ID   DES_SOLLC               Reviewed;         478 AA.
AC   Q9FPM6;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=9-divinyl ether synthase;
DE            Short=LeDES;
DE            EC=4.2.1.121;
DE   AltName: Full=Colneleate synthase;
DE   AltName: Full=Cytochrome P450 74D1;
GN   Name=DES; Synonyms=CYP74D1;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Castlemart;
RX   PubMed=11060314; DOI=10.1074/jbc.m008964200;
RA   Itoh A., Howe G.A.;
RT   "Molecular cloning of a divinyl ether synthase. Identification as a CYP74
RT   cytochrome P-450.";
RL   J. Biol. Chem. 276:3620-3627(2001).
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. Can use (9S,10E,12Z)-9-hydroperoxy-
CC       10,12-octadecadienoic acid (9-HPOD) and (10E,12Z,15Z)-(9S)-9-
CC       hydroperoxyoctadeca-10,12,15-trienoic acid (9-HPOT) as substrates but
CC       has a very low activity with the corresponding 13-hydroperoxides.
CC       {ECO:0000269|PubMed:11060314}.
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:11060314};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=67 uM for (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
CC         {ECO:0000269|PubMed:11060314};
CC         KM=48 uM for (10E,12Z,15Z)-(9S)-9-hydroperoxyoctadeca-10,12,15-
CC         trienoic acid {ECO:0000269|PubMed:11060314};
CC         Note=kcat is 890 sec(-1) for (9S,10E,12Z)-9-hydroperoxy-10,12-
CC         octadecadienoic acid. kcat is 500 sec(-1) for (10E,12Z,15Z)-(9S)-9-
CC         hydroperoxyoctadeca-10,12,15-trienoic acid.;
CC   -!- TISSUE SPECIFICITY: Expressed in roots. Detected in stems, but not in
CC       flower buds, petioles, cotyledons or leaves.
CC       {ECO:0000269|PubMed:11060314}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. 9-divinyl ether
CC       synthase subfamily. {ECO:0000305}.
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DR   EMBL; AF317515; AAG42261.1; -; mRNA.
DR   RefSeq; NP_001234527.1; NM_001247598.1.
DR   AlphaFoldDB; Q9FPM6; -.
DR   SMR; Q9FPM6; -.
DR   STRING; 4081.Solyc01g109140.2.1; -.
DR   PaxDb; Q9FPM6; -.
DR   PRIDE; Q9FPM6; -.
DR   EnsemblPlants; Solyc01g109140.3.1; Solyc01g109140.3.1; Solyc01g109140.3.
DR   GeneID; 543675; -.
DR   Gramene; Solyc01g109140.3.1; Solyc01g109140.3.1; Solyc01g109140.3.
DR   KEGG; sly:543675; -.
DR   eggNOG; ENOG502QV50; Eukaryota.
DR   HOGENOM; CLU_045757_0_0_1; -.
DR   InParanoid; Q9FPM6; -.
DR   OMA; PKIFANP; -.
DR   OrthoDB; 759497at2759; -.
DR   PhylomeDB; Q9FPM6; -.
DR   BRENDA; 4.2.1.121; 3101.
DR   Proteomes; UP000004994; Chromosome 1.
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   Heme; Iron; Lyase; Metal-binding; Reference proteome.
FT   CHAIN           1..478
FT                   /note="9-divinyl ether synthase"
FT                   /id="PRO_0000415389"
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;  54189 MW;  FDF2263339DC0F82 CRC64;
     MSSYSELSNL PIREIPGDYG FPIISAIKDR YDYFYNQGED AWFHNKAEKY KSTVVKINMA
     PGPFTSNDYK LVAFLDANSF VCMFDNSLID KTDTLGGTFK PGKEYYGGYR PVAFIDTKDP
     NHAALKGYIL SSFAKRHNLF IPLFRNTLSD HLFNNLEKQV TEQGKADFNA LLPTMTFDFI
     FRLLCDQKNP SDTVLGAQGP EHLRKWLFPQ LIPSLSAKKL PNIIEDMLFH NFLIPFGFIK
     SDYNKLVDAF SKSAVSMLDE AEKLGIKREE AVQNILFLVG INMFAGLNAF FPHLFRFVGE
     AGASLHTQLA KEIRSVIKEE GGAITLSAIN KMSLVKSVVY ETLRLRPPVP LQYGKAKKEF
     MVQSHDASYK INKGQFVVGY QPMASRDPKI FANPDEFVPD RFMNDGEKML KHVLWSNGRE
     TESPAPDNKQ CPGKDLVHLL GRLILVEFFI RYDTFTLEIT PLFRAPNVAF NTLTKASK