JMT2_THECC
ID JMT2_THECC Reviewed; 373 AA.
AC A0A061FBW2;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=Probable jasmonic acid carboxyl methyltransferase 2 {ECO:0000312|EMBL:EOY14825.1};
DE EC=2.1.1.141 {ECO:0000250|UniProtKB:Q9AR07};
GN ORFNames=TCM_034091 {ECO:0000312|EMBL:EOY14825.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6;
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Livingstone D. III,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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: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 -!- SIMILARITY: Belongs to the methyltransferase superfamily. Type-7
CC methyltransferase family. {ECO:0000305}.
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DR EMBL; CM001886; EOY14825.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FBW2; -.
DR SMR; A0A061FBW2; -.
DR STRING; 3641.EOY14825; -.
DR EnsemblPlants; EOY14825; EOY14825; TCM_034091.
DR Gramene; EOY14825; EOY14825; TCM_034091.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR HOGENOM; CLU_019628_2_0_1; -.
DR OMA; YYAPCME; -.
DR OrthoDB; 689338at2759; -.
DR UniPathway; UPA00382; -.
DR Proteomes; UP000026915; Chromosome 8.
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: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 3: Inferred from homology;
KW Cytoplasm; Magnesium; Metal-binding; Methyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..373
FT /note="Probable jasmonic acid carboxyl methyltransferase 2"
FT /id="PRO_0000451778"
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 58..59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A0A6C0WW36"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE70"
FT BINDING 94..97
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 135..137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 152..154
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 153..157
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 263
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q9FLN8"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:A4GE69"
FT SITE 150
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q9FZN8"
FT SITE 222
FT /note="Involved in substrate discrimination"
FT /evidence="ECO:0000250|UniProtKB:Q2HXI6"
SQ SEQUENCE 373 AA; 41388 MW; 05BFC15A0CD26C0A CRC64;
MEVMQVLHMN KGNGETSYAK NSTVQSKIIS VGKPIIEEAV HEISCNNLLE SMGIADLGCS
SGPNTLSVIS EIMDMVQTTS RRLGRPVPEF RVYLNDLYSN DFNYIFMSLP AFYHRLKEEK
GIGCGSCYIS GVAGSFYGRL FPSKSLHFVH SSSSLHWLSQ VPPGLESKAL APLNKGKVYI
SKSSPQSVLN AYSLQFQNDF SMFIESRSQE LVPGGRMVLS FMGRRSTDPT TEESCHHWEL
LAQAIMSLVR EGLIEEAKVD SFNAPYYAPC AEEIKVEIQK VGSFVIDRLE GFEIDWDGGA
VSDVQTAQGK LLIGQRVAKT IRAVVESMLE SHFGIGQDIM DDLFSRYAEI VGNHLSKTRT
KYINLVISLI KKG
