ID   Y4762_MYCUA             Reviewed;         310 AA.
AC   A0PWG3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_4762;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_4762;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- FUNCTION: Exhibits S-adenosyl-L-methionine-dependent methyltransferase
CC       activity. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR   EMBL; CP000325; ABL06682.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0PWG3; -.
DR   SMR; A0PWG3; -.
DR   STRING; 362242.MUL_4762; -.
DR   EnsemblBacteria; ABL06682; ABL06682; MUL_4762.
DR   KEGG; mul:MUL_4762; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; PMDITEL; -.
DR   Proteomes; UP000000765; Chromosome.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR011610; CHP00027_methylltransferase.
DR   InterPro; IPR007213; Ppm1/Ppm2/Tcmp.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04072; LCM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00027; mthyl_TIGR00027; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..310
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_4762"
FT                   /id="PRO_0000361251"
FT   BINDING         132
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         161..162
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   310 AA;  34535 MW;  DBE6FB1E4C68B24F CRC64;
     MRTHDDTWDI RTSVGATAVM VAAARAVETS KPEPLIRDPY ARMLVTNANA GVIWEAMLDQ
     EMVAKVEAID AETAATVEHM RSYQAVRTNF FDTYFADAVA AGIRQVVILA SGLDSRAYRL
     DWPAGTTVYE IDQPQVLAYK SATLAENGVT PAAERREVAI DLRQDWPSAL RAAGFDPSAR
     TAWLAEGLLM YLPAEAQDRL FTQIGELSCA GSRIAAETAG NHADERREQM RERFRKVAQT
     LGLEQTIDVH ELIYHDPDRA PLGQWLNEHG WRANAQNACD EMHRVGRWVE GVPMADDKQA
     YSDFVTAERL