JMT_ARATH
ID JMT_ARATH Reviewed; 389 AA.
AC Q9AR07; Q0WR43; Q9FWR8;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 3.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Jasmonate O-methyltransferase {ECO:0000303|PubMed:11287667};
DE EC=2.1.1.141 {ECO:0000269|PubMed:11287667};
DE AltName: Full=S-adenosyl-L-methionine:jasmonic acid carboxyl methyltransferase {ECO:0000303|PubMed:11287667};
GN Name=JMT {ECO:0000303|PubMed:11287667};
GN OrderedLocusNames=At1g19640 {ECO:0000312|Araport:AT1G19640};
GN ORFNames=F14P1.3 {ECO:0000312|EMBL:AAF98406.1};
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 [GENOMIC DNA / MRNA], FUNCTION, ENZYME ACTIVITY, TISSUE
RP SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND PATHWAY.
RX PubMed=11287667; DOI=10.1073/pnas.081557298;
RA Seo H.S., Song J.T., Cheong J.-J., Lee Y.-H., Lee Y.-W., Hwang I.,
RA Lee J.S., Choi Y.D.;
RT "Jasmonic acid carboxyl methyltransferase: a key enzyme for jasmonate-
RT regulated plant responses.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4788-4793(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the methylation of jasmonate into methyljasmonate,
CC a plant volatile that acts as an important cellular regulator mediating
CC diverse developmental processes and defense responses.
CC {ECO:0000269|PubMed:11287667}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate +
CC S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:13349, ChEBI:CHEBI:15929,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:58431, ChEBI:CHEBI:59789;
CC EC=2.1.1.141; Evidence={ECO:0000269|PubMed:11287667};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9FLN8};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q9FLN8};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=38.5 uM for methyl jasmonate {ECO:0000269|PubMed:11287667};
CC -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000269|PubMed:11287667}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9SBK6}. Nucleus
CC {ECO:0000250|UniProtKB:Q9SBK6}. Note=Predominantly cytoplasmic (By
CC similarity). Partially nuclear (By similarity).
CC {ECO:0000250|UniProtKB:Q9SBK6}.
CC -!- TISSUE SPECIFICITY: Expressed in rosettes, cauline leaves and
CC developing flowers but not in young seedlings.
CC {ECO:0000269|PubMed:11287667}.
CC -!- INDUCTION: By wounding and methyl jasmonate treatment.
CC {ECO:0000269|PubMed:11287667}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF98406.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY008434; AAG23343.1; -; mRNA.
DR EMBL; AY008435; AAG23344.1; -; Genomic_DNA.
DR EMBL; AC024609; AAF98406.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29876.1; -; Genomic_DNA.
DR EMBL; AK228480; BAF00406.1; -; mRNA.
DR PIR; B86329; B86329.
DR RefSeq; NP_173394.1; NM_101820.4.
DR AlphaFoldDB; Q9AR07; -.
DR SMR; Q9AR07; -.
DR STRING; 3702.AT1G19640.1; -.
DR SwissLipids; SLP:000001779; -.
DR PaxDb; Q9AR07; -.
DR PRIDE; Q9AR07; -.
DR ProteomicsDB; 238987; -.
DR EnsemblPlants; AT1G19640.1; AT1G19640.1; AT1G19640.
DR GeneID; 838551; -.
DR Gramene; AT1G19640.1; AT1G19640.1; AT1G19640.
DR KEGG; ath:AT1G19640; -.
DR Araport; AT1G19640; -.
DR TAIR; locus:2013149; AT1G19640.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR HOGENOM; CLU_019628_2_0_1; -.
DR InParanoid; Q9AR07; -.
DR OMA; YYAPCME; -.
DR OrthoDB; 689338at2759; -.
DR BioCyc; ARA:AT1G19640-MON; -.
DR BRENDA; 2.1.1.141; 399.
DR SABIO-RK; Q9AR07; -.
DR UniPathway; UPA00382; -.
DR PRO; PR:Q9AR07; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9AR07; baseline and differential.
DR Genevisible; Q9AR07; AT.
DR GO; GO:0005737; C:cytoplasm; NAS:TAIR.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030795; F:methyl jasmonate methylesterase activity; IDA:TAIR.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009694; P:jasmonic acid metabolic process; IDA:TAIR.
DR GO; GO:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009611; P:response to wounding; IEP:TAIR.
DR Gene3D; 1.10.1200.270; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR005299; MeTrfase_7.
DR InterPro; IPR042086; MeTrfase_capping.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR31009; PTHR31009; 1.
DR Pfam; PF03492; Methyltransf_7; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Methyltransferase; Nucleus; Oxylipin biosynthesis; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..389
FT /note="Jasmonate O-methyltransferase"
FT /id="PRO_0000204464"
FT BINDING 18
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 18
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 21..25
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 59..60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 60
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT BINDING 65
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 95..98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 142..144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 159..161
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 160..164
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 186
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 272
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 275
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 378
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT SITE 157
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 234
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q2HXI6"
FT SITE 353
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT CONFLICT 213
FT /note="W -> L (in Ref. 1; AAG23343/AAG23344)"
FT /evidence="ECO:0000305"
FT CONFLICT 321
FT /note="V -> A (in Ref. 1; AAG23343/AAG23344)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="A -> T (in Ref. 1; AAG23343/AAG23344)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43443 MW; 772F62FC627DB181 CRC64;
MEVMRVLHMN KGNGETSYAK NSTAQSNIIS LGRRVMDEAL KKLMMSNSEI SSIGIADLGC
SSGPNSLLSI SNIVDTIHNL CPDLDRPVPE LRVSLNDLPS NDFNYICASL PEFYDRVNNN
KEGLGFGRGG GESCFVSAVP GSFYGRLFPR RSLHFVHSSS SLHWLSQVPC REAEKEDRTI
TADLENMGKI YISKTSPKSA HKAYALQFQT DFWVFLRSRS EELVPGGRMV LSFLGRRSLD
PTTEESCYQW ELLAQALMSM AKEGIIEEEK IDAFNAPYYA ASSEELKMVI EKEGSFSIDR
LEISPIDWEG GSISEESYDL VIRSKPEALA SGRRVSNTIR AVVEPMLEPT FGENVMDELF
ERYAKIVGEY FYVSSPRYAI VILSLVRAG
