JMT_BRARP
ID JMT_BRARP Reviewed; 392 AA.
AC Q9SBK6;
DT 21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Jasmonate O-methyltransferase {ECO:0000305};
DE EC=2.1.1.141 {ECO:0000250|UniProtKB:Q9AR07};
DE AltName: Full=Floral nectary-specific protein 1 {ECO:0000303|PubMed:10809010};
DE AltName: Full=S-adenosyl-L-methionine:jasmonic acid carboxyl methyltransferase {ECO:0000305};
GN Name=JMT {ECO:0000305}; Synonyms=NTR1 {ECO:0000303|PubMed:10809010};
OS Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX NCBI_TaxID=51351;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RC TISSUE=Flower;
RX PubMed=10809010; DOI=10.1023/a:1006381625421;
RA Song J.T., Seo H.S., Song S.I., Lee J.S., Choi Y.D.;
RT "NTR1 encodes a floral nectary-specific gene in Brassica campestris L. ssp.
RT pekinensis.";
RL Plant Mol. Biol. 42:647-655(2000).
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:0000250|UniProtKB:Q9AR07}.
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:0000250|UniProtKB:Q9AR07};
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 -!- PATHWAY: Lipid metabolism; oxylipin biosynthesis.
CC {ECO:0000250|UniProtKB:Q9AR07}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10809010}. Nucleus
CC {ECO:0000269|PubMed:10809010}. Note=Predominantly cytoplasmic
CC (PubMed:10809010). Partially nuclear (PubMed:10809010).
CC {ECO:0000269|PubMed:10809010}.
CC -!- TISSUE SPECIFICITY: Specifically expressed to the flower base.
CC Localizes specifically to both the lateral and median nectaries of
CC flowers (at protein level). {ECO:0000269|PubMed:10809010}.
CC -!- DEVELOPMENTAL STAGE: Increases with flower development, especially
CC during nectary development, but decreases abruptly with the opening of
CC the flower. {ECO:0000269|PubMed:10809010}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; AF179222; AAF22289.1; -; mRNA.
DR AlphaFoldDB; Q9SBK6; -.
DR SMR; Q9SBK6; -.
DR STRING; 51351.Q9SBK6; -.
DR EnsemblPlants; Bra016498.1; Bra016498.1-P; Bra016498.
DR Gramene; Bra016498.1; Bra016498.1-P; Bra016498.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR HOGENOM; CLU_019628_2_0_1; -.
DR InParanoid; Q9SBK6; -.
DR OMA; RKASHIN; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000011750; Chromosome A08.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-EC.
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:0032259; P:methylation; IBA:GO_Central.
DR GO; GO:0031408; P:oxylipin biosynthetic process; IEA:UniProtKB-UniPathway.
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..392
FT /note="Jasmonate O-methyltransferase"
FT /id="PRO_0000204465"
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 145..147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 162..164
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 163..167
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 190
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 278
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 381
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT SITE 160
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 238
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q2HXI6"
SQ SEQUENCE 392 AA; 43816 MW; 25B78530E93B5757 CRC64;
MEVMRILHMN KGNGETSYAK NSIVQSNIIS LGRRVMDEAL KKLMIRNSEI LSFGIADLGC
SSGPNSLLSI SNIVETIQNL CHDLDRPVPE LSLSLNDLPS NDFNYIFASL PEFYDRVKKR
DNNYESLGFE HGSGGPCFVS AVPGSFYGRL FPRRSLHFVH SSSSLHWLSQ VPCGEVNKKD
GVVITADLDN RGKIYLSKTS PKSAHKVYAL QFQTDFSVFL RSRSEELVPG GRMVLSFLGR
SSPDPTTEES CYQWELLAQA LMSLAKEGII EEENIDAFNA PYYAASPEEL KMAIEKEGSF
SIDRLEISPV DWEGGSISDD SYDIVRFKPE ALASGRRVAK TIRAVVEPML EPTFGQKVMD
ELFERYAKLV GEYVYVSSPR YTIVIVSLLR MG
