ID   VTSS2_HYOMU             Reviewed;         300 AA.
AC   Q39979;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Vetispiradiene synthase 2;
DE            Short=HVS2;
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; U20189; AAA86338.1; -; mRNA.
DR   PIR; B56118; B56118.
DR   AlphaFoldDB; Q39979; -.
DR   SMR; Q39979; -.
DR   KEGG; ag:AAA86338; -.
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:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR   InterPro; IPR034741; Terpene_cyclase-like_1_C.
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..300
FT                   /note="Vetispiradiene synthase 2"
FT                   /id="PRO_0000398185"
FT   MOTIF           54..58
FT                   /note="DDXXD motif"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         54
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         58
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         197
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         205
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   300 AA;  34959 MW;  9F60D2BAB580A79D CRC64;
     SRWWKDLDFV TTLPYARDRA VECYFWTMGV YAEPQYSQAR VMLAKTIAMI SIVDDTFDAY
     GIVKEFEVYT DAIQRWDISQ IDRLPEYMKI SYKALLDLYD DYEKELSKDG RSDVVHYAKE
     RMKEIVRNYF IEAKWFIEGY MPSVSEYLSN ALATSTYYLL TTTSYLGMKS ATKEHFEWLA
     TNPKILEANA TLCRVVDDIA TYEVEKGRGQ IATGIECYMR DYGVSTEVAM EKFQEMAEIA
     WKDVNEEILR PTPVSAEILT RILNLARIID VTYKHNQDGY THPEKFKPHI IALLVDSIEI