ID   DES_CAPAN               Reviewed;         478 AA.
AC   Q0PHS9;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=9-divinyl ether synthase;
DE            Short=StDES;
DE            EC=4.2.1.121;
DE   AltName: Full=Colneleate synthase;
DE   AltName: Full=Cytochrome P450 74D4;
GN   Name=DES; Synonyms=CYP74D4;
OS   Capsicum annuum (Capsicum pepper).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX   NCBI_TaxID=4072;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leaf;
RA   Gullner G., Kunstler A., Kiraly L., Pogany M., Tobias I.;
RT   "Induction of divinyl ether synthase gene transcription in pepper leaves
RT   inoculated with Tobamoviruses.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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).
CC   -!- FUNCTION: Involved in the biosynthesis of the anti-fungal toxins
CC       colneleic acid and colnelenic acid. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the cytochrome P450 family. 9-divinyl ether
CC       synthase subfamily. {ECO:0000305}.
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DR   EMBL; DQ832721; ABH03632.1; -; mRNA.
DR   RefSeq; NP_001311513.1; NM_001324584.1.
DR   AlphaFoldDB; Q0PHS9; -.
DR   SMR; Q0PHS9; -.
DR   GeneID; 107840369; -.
DR   KEGG; cann:107840369; -.
DR   Proteomes; UP000189700; Genome assembly.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Heme; Iron; Lyase; Metal-binding.
FT   CHAIN           1..478
FT                   /note="9-divinyl ether synthase"
FT                   /id="PRO_0000415392"
FT   BINDING         431
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;  54035 MW;  25AEB41840094945 CRC64;
     MSSYSESPKL PVREIPGDYG FPIISAIKDR YDYFYNQGED AWFHGKAEKY KSTVVKINMA
     PGPFTSNDYK LVAFLDATSF VYMFDNTLID KTDTLGGTFK PGKEYYGGYR PVAFVDTKDP
     NHAALKGYIL SSFAKRHNLF IPLFRNSLSD HLFNDLEKQV SEQGKSDFNA LLPNMTFGFI
     FRLLCDQTNP SDTVLGAQGP EHLRKWLFPQ LIPSLSARKL PSFIEDLLFH NFLIPFGFVK
     SDYQKLVDAF SKSAVSMLDE AEKLGIKREE AVHNMLFLVG INMFAGLNAF FPHLIRFVGE
     AGPNLHTRLA NEIRTAIKEE GGAITLSAIN KMSLVKSVVY ETLRLRPPVP LQYGKAKKDF
     MVQSHDASYK INKGQFLVGY NPMASRDPKI FANPDEFVPD RFMGDGEKML KHVLWSNGRE
     TENPAPENKQ CAGKDLVQLL GRLILVEFFM RYDTFTVEIT PLFRAPNVAI KTLTKATS