {ECO:0000303|PubMed:28258968};
DE Short=PhDS {ECO:0000303|PubMed:28258968};
DE EC=4.2.3.194 {ECO:0000269|PubMed:28258968};
DE AltName: Full=Drimenol cyclase {ECO:0000305};
DE AltName: Full=Sesquiterpene synthase {ECO:0000305};
OS Persicaria hydropiper (Marshpepper knotweed) (Polygonum hydropiper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Polygonaceae; Polygonoideae; Persicarieae; Persicaria.
OX NCBI_TaxID=46901;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=28258968; DOI=10.1111/tpj.13527;
RA Henquet M.G.L., Prota N., van der Hooft J.J.J., Varbanova-Herde M.,
RA Hulzink R.J.M., de Vos M., Prins M., de Both M.T.J., Franssen M.C.R.,
RA Bouwmeester H., Jongsma M.;
RT "Identification of a drimenol synthase and drimenol oxidase from Persicaria
RT hydropiper, involved in the biosynthesis of insect deterrent drimanes.";
RL Plant J. 90:1052-1063(2017).
CC -!- FUNCTION: Catalyzes the conversion of (2E,6E)-farnesyl diphosphate
CC (FPP) into drimenol, a precursor of the sesquiterpenoid polygodial
CC (PubMed:28258968). Polygodial has been shown to be an antifeedant for a
CC number of herbivorous insects (Probable). {ECO:0000269|PubMed:28258968,
CC ECO:0000305|PubMed:28258968}.
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:28258968};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28291;
CC Evidence={ECO:0000269|PubMed:28258968};
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}.
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:0000305|PubMed:28258968}.
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; KC754968; AHF22834.1; -; mRNA.
DR PDB; 7CJY; X-ray; 2.20 A; A/B=19-559.
DR PDBsum; 7CJY; -.
DR AlphaFoldDB; W0FFD7; -.
DR SMR; W0FFD7; -.
DR KEGG; ag:AHF22834; -.
DR BRENDA; 4.2.3.194; 13328.
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 3D-structure; Lyase; Magnesium; Metal-binding.
FT CHAIN 1..559
FT /note="(-)-drimenol synthase"
FT /id="PRO_0000449919"
FT MOTIF 311..315
FT /note="DDXXD motif"
FT /evidence="ECO:0000305"
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 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 315
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 460
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT BINDING 464
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:Q40577"
FT TURN 28..33
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 39..65
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 90..102
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 113..125
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 132..138
FT /evidence="ECO:0007829|PDB:7CJY"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 147..151
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 163..165
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 171..190
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 197..205
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 232..264
FT /evidence="ECO:0007829|PDB:7CJY"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:7CJY"
FT TURN 272..275
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 294..315
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 320..332
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 343..345
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 346..363
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 364..366
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 372..394
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 401..407
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 409..413
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 415..424
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 427..429
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 432..439
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 443..460
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 463..465
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 473..481
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 485..506
FT /evidence="ECO:0007829|PDB:7CJY"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 515..531
FT /evidence="ECO:0007829|PDB:7CJY"
FT STRAND 540..542
FT /evidence="ECO:0007829|PDB:7CJY"
FT HELIX 543..553
FT /evidence="ECO:0007829|PDB:7CJY"
SQ SEQUENCE 559 AA; 64727 MW; 50241585142B2CAF CRC64;
MSTAVNVPSA VRPADKRPIA SFHPSPWGDY FLKYVPCDQV TQAKMEDEVK KVEEDVKKEL
RKLAKAVGKP LELLNFIDVV ERLGVGYRLE QEIEDLVQAI FDNDKFGVDE FDLYHTSLWF
RLLRQHGFHV SCDVFGKFKG RNGRFKDSLA SDVKGILGLY EASHVRTHGD DTLDEALVFT
TTHLKAVVTN QPNHPLVPQV THALMQPYHK GMPRLESRHF IAFYEKDPYH DKTLLKFGKL
DFNLVQALHK KELKDLSRWW KDLDMHAKMP FPSRDRVPEG YFWTLGPFYE PQFALCRKFF
LQVFKVTSIV DDIYDAYGTI DELTAFTKAA ERWDRSCLDE LPEYMKVSYA SLIDTFEEFE
RDLAPQGRSW SVKYAREEMI QMCRVYYQEA KWCHEKYSPT CDEYLEKASI VSFGYNLGTV
VCFLGMGDVA TKEAFEWARG NPKVVRAAGI IGRLMDDIGS HHFEQGRDHV PSAVECYIRQ
HGVDEVTAQR ELGKRVESSW KDINEMMLKP YMMPKPLLTR ILNECRIVDV IYKGEDSYTF
SNTTMKKNIS HILTDPIPI
