JMT1_THECC
ID JMT1_THECC Reviewed; 373 AA.
AC A0A061FDP1;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 03-SEP-2014, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=Probable jasmonic acid carboxyl methyltransferase 1 {ECO:0000312|EMBL:EOY14822.1};
DE EC=2.1.1.141 {ECO:0000250|UniProtKB:Q9AR07};
GN ORFNames=TCM_034089 {ECO:0000312|EMBL:EOY14822.1};
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; EOY14822.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FDP1; -.
DR SMR; A0A061FDP1; -.
DR STRING; 3641.EOY14822; -.
DR EnsemblPlants; EOY14822; EOY14822; TCM_034089.
DR Gramene; EOY14822; EOY14822; TCM_034089.
DR eggNOG; ENOG502QQYU; Eukaryota.
DR HOGENOM; CLU_019628_2_0_1; -.
DR OMA; ADTHTEQ; -.
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 1"
FT /id="PRO_0000451777"
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; 41465 MW; 33B07DAF27FEB8A9 CRC64;
MEVMQVLHMN RGNGENSYAK NSTVQSKIIS IGKPIIEEAV HEISCNNVLE SMGIADLGCS
SGPNTLCVIS EIMDMVQATS HRLGHPVPEF RLYLNDLYSN DFNSIFMSLP AFYHRLKEEK
GIGCGSCFIS GVAGSFYGRL FPSKSLHYVH SSSSLHWLSQ VPPGLESNAV TPLNKGKVYI
SKSSPHSVLH AYSLQFQNDF PMFIESRSQE LVSGGRMVLS LFGRRSTDPT TEESCYQWEL
LAQAIMSLVR EGLIEEEKVD SFNTPFYAPC AEEIKVEIQK EGSFIIDRLE GFEIDWDGGA
VSDVHTAQGK LLIGQRAAKA LRAVVESMLE SHFGIGQDIM DDLFSRYAEI VGNHLSKTRT
KYFNLVISLT RKG
