ID   DES_TOBAC               Reviewed;         478 AA.
AC   Q8W2N5;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=9-divinyl ether synthase;
DE            Short=NtDES1;
DE            EC=4.2.1.121;
DE   AltName: Full=Colneleate synthase;
DE   AltName: Full=Cytochrome P450 74D3;
GN   Name=DES1; Synonyms=CYP74D3;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION BY
RP   ELICITOR, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=cv. Wisconsin 38;
RX   PubMed=17085514; DOI=10.1104/pp.106.087304;
RA   Fammartino A., Cardinale F., Gobel C., Mene-Saffrane L., Fournier J.,
RA   Feussner I., Esquerre-Tugaye M.T.;
RT   "Characterization of a divinyl ether biosynthetic pathway specifically
RT   associated with pathogenesis in tobacco.";
RL   Plant Physiol. 143:378-388(2007).
RN   [2]
RP   NOMENCLATURE.
RX   DOI=10.1007/s12042-008-9022-1;
RA   Nelson D.R., Ming R., Alam M., Schuler M.A.;
RT   "Comparison of cytochrome P450 genes from six plant genomes.";
RL   Trop. Plant Biol. 1:216-235(2008).
RN   [3]
RP   INDUCTION BY ELICITOR; ETHYLENE; JASMONIC ACID AND SALICYLIC ACID.
RX   PubMed=20137961; DOI=10.1016/j.plaphy.2010.01.012;
RA   Fammartino A., Verdaguer B., Fournier J., Tamietti G., Carbonne F.,
RA   Esquerre-Tugaye M.T., Cardinale F.;
RT   "Coordinated transcriptional regulation of the divinyl ether biosynthetic
RT   genes in tobacco by signal molecules related to defense.";
RL   Plant Physiol. Biochem. 48:225-231(2010).
CC   -!- FUNCTION: Strictly inducible cytochrome P450 involved in the
CC       biosynthesis of the anti-fungal toxins colneleic acid and colnelenic
CC       acid. Can use (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid (9-
CC       HPOD) and (10E,12Z,15Z)-(9S)-9-hydroperoxyoctadeca-10,12,15-trienoic
CC       acid (9-HPOT) as substrates but has a very low activity with the
CC       corresponding 13-hydroperoxides. {ECO:0000269|PubMed:17085514}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(9S)-hydroperoxy-(10E,12Z)-octadecadienoate = colneleate +
CC         H2O; Xref=Rhea:RHEA:28174, ChEBI:CHEBI:15377, ChEBI:CHEBI:60955,
CC         ChEBI:CHEBI:60957; EC=4.2.1.121;
CC         Evidence={ECO:0000269|PubMed:17085514};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17085514}.
CC   -!- TISSUE SPECIFICITY: Not detected in leaves, stems or roots of healthy
CC       plants. {ECO:0000269|PubMed:17085514}.
CC   -!- INDUCTION: Up-regulated 2 hours after addition of elicitor, with a peak
CC       after 4 hours. In roots inoculated with zoospores of P.parasitica (Ppm
CC       race 0), detected 1 day-post-inoculation. Up-regulated by ethylene and
CC       methyl jasmonate. Not induced systemically. Not induced by salicylic
CC       acid or by wounding. {ECO:0000269|PubMed:17085514,
CC       ECO:0000269|PubMed:20137961}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. 9-divinyl ether
CC       synthase subfamily. {ECO:0000305}.
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DR   EMBL; AF070976; AAL40900.1; -; mRNA.
DR   RefSeq; NP_001312606.1; NM_001325677.1.
DR   AlphaFoldDB; Q8W2N5; -.
DR   SMR; Q8W2N5; -.
DR   STRING; 4097.Q8W2N5; -.
DR   GeneID; 107799697; -.
DR   KEGG; nta:107799697; -.
DR   PhylomeDB; Q8W2N5; -.
DR   BRENDA; 4.2.1.121; 3645.
DR   Proteomes; UP000084051; Unplaced.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0102895; F:colneleate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   GO; GO:0016125; P:sterol metabolic process; IBA:GO_Central.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; SSF48264; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Heme; Iron; Lyase; Metal-binding; Reference proteome.
FT   CHAIN           1..478
FT                   /note="9-divinyl ether synthase"
FT                   /id="PRO_0000415390"
FT   BINDING         432
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   478 AA;  54079 MW;  3EC3624BF0A1BE7B CRC64;
     MSSFLVSSNN LPEREIPGDY GFPIISAIKD RYDYFYKQGE DVWFHSKAEK YNSTVVKINM
     APGPFTSNDY KLVAFLDANS FVYMFDNSLI DKTDTLGGTF KPGKEYYGGY RPVAFVDTSD
     PNHAALKNYI LTSFAKRHNL FIPLFRNSVS DHLFQNLEKQ VSDQGKSDFN ALLPNMTFGF
     IFRLLCDQTN PSDTVLGAQG PEHLRKWLFP QLIPSLSARK LPSFIEDLLF HNFLIPFGLV
     KSDYNKLVDA FSKNAGSMLD EAEKLGIKRE EAVHNILFLV GINMFAGLNA FFPHLIRFVG
     EAGPTLHARL AKEIRTAIKE EGGAVTLSAI NKMSLVESIV YETLRLRPPV PLQYGKAKKD
     FMVQSHDASY MIKKGQFLVG YQPMASRDPK IFDKPDDFIP DRFMGEGVKM LKHVLWSNGR
     ETENPAPDNK QCAGKDLVHL LGRLMLVEFF LRYDTFTVEI TPLFRAPNVA IKTLTKAT