C82G1_ARATH
ID C82G1_ARATH Reviewed; 515 AA.
AC Q9LSF8; F4J8Y2;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Dimethylnonatriene synthase {ECO:0000303|PubMed:21088219};
DE EC=1.14.14.59 {ECO:0000269|PubMed:21088219};
DE AltName: Full=Cytochrome P450 82G1 {ECO:0000303|PubMed:21088219};
DE AltName: Full=Protein OVIPOSITION RATE 9 {ECO:0000303|PubMed:26699853};
DE AltName: Full=Trimethyltridecatetraene synthase {ECO:0000303|PubMed:21088219};
DE EC=1.14.14.58 {ECO:0000269|PubMed:21088219};
GN Name=CYP82G1 {ECO:0000303|PubMed:21088219};
GN Synonyms=OR9 {ECO:0000303|PubMed:26699853};
GN OrderedLocusNames=At3g25180 {ECO:0000312|Araport:AT3G25180};
GN ORFNames=MJL12.5 {ECO:0000312|EMBL:BAB02077.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:131-135(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RX PubMed=14993207; DOI=10.1101/gr.1515604;
RA Castelli V., Aury J.-M., Jaillon O., Wincker P., Clepet C., Menard M.,
RA Cruaud C., Quetier F., Scarpelli C., Schaechter V., Temple G., Caboche M.,
RA Weissenbach J., Salanoubat M.;
RT "Whole genome sequence comparisons and 'full-length' cDNA sequences: a
RT combined approach to evaluate and improve Arabidopsis genome annotation.";
RL Genome Res. 14:406-413(2004).
RN [4]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY, TISSUE
RP SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=21088219; DOI=10.1073/pnas.1009975107;
RA Lee S., Badieyan S., Bevan D.R., Herde M., Gatz C., Tholl D.;
RT "Herbivore-induced and floral homoterpene volatiles are biosynthesized by a
RT single P450 enzyme (CYP82G1) in Arabidopsis.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:21205-21210(2010).
RN [5]
RP REVIEW.
RX PubMed=21334702; DOI=10.1016/j.phytochem.2011.01.019;
RA Tholl D., Sohrabi R., Huh J.-H., Lee S.;
RT "The biochemistry of homoterpenes--common constituents of floral and
RT herbivore-induced plant volatile bouquets.";
RL Phytochemistry 72:1635-1646(2011).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=26699853; DOI=10.1371/journal.pone.0145124;
RA Broekgaarden C., Bucher J., Bac-Molenaar J., Keurentjes J.J., Kruijer W.,
RA Voorrips R.E., Vosman B.;
RT "Novel genes affecting the interaction between the cabbage whitefly and
RT Arabidopsis uncovered by genome-wide association mapping.";
RL PLoS ONE 10:E0145124-E0145124(2015).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=29271603; DOI=10.1111/mpp.12654;
RA Rajarammohan S., Pradhan A.K., Pental D., Kaur J.;
RT "Genome-wide association mapping in Arabidopsis identifies novel genes
RT underlying quantitative disease resistance to Alternaria brassicae.";
RL Mol. Plant Pathol. 19:1719-1732(2018).
RN [8]
RP INDUCTION BY 8-HYDROXY-7-KETO-D-CADINENE AND PSEUDOMONAS SYRINGAE.
RX PubMed=30967019; DOI=10.1098/rstb.2018.0319;
RA Tian X., Fang X., Huang J.-Q., Wang L.-J., Mao Y.-B., Chen X.-Y.;
RT "A gossypol biosynthetic intermediate disturbs plant defence response.";
RL Philos. Trans. R. Soc. Lond., B, Biol. Sci. 374:20180319-20180319(2019).
CC -!- FUNCTION: Involved in the biosynthesis of homoterpenes, attractants of
CC herbivores parasitoids and predators (e.g. predatory mites and
CC parasitoid wasps) (PubMed:21334702). Catalyzes the conversion of the
CC C20 (E,E)-geranyllinalool to C16-homoterpene 4,8,12-trimethyltrideca-
CC 1,3,7,11-tetraene (TMTT) of the C15 (E)-nerolidol to C11-homoterpene
CC (E)-4,8-dimethyl-1,3,7-nonatriene (DMNT); these volatile compounds are
CC produced upon insect herbivore attack and emitted from flowers and
CC vegetative tissues during herbivore feeding (PubMed:21088219). Required
CC during resistance responses to the fungus Alternaria brassicae
CC (PubMed:29271603). Prevents oviposition of the phloem-feeding insect
CC cabbage whitefly (Aleyrodes proletella) (PubMed:26699853).
CC {ECO:0000269|PubMed:21088219, ECO:0000269|PubMed:26699853,
CC ECO:0000269|PubMed:29271603, ECO:0000303|PubMed:21334702}.
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:21088219};
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:21088219};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000250|UniProtKB:P04798};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.68 uM for (E,E)-geranyllinalool {ECO:0000269|PubMed:21088219};
CC KM=1.84 uM for (E)-nerolidol {ECO:0000269|PubMed:21088219};
CC Vmax=16.37 pmol/sec/mg enzyme toward (E,E)-geranyllinalool
CC {ECO:0000269|PubMed:21088219};
CC Vmax=29.09 pmol/sec/mg enzyme toward (E)-nerolidol
CC {ECO:0000269|PubMed:21088219};
CC -!- PATHWAY: Secondary metabolite biosynthesis; terpenoid biosynthesis.
CC {ECO:0000269|PubMed:21088219}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9LSF8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9LSF8-2; Sequence=VSP_041620, VSP_041621;
CC -!- TISSUE SPECIFICITY: Expressed in stems, flower peduncles, receptacle of
CC developing and mature flowers and in stigma of mature opening flower
CC buds. {ECO:0000269|PubMed:21088219}.
CC -!- INDUCTION: By wounding, upon insect feeding, by the fungal elicitor
CC alamethicin and infection with the bacterial pathogen Pseudomonas
CC syringae DC3000 (PubMed:21088219). Induced by the biosynthetic
CC intermediate 8-hydroxy-7-keto-d-cadinene (C234), especially in synergy
CC with the bacterial pathogen P.syringae pv. maculicola (Psm)
CC (PubMed:30967019). {ECO:0000269|PubMed:21088219,
CC ECO:0000269|PubMed:30967019}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions, but loss of TMTT production after alamethicin elicitation
CC (PubMed:21088219). Enhanced susceptibility to the fungus Alternaria
CC brassicae (PubMed:29271603). Increased oviposition rate of the phloem-
CC feeding insect cabbage whitefly (Aleyrodes proletella)
CC (PubMed:26699853). {ECO:0000269|PubMed:21088219,
CC ECO:0000269|PubMed:26699853, ECO:0000269|PubMed:29271603}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BX822752; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB026647; BAB02077.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76989.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76990.1; -; Genomic_DNA.
DR EMBL; BX822302; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BX822752; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_189154.1; NM_113423.4. [Q9LSF8-1]
DR RefSeq; NP_974359.1; NM_202630.2. [Q9LSF8-2]
DR AlphaFoldDB; Q9LSF8; -.
DR SMR; Q9LSF8; -.
DR STRING; 3702.AT3G25180.1; -.
DR iPTMnet; Q9LSF8; -.
DR PaxDb; Q9LSF8; -.
DR PRIDE; Q9LSF8; -.
DR ProteomicsDB; 239211; -. [Q9LSF8-1]
DR EnsemblPlants; AT3G25180.1; AT3G25180.1; AT3G25180. [Q9LSF8-1]
DR EnsemblPlants; AT3G25180.2; AT3G25180.2; AT3G25180. [Q9LSF8-2]
DR GeneID; 822110; -.
DR Gramene; AT3G25180.1; AT3G25180.1; AT3G25180. [Q9LSF8-1]
DR Gramene; AT3G25180.2; AT3G25180.2; AT3G25180. [Q9LSF8-2]
DR KEGG; ath:AT3G25180; -.
DR Araport; AT3G25180; -.
DR TAIR; locus:2090275; AT3G25180.
DR eggNOG; KOG0156; Eukaryota.
DR HOGENOM; CLU_001570_4_0_1; -.
DR InParanoid; Q9LSF8; -.
DR OMA; NHQHARE; -.
DR OrthoDB; 702827at2759; -.
DR PhylomeDB; Q9LSF8; -.
DR BioCyc; ARA:AT3G25180-MON; -.
DR BioCyc; MetaCyc:AT3G25180-MON; -.
DR BRENDA; 1.14.14.58; 399.
DR BRENDA; 1.14.14.59; 399.
DR UniPathway; UPA00213; -.
DR PRO; PR:Q9LSF8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LSF8; baseline and differential.
DR Genevisible; Q9LSF8; AT.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0097008; F:(3E)-4,8-dimethyl-1,3,7-nonatriene synthase activity; IDA:TAIR.
DR GO; GO:0097007; F:4,8,12-trimethyltrideca-1,3,7,11-tetraene synthase activity; IDA:TAIR.
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:0050832; P:defense response to fungus; IMP:UniProtKB.
DR GO; GO:0002213; P:defense response to insect; IMP:UniProtKB.
DR GO; GO:0098542; P:defense response to other organism; IBA:GO_Central.
DR GO; GO:1901045; P:negative regulation of oviposition; IMP:UniProtKB.
DR GO; GO:0009617; P:response to bacterium; IEP:UniProtKB.
DR GO; GO:0046246; P:terpene biosynthetic process; IDA:TAIR.
DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniPathway.
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 Alternative splicing; Heme; Iron; Isopeptide bond; Membrane; Metal-binding;
KW Monooxygenase; Oxidoreductase; Plant defense; Reference proteome;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..515
FT /note="Dimethylnonatriene synthase"
FT /id="PRO_0000411200"
FT TRANSMEM 3..23
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000255"
FT BINDING 452
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:P04798"
FT CROSSLNK 252
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q9SZU1"
FT VAR_SEQ 383..402
FT /note="IREAREDCFVGGYRVEKGTR -> HKSKNLYCHYNSYFMTLLIL (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_041620"
FT VAR_SEQ 403..515
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14993207"
FT /id="VSP_041621"
SQ SEQUENCE 515 AA; 58570 MW; 4F5A92951A10447C CRC64;
MTFLFSTLQL SLFSLALVIF GYIFLRKQLS RCEVDSSTIP EPLGALPLFG HLHLLRGKKL
LCKKLAAMSQ KHGPIFSLKL GFYRLVVASD PKTVKDCFTT NDLATATRPN IAFGRYVGYN
NASLTLAPYG DYWRELRKIV TVHLFSNHSI EMLGHIRSSE VNTLIKHLYK GNGGTSIVKI
DMLFEFLTFN IILRKMVGKR IGFGEVNSDE WRYKEALKHC EYLAVIPMIG DVIPWLGWLD
FAKNSQMKRL FKELDSVNTK WLHEHLKKRS RNEKDQERTI MDLLLDILPE DIVISGHVRD
VIVKATILAL TLTGSDSTSI TLTWAVSLLL NNPAALEAAQ EEIDNSVGKG RWIEESDIQN
LKYLQAIVKE THRLYPPAPL TGIREAREDC FVGGYRVEKG TRLLVNIWKL HRDPKIWPDP
KTFKPERFME DKSQCEKSNF EYIPFGSGRR SCPGVNLGLR VVHFVLARLL QGFELHKVSD
EPLDMAEGPG LALPKINPVE VVVMPRLDPK LYSLL
