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C92C5_MAIZE
ID   C92C5_MAIZE             Reviewed;         531 AA.
AC   A0A1D6HSP4; B6ST66;
DT   03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2016, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Dimethylnonatriene synthase {ECO:0000303|PubMed:27662898};
DE            EC=1.14.14.59 {ECO:0000269|PubMed:27662898};
DE   AltName: Full=Cytochrome P-450 19 {ECO:0000312|EMBL:ONM51434.1};
DE   AltName: Full=Cytochrome P450 92C5 {ECO:0000303|PubMed:27662898};
DE   AltName: Full=Trimethyltridecatetraene synthase {ECO:0000303|PubMed:27662898};
DE            EC=1.14.14.58 {ECO:0000269|PubMed:27662898};
GN   Name=CYP92C5 {ECO:0000303|PubMed:27662898};
GN   ORFNames=ZEAMMB73_Zm00001d018839 {ECO:0000312|EMBL:ONM51434.1};
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. B73; TISSUE=Seedling;
RX   PubMed=19965430; DOI=10.1126/science.1178534;
RA   Schnable P.S., Ware D., Fulton R.S., Stein J.C., Wei F., Pasternak S.,
RA   Liang C., Zhang J., Fulton L., Graves T.A., Minx P., Reily A.D.,
RA   Courtney L., Kruchowski S.S., Tomlinson C., Strong C., Delehaunty K.,
RA   Fronick C., Courtney B., Rock S.M., Belter E., Du F., Kim K., Abbott R.M.,
RA   Cotton M., Levy A., Marchetto P., Ochoa K., Jackson S.M., Gillam B.,
RA   Chen W., Yan L., Higginbotham J., Cardenas M., Waligorski J., Applebaum E.,
RA   Phelps L., Falcone J., Kanchi K., Thane T., Scimone A., Thane N., Henke J.,
RA   Wang T., Ruppert J., Shah N., Rotter K., Hodges J., Ingenthron E.,
RA   Cordes M., Kohlberg S., Sgro J., Delgado B., Mead K., Chinwalla A.,
RA   Leonard S., Crouse K., Collura K., Kudrna D., Currie J., He R.,
RA   Angelova A., Rajasekar S., Mueller T., Lomeli R., Scara G., Ko A.,
RA   Delaney K., Wissotski M., Lopez G., Campos D., Braidotti M., Ashley E.,
RA   Golser W., Kim H., Lee S., Lin J., Dujmic Z., Kim W., Talag J., Zuccolo A.,
RA   Fan C., Sebastian A., Kramer M., Spiegel L., Nascimento L., Zutavern T.,
RA   Miller B., Ambroise C., Muller S., Spooner W., Narechania A., Ren L.,
RA   Wei S., Kumari S., Faga B., Levy M.J., McMahan L., Van Buren P.,
RA   Vaughn M.W., Ying K., Yeh C.-T., Emrich S.J., Jia Y., Kalyanaraman A.,
RA   Hsia A.-P., Barbazuk W.B., Baucom R.S., Brutnell T.P., Carpita N.C.,
RA   Chaparro C., Chia J.-M., Deragon J.-M., Estill J.C., Fu Y., Jeddeloh J.A.,
RA   Han Y., Lee H., Li P., Lisch D.R., Liu S., Liu Z., Nagel D.H., McCann M.C.,
RA   SanMiguel P., Myers A.M., Nettleton D., Nguyen J., Penning B.W.,
RA   Ponnala L., Schneider K.L., Schwartz D.C., Sharma A., Soderlund C.,
RA   Springer N.M., Sun Q., Wang H., Waterman M., Westerman R., Wolfgruber T.K.,
RA   Yang L., Yu Y., Zhang L., Zhou S., Zhu Q., Bennetzen J.L., Dawe R.K.,
RA   Jiang J., Jiang N., Presting G.G., Wessler S.R., Aluru S.,
RA   Martienssen R.A., Clifton S.W., McCombie W.R., Wing R.A., Wilson R.K.;
RT   "The B73 maize genome: complexity, diversity, and dynamics.";
RL   Science 326:1112-1115(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=18937034; DOI=10.1007/s11103-008-9415-4;
RA   Alexandrov N.N., Brover V.V., Freidin S., Troukhan M.E., Tatarinova T.V.,
RA   Zhang H., Swaller T.J., Lu Y.-P., Bouck J., Flavell R.B., Feldmann K.A.;
RT   "Insights into corn genes derived from large-scale cDNA sequencing.";
RL   Plant Mol. Biol. 69:179-194(2009).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND INDUCTION BY HERBIVORES.
RC   STRAIN=cv. B73;
RX   PubMed=27662898; DOI=10.1105/tpc.15.00919;
RA   Richter A., Schaff C., Zhang Z., Lipka A.E., Tian F., Koellner T.G.,
RA   Schnee C., Preiss S., Irmisch S., Jander G., Boland W., Gershenzon J.,
RA   Buckler E.S., Degenhardt J.;
RT   "Characterization of biosynthetic pathways for the production of the
RT   volatile homoterpenes DMNT and TMTT in Zea mays.";
RL   Plant Cell 28:2651-2665(2016).
RN   [4]
RP   PATHWAY, AND REVIEW.
RX   PubMed=30187155; DOI=10.1007/s00425-018-2999-2;
RA   Block A.K., Vaughan M.M., Schmelz E.A., Christensen S.A.;
RT   "Biosynthesis and function of terpenoid defense compounds in maize (Zea
RT   mays).";
RL   Planta 249:21-30(2019).
CC   -!- FUNCTION: Involved in the biosynthesis of homoterpenes, attractants of
CC       herbivores parasitoids and predators (e.g. predatory mites and
CC       parasitoid wasps) (By similarity). Component of the volatile terpenes
CC       biosynthesis pathways (PubMed:30187155). Converts mainly nerolidol to
CC       dimethylnonatriene (DMNT) and, to a lower extent, geranyllinalool to
CC       trimethyltridecatetraene (TMTT) (PubMed:27662898).
CC       {ECO:0000250|UniProtKB:Q9LSF8, ECO:0000269|PubMed:27662898,
CC       ECO:0000303|PubMed:30187155}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(6E,10E)-geranyllinalool + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (3E,7E)-4,8,12-trimethyltrideca 1,3,7,11-tetraene + but-
CC         3-en-2-one + H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:13545, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:48058, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:74299, ChEBI:CHEBI:74322; EC=1.14.14.58;
CC         Evidence={ECO:0000269|PubMed:27662898};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13546;
CC         Evidence={ECO:0000269|PubMed:27662898};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3S,6E)-nerolidol + O2 + reduced [NADPH--hemoprotein
CC         reductase] = (3E)-4,8-dimethylnona-1,3,7-triene + but-3-en-2-one +
CC         H(+) + 2 H2O + oxidized [NADPH--hemoprotein reductase];
CC         Xref=Rhea:RHEA:55424, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:48058, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:59958, ChEBI:CHEBI:60158; EC=1.14.14.59;
CC         Evidence={ECO:0000269|PubMed:27662898};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:55425;
CC         Evidence={ECO:0000269|PubMed:27662898};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000250|UniProtKB:Q96242};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=14.2 uM for (E)-nerolidol {ECO:0000269|PubMed:27662898};
CC         KM=5.6 uM for (6E,10E)-geranyllinalool {ECO:0000269|PubMed:27662898};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC       {ECO:0000305|PubMed:30187155}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Strongly induced in response to herbivory-mediated wounding.
CC       {ECO:0000269|PubMed:27662898}.
CC   -!- DISRUPTION PHENOTYPE: Impaired biosynthesis of dimethylnonatriene
CC       (DMNT), but abnormal accumulation of (E)-nerolidol (PubMed:27662898).
CC       Reduced levels of trimethyltridecatetraene (TMTT) (PubMed:27662898).
CC       {ECO:0000269|PubMed:27662898}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; CM007650; ONM51434.1; -; Genomic_DNA.
DR   EMBL; EU955931; ACG28049.1; -; mRNA.
DR   RefSeq; XP_008652034.1; XM_008653812.1.
DR   AlphaFoldDB; A0A1D6HSP4; -.
DR   SMR; A0A1D6HSP4; -.
DR   STRING; 4577.GRMZM2G102079_P01; -.
DR   EnsemblPlants; Zm00001eb300490_T001; Zm00001eb300490_P001; Zm00001eb300490.
DR   GeneID; 103631958; -.
DR   Gramene; Zm00001eb300490_T001; Zm00001eb300490_P001; Zm00001eb300490.
DR   KEGG; zma:103631958; -.
DR   MaizeGDB; 9035643; -.
DR   eggNOG; KOG0156; Eukaryota.
DR   OMA; ICPAYDL; -.
DR   OrthoDB; 702827at2759; -.
DR   BRENDA; 1.14.14.58; 6752.
DR   BRENDA; 1.14.14.59; 6752.
DR   UniPathway; UPA00213; -.
DR   Proteomes; UP000007305; Chromosome 7.
DR   ExpressionAtlas; A0A1D6HSP4; baseline and differential.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0097007; F:4,8,12-trimethyltrideca-1,3,7,11-tetraene synthase activity; IEA:RHEA.
DR   GO; GO:0102171; F:DMNT synthase activity; IEA:RHEA.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0010333; F:terpene synthase activity; IDA:UniProtKB.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0080027; P:response to herbivore; IEP:UniProtKB.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IDA:UniProtKB.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Membrane; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Plant defense; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..531
FT                   /note="Dimethylnonatriene synthase"
FT                   /id="PRO_0000447524"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   BINDING         464
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|UniProtKB:Q96242"
FT   CONFLICT        526..531
FT                   /note="LYSATE -> F (in Ref. 2; ACG28049)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   531 AA;  57704 MW;  664F765BA033D783 CRC64;
     MELASTMSVA MALAAAIFVV LCSVVASARG RREKALKLPP GPRGWPVLGS LGALAGALPP
     HRALAALAAR HGPLMHLRLG SYHTVVASSA DAARLVLRTH DSALADRPDT AAGEITSYGY
     LGIVHTPRGA YWRMARRLCA TELFSARRVE SFQDVRAQEM RALARGLFGC AAGRRAVAVR
     EHVAGATMRN ILRMAVGEKW SGCYGSPEGE AFRRSLDEAF AATGAVSNVG EWVPWLGWLD
     VQGFKRKMKR LHDLHDHFYE KILVDHEERR RLAQASGGEF VATDLVDVLL QLSEESTKLE
     SESEARLPRD GVKALIQDII AGGTESSAVT IEWAMAELLR HPEAMAKATD ELDRVVGSGR
     WVAERDLPEL HYIDAVVKET LRLHPVGPLL VPHYARERTV VAGYDVPAGA RVLVNAWAIA
     RDPASWPDAP DAFQPERFLG AAAAVDVRGA HFELLPFGSG RRICPAYDLA MKLVAAGVAN
     LVHGFAWRLP DGVAAEDVSM EEHVGLSTRR KVPLFAVAEP RLPVHLYSAT E
 
 
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