DES_SOLTU
ID DES_SOLTU Reviewed; 478 AA.
AC Q9AVQ1;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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 74D2;
GN Name=DES; Synonyms=CYP74D2;
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], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY PATHOGEN, AND TISSUE
RP SPECIFICITY.
RC STRAIN=cv. Desiree;
RX PubMed=11696374; DOI=10.1016/s0014-5793(01)03019-8;
RA Stumpe M., Kandzia R., Gobel C., Rosahl S., Feussner I.;
RT "A pathogen-inducible divinyl ether synthase (CYP74D) from elicitor-treated
RT potato suspension cells.";
RL FEBS Lett. 507:371-376(2001).
RN [2]
RP FUNCTION.
RC STRAIN=cv. Desiree;
RX PubMed=17258245; DOI=10.1016/j.phytochem.2006.12.010;
RA Eschen-Lippold L., Rothe G., Stumpe M., Goebel C., Feussner I., Rosahl S.;
RT "Reduction of divinyl ether-containing polyunsaturated fatty acids in
RT transgenic potato plants.";
RL Phytochemistry 68:797-801(2007).
RN [3]
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 [4]
RP INDUCTION BY PATHOGEN.
RC STRAIN=cv. Bintje, cv. Cara, cv. Desiree, cv. Esterling, and cv. Matilda;
RX PubMed=18538577; DOI=10.1016/j.plaphy.2008.04.010;
RA Fauconnier M.L., Rojas-Beltran J., Dupuis B., Delaplace P., Frettinger P.,
RA Gosset V., du Jardin P.;
RT "Changes in oxylipin synthesis after Phytophthora infestans infection of
RT potato leaves do not correlate with resistance.";
RL Plant Physiol. Biochem. 46:823-831(2008).
CC -!- FUNCTION: Involved in the biosynthesis of the anti-fungal and
CC antibacterial toxins colneleic acid and colnelenic acid. Can use
CC (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid (9-HPOD) and
CC (10E,12Z,15Z)-(9S)-9-hydroperoxyoctadeca-10,12,15-trienoic acid (9-
CC HPOT) as substrates but has no activity with the corresponding 13-
CC hydroperoxides. {ECO:0000269|PubMed:11696374,
CC ECO:0000269|PubMed:17258245}.
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:11696374};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17.4 uM for (9S,10E,12Z)-9-hydroperoxy-10,12-octadecadienoic acid
CC {ECO:0000269|PubMed:11696374};
CC KM=26.1 uM for (10E,12Z,15Z)-(9S)-9-hydroperoxyoctadeca-10,12,15-
CC trienoic acid {ECO:0000269|PubMed:11696374};
CC Vmax=5.3 umol/min/mg enzyme with (9S,10E,12Z)-9-hydroperoxy-10,12-
CC octadecadienoic acid as substrate {ECO:0000269|PubMed:11696374};
CC Vmax=2.8 umol/min/mg enzyme with (10E,12Z,15Z)-(9S)-9-
CC hydroperoxyoctadeca-10,12,15-trienoic acid as substrate
CC {ECO:0000269|PubMed:11696374};
CC pH dependence:
CC Optimum pH is 5.5 - 7.5. {ECO:0000269|PubMed:11696374};
CC -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:11696374}.
CC -!- INDUCTION: Up-regulated 6 and 12 hours-post-infection after
CC infiltration with P.syringae pv. maculicola and between 2 and 4 dpi
CC after infection by P.infestans. {ECO:0000269|PubMed:11696374,
CC ECO:0000269|PubMed:18538577}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. 9-divinyl ether
CC synthase subfamily. {ECO:0000305}.
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DR EMBL; AJ309541; CAC28152.1; -; mRNA.
DR RefSeq; NP_001305517.1; NM_001318588.1.
DR AlphaFoldDB; Q9AVQ1; -.
DR SMR; Q9AVQ1; -.
DR STRING; 4113.PGSC0003DMT400064771; -.
DR GeneID; 102588225; -.
DR KEGG; ag:CAC28152; -.
DR KEGG; sot:102588225; -.
DR eggNOG; ENOG502QV50; Eukaryota.
DR InParanoid; Q9AVQ1; -.
DR BioCyc; MetaCyc:MON-12728; -.
DR BRENDA; 4.2.1.121; 5757.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR ExpressionAtlas; Q9AVQ1; baseline.
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_0000415391"
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; 54114 MW; 59EA8DFFCE1C6EBB CRC64;
MSSYSELSNL PIREIPGDYG FPIISAIKDR YDYFYNQGED AWFHNKAEKY KSTVVKINMA
PGPFTSNDYK LVAFLDANSF VCMFDNSLID KTDTLGGTFK PGKEYYSGYR PVAFIDTKDP
NHAALKGYIL SAFAKRHNLF IPLFRNSLSD HLFNNLEKQV TEQGKSDFNA LLPTMTFNFI
FRLLCDQTNP SDTVLGAQGP EHLRKWLFPQ LIPSLSAKKL PNIIEDTLFH NFLIPFGFIK
SDYNKLVDAF SKSAVSILDE AEKLGIKREE AVQNILFLVG INMFAGLNAF SPHLFRFVGE
AGASLHTQLA KEIRTVIKEE GGAITLSAIN KMSLVKSVVY ETLRLRPPVP LQYGKAKKDF
MVQSHDASYK INKGQFVVGY QPMASRDPKI FANPDEFVPD RFMNDGEKML KHVLWSNGRE
TENPAPDNKQ CPGKDLVHLL GRLILVEFFM RYDTFTVEIT PLFRAPNVAF KTLTKASK
