ID   Y4430_MYCUA             Reviewed;         307 AA.
AC   A0PVP6;
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_4430;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MUL_4430;
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; ABL06415.1; -; Genomic_DNA.
DR   RefSeq; WP_011742016.1; NC_008611.1.
DR   AlphaFoldDB; A0PVP6; -.
DR   SMR; A0PVP6; -.
DR   STRING; 362242.MUL_4430; -.
DR   EnsemblBacteria; ABL06415; ABL06415; MUL_4430.
DR   KEGG; mul:MUL_4430; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   OMA; TYPGEHT; -.
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..307
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MUL_4430"
FT                   /id="PRO_0000361248"
FT   BINDING         128
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         157..158
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   307 AA;  32633 MW;  051BF4B9325CBBF7 CRC64;
     MARTEGDSWD LANSVGATAT MVAAARAAAT RRSRPIIADP FAEPLVRAVG LDLFTRAASG
     EVDLDEVAAG LGFVRMVDTF AARALFFDKF FADAIAAGLR QVVIVASGLD ARPYRLPWPT
     GMRVYEIDQP EVIEFKTTTL ARLGASPTAD HHPVGIDLRD DWPSALRAAG FDAARPTAWL
     AEGVRIGFLP PEAETRLLDN VIELSAVGSR LAADYGTING SSAESQQLAQ QMTEGWRAHG
     LDMDIAGLTY PGEHTDVAAY LRSHGWKTAT ADHGDLVLAA GLAELTAADR QSPASTIGFV
     TAVRSTD