ID   Y450_MYCUA              Reviewed;         301 AA.
AC   A0PLD8;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MUL_0450;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_0450;
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; ABL03157.1; -; Genomic_DNA.
DR   RefSeq; WP_011738782.1; NC_008611.1.
DR   AlphaFoldDB; A0PLD8; -.
DR   SMR; A0PLD8; -.
DR   STRING; 362242.MUL_0450; -.
DR   PRIDE; A0PLD8; -.
DR   EnsemblBacteria; ABL03157; ABL03157; MUL_0450.
DR   KEGG; mul:MUL_0450; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; TRFYDQF; -.
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..301
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_0450"
FT                   /id="PRO_0000361249"
FT   BINDING         127
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         156..157
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  33003 MW;  2C9C0386623339FE CRC64;
     MVRTDRDRWD LATSVGATAT MVAAQRALAA DPQYALIDDP YAAPLVRAVD IDVYTRLVNG
     QIPVDVESGF DPARMPEAMA CRTRFYDQFF VDATRSGISQ VVILASGLDA RAYRLGWPAG
     TVVHEVDMPQ VIEFKTLTLA DLGAKPTAER RTVAVDLRDD WAAVLQAAGF DKDVPSAWSA
     EGLLVYLPDD AQGALFDNVT ALSATGSRLA FEFVPDTAVF NDERWRSHHA RMSELGFEID
     FNDLVYHGQR SHVIDHLARD GWQSASHTAK ELHAANGLDY PDDDIAAVFA DITYTSAVLG
     R