ID   Y1075_MYCLE             Reviewed;         224 AA.
AC   Q9CCA7; Q49969;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Putative O-methyltransferase ML1075;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=ML1075;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Cation-dependent O-methyltransferase family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01019}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA62911.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U15180; AAA62911.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL583920; CAC31456.1; -; Genomic_DNA.
DR   PIR; E87043; E87043.
DR   PIR; T45194; T45194.
DR   RefSeq; NP_301788.1; NC_002677.1.
DR   RefSeq; WP_010908112.1; NC_002677.1.
DR   AlphaFoldDB; Q9CCA7; -.
DR   SMR; Q9CCA7; -.
DR   STRING; 272631.ML1075; -.
DR   EnsemblBacteria; CAC31456; CAC31456; CAC31456.
DR   KEGG; mle:ML1075; -.
DR   PATRIC; fig|272631.5.peg.1928; -.
DR   Leproma; ML1075; -.
DR   eggNOG; COG4122; Bacteria.
DR   HOGENOM; CLU_067676_2_0_11; -.
DR   OMA; RGMRPDG; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002935; SAM_O-MeTrfase.
DR   Pfam; PF01596; Methyltransf_3; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS51682; SAM_OMT_I; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..224
FT                   /note="Putative O-methyltransferase ML1075"
FT                   /id="PRO_0000380097"
FT   BINDING         51
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         73
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         75..76
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         81
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         99
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         100
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ   SEQUENCE   224 AA;  23221 MW;  C83261E091BDB47B CRC64;
     MYGTGNNAVT PDQAAASRAD SLFAHAEGSI SEDAILASAR ERSEEIGARA VTPAVGALLS
     LLTKLSGGKA VAEVGTGAGV SGLWLLSGMS YDGVLTTIDI EPEYLRLAKQ AFSEAGIGPS
     RTRLISGRGQ DVLTRLADES YDLVFIDADP IDQPAYVVEG VRLLRSCGII VVHRAALGGR
     AGDPAARDAE VTAVREAARL IAENERLTPA LVPLGDGLLA AVRE