ID   A0A067L0Y5_JATCU        Unreviewed;      1087 AA.
AC   A0A067L0Y5;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=methionine S-methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00888};
DE            EC=2.1.1.12 {ECO:0000256|PROSITE-ProRule:PRU00888};
GN   ORFNames=JCGZ_24897 {ECO:0000313|EMBL:KDP40898.1};
OS   Jatropha curcas (Barbados nut).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Crotonoideae; Jatropheae;
OC   Jatropha.
OX   NCBI_TaxID=180498 {ECO:0000313|EMBL:KDP40898.1, ECO:0000313|Proteomes:UP000027138};
RN   [1] {ECO:0000313|EMBL:KDP40898.1, ECO:0000313|Proteomes:UP000027138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. GZQX0401 {ECO:0000313|Proteomes:UP000027138};
RC   TISSUE=Young leaves {ECO:0000313|EMBL:KDP40898.1};
RX   PubMed=24837971; DOI=10.1371/journal.pone.0097878;
RA   Zhang L., Zhang C., Wu P., Chen Y., Li M., Jiang H., Wu G.;
RT   "Global Analysis of Gene Expression Profiles in Physic Nut (Jatropha curcas
RT   L.) Seedlings Exposed to Salt Stress.";
RL   PLoS ONE 9:E97878-E97878(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-methionine + S-adenosyl-L-methionine = S-adenosyl-L-
CC         homocysteine + S-methyl-L-methionine; Xref=Rhea:RHEA:13761,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:57856, ChEBI:CHEBI:58252,
CC         ChEBI:CHEBI:59789; EC=2.1.1.12; Evidence={ECO:0000256|PROSITE-
CC         ProRule:PRU00888};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. {ECO:0000256|PROSITE-ProRule:PRU00888}.
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DR   EMBL; KK914327; KDP40898.1; -; Genomic_DNA.
DR   RefSeq; XP_012069132.1; XM_012213742.1.
DR   AlphaFoldDB; A0A067L0Y5; -.
DR   STRING; 180498.A0A067L0Y5; -.
DR   GeneID; 105631576; -.
DR   KEGG; jcu:105631576; -.
DR   OrthoDB; 464292at2759; -.
DR   Proteomes; UP000027138; Unassembled WGS sequence.
DR   GO; GO:0030732; F:methionine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR025779; Met_S-MeTrfase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR007848; Small_mtfrase_dom.
DR   PANTHER; PTHR47087; METHIONINE S-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR47087:SF1; METHIONINE S-METHYLTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   Pfam; PF05175; MTS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51555; SAM_MT12; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|PROSITE-ProRule:PRU00888};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027138};
KW   S-adenosyl-L-methionine {ECO:0000256|PROSITE-ProRule:PRU00888};
KW   Transferase {ECO:0000256|PROSITE-ProRule:PRU00888}.
FT   DOMAIN          114..167
FT                   /note="Methyltransferase small"
FT                   /evidence="ECO:0000259|Pfam:PF05175"
FT   DOMAIN          729..1076
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   1087 AA;  121114 MW;  57EE9EF00ACF0BC5 CRC64;
     MAAFVSMDDF LKNCEQSGDA AYAAFRSLLE RLEDSKTRKE ARIFLSDLHK RVGDSDQCLQ
     KYHFRIQDIF LDQFEGYQGR KKLTMMVIPS IFMPEDWSFT FYEGLNRHPE SIFKDRTVAE
     LGCGNGWISI ALADKWLPSK VYGLDINPRA IKISWINLYL NALDENGQPI YDAEKKTLLE
     RVEFHESDLL AYCRDNDIQL ERIVGCIPQI LNPNPDAMSK MITENASEEF LHSLSNYCAL
     QGFVEDQFGL GLIARAVEEG IAVIKPMGIM IFNMGGRPGQ AVCKRLFERR GFHVSKLWQT
     KVIQAGDTDI SALVEIEKNS PHRFEFFMGL SGDQPICART AWAYGKAGGR IAHALSVYSC
     QLRQPNQVKK IFEFLKNGFQ EVSSSLDLSF VDDSVADEKI PYLAYLAGEL KEQSCFPYES
     PAGSKRFRNL IAGFMKTYHH VPLSSNNVVI FPSRAVAIEN TLRLFSPRLA IVDEHLTRHL
     PRQWLTSLAI EGTENYDPSK DTITVIEAPR QSDLMVELIK KLKPQVVVTG MAQFEAVTSS
     AFIQLLDITR EIGSRLFLDI SDHLELSSLP SPNGVLKYLS GARLPSHAAI LCGLVKNQVY
     SDLEVAFVVS EEEAIFKALS KTVEVLEGNT APIRQFYYGC LFHELLAFQL ADRRPLAERE
     CEKAKSVEAI GFSSSAISVL NDSELSITEE EKSSLIHMDA DQSFLPIPST VKAAIFESFA
     RQNMAESEVD VTPSIKQFIK SNYGFHTDNN TEFVYADFSQ ALLNRLILCC IQEGGTFCFP
     AGSNGNYVSA AKFLKANILS IPTDSASGFK LTDKLLNEAL NTVNKPWVYI SGPTINPTGL
     LYNNKEMESI LTTCAKFGAR VVIDTSFSGL EFDLEGWGGW NLEATLSKLN ASANPSFSVS
     LLGGLSLKLL SGVLKFGFLV LNNPTLVDAF YSFPGLSKPH STVKYAIKKL LGLDESKARD
     LTDDVAEQTR NLKSRSQRMK ETLEKCGWEV LEPCGGVSMM AKPAAYLNKV IKIKHSPEDG
     AGNAAPYEIK LNDSNIRDAI VKSTGLCINS GLWTGIPSYC RFTIALEEND FERALNCIIK
     FKDLISN
//