ID   VTSS1_SOLTU             Reviewed;         556 AA.
AC   Q9XJ32;
DT   05-OCT-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Vetispiradiene synthase 1;
DE            EC=4.2.3.21;
GN   Name=PVS1;
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND INDUCTION BY PATHOGEN.
RC   STRAIN=cv. Rishiri; TISSUE=Tuber;
RX   PubMed=10588069; DOI=10.1093/oxfordjournals.pcp.a029633;
RA   Yoshioka H., Yamada N., Doke N.;
RT   "cDNA cloning of sesquiterpene cyclase and squalene synthase, and
RT   expression of the genes in potato tuber infected with Phytophthora
RT   infestans.";
RL   Plant Cell Physiol. 40:993-998(1999).
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:10588069};
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 infection with P.infestans.
CC       {ECO:0000269|PubMed:10588069}.
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; AB022598; BAA82092.1; -; mRNA.
DR   AlphaFoldDB; Q9XJ32; -.
DR   SMR; Q9XJ32; -.
DR   STRING; 4113.PGSC0003DMT400046973; -.
DR   eggNOG; ENOG502QUCN; Eukaryota.
DR   InParanoid; Q9XJ32; -.
DR   BRENDA; 4.2.3.21; 5757.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
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   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   Cytoplasm; Lyase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..556
FT                   /note="Vetispiradiene synthase 1"
FT                   /id="PRO_0000398187"
FT   MOTIF           309..313
FT                   /note="DDXXD motif"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         313
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         452
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         456
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
FT   BINDING         460
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="3"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   556 AA;  64459 MW;  0C82813E48AFDFD9 CRC64;
     MTPAAVVMSN YGEEEIVRPI ADFSPSLWGD RFHSFSLDNQ IAGKYAQEIE TLKEQSRIIL
     SASSRRTLAE KLDLIDIVER LGIAYHFEKQ IDDMLDQFYK ADPNFEAHEY NDLQTLSVQF
     RLLRQHGYNI SPKLFIRFQD AKGKFKESLC NDIKGLLNLY EASHVRTHGE DILEEALAFS
     TAHLESAAPH LKSPLSKQVT HALEQSLHKS IPRVETRYFI SIYEEEEQKN DVLLQFAKLD
     FNLLQMLHKQ ELSEVSRWWK DLDFVTTLPY ARDRAVECYF WTMGVYAEPQ YSQARVMLAK
     TIAMISIVDD TFDAYGIVKE LEIYTDAIQR WDISQIDRLP DYMKISYKAL LDLYNDYEME
     LSKDGRSDVV HYAKERMKEI VRNYFVEAKW FIEGYMPPVS EYLSNALATS TYYLLTTTSY
     LGMKSANKQD FEWLAKNPKI LEANVTLCRV IDDIATYEVE KGRGQIATGI ECYMRDYGVS
     TEKAMEKFQE MAETAWKDVN EGILRPTPVS TEILTRILNL ARIIDVTYKH NQDGYTHPEK
     VLKPHIIALL VDSIEI