ID   VTSS3_HYOMU             Reviewed;         350 AA.
AC   Q39980;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Vetispiradiene synthase 3;
DE            Short=HVS3;
DE            EC=4.2.3.21;
DE   Flags: Fragment;
OS   Hyoscyamus muticus (Egyptian henbane).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Hyoscyameae;
OC   Hyoscyamus.
OX   NCBI_TaxID=35626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND INDUCTION BY ELICITOR.
RX   PubMed=7706281; DOI=10.1074/jbc.270.13.7375;
RA   Back K., Chappell J.;
RT   "Cloning and bacterial expression of a sesquiterpene cyclase from
RT   Hyoscyamus muticus and its molecular comparison to related terpene
RT   cyclases.";
RL   J. Biol. Chem. 270:7375-7381(1995).
CC   -!- FUNCTION: Sesquiterpene synthase that catalyzes the formation of
CC       vetispiradiene from trans,trans-farnesyl diphosphate. The initial
CC       internal cyclization produces the monocyclic intermediate germacrene A.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate = (-)-vetispiradiene +
CC         diphosphate; Xref=Rhea:RHEA:10340, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46971, ChEBI:CHEBI:175763; EC=4.2.3.21;
CC         Evidence={ECO:0000269|PubMed:7706281};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: By elicitor from R.solani. {ECO:0000269|PubMed:7706281}.
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   -!- SIMILARITY: Belongs to the terpene synthase family. Tpsa subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U20190; AAA86339.1; -; mRNA.
DR   PIR; C56118; C56118.
DR   AlphaFoldDB; Q39980; -.
DR   SMR; Q39980; -.
DR   KEGG; ag:AAA86339; -.
DR   UniPathway; UPA00213; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0034003; F:vetispiradiene synthase activity; IEA:UniProtKB-EC.
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   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR034741; Terpene_cyclase-like_1_C.
DR   InterPro; IPR044814; Terpene_cyclase_plant_C1.
DR   InterPro; IPR005630; Terpene_synthase_metal-bd.
DR   Pfam; PF03936; Terpene_synth_C; 1.
DR   SFLD; SFLDG01019; Terpene_Cyclase_Like_1_C_Termi; 1.
DR   SUPFAM; SSF48576; SSF48576; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Lyase; Magnesium; Metal-binding.
FT   CHAIN           <1..350
FT                   /note="Vetispiradiene synthase 3"
FT                   /id="PRO_0000398186"
FT   MOTIF           103..107
FT                   /note="DDXXD motif"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         103
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         107
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         250
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         254
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   350 AA;  41104 MW;  FEE71BC7EFEADAAE CRC64;
     LHKSIPRVET RYFITIYEEE ELKNDVLLRF AKLDFNLLQM LHKQELTEVS MWWKDLDFVT
     TLPYARDRAV ECYFWTVGVY AEPQYSEARV MLAKTIAMIS IVDDTFDAYG IVKELEVYTD
     AIQRWDINQI DRLPDYMKIS YKVLLDLYKD YETELSKDGR SEVVHYAKER MKEIVRNYFV
     EAKWFIEGYM PPVSEYLNNR LATSTYYLLT TTSYLGMKCA NKEDFEWLTK NPKILEANVT
     LCRVIDDIAT YEVEKGRGQI ATGIECYMRD YGVSTEEAME KFQEMAEIAW KDVNEGILRP
     TPVSAKILTR ILNLARIIDV TYLHNQDGYT HPEKVLKPHI IALVVDSIEI