ID   Y4009_MYCSJ             Reviewed;         220 AA.
AC   A3Q3Q7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Putative O-methyltransferase Mjls_4009;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=Mjls_4009;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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=ABN99784.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000580; ABN99784.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; A3Q3Q7; -.
DR   SMR; A3Q3Q7; -.
DR   STRING; 164757.Mjls_4009; -.
DR   KEGG; mjl:Mjls_4009; -.
DR   HOGENOM; CLU_067676_2_0_11; -.
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; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..220
FT                   /note="Putative O-methyltransferase Mjls_4009"
FT                   /id="PRO_0000380101"
FT   BINDING         47
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         71..72
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         143
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ   SEQUENCE   220 AA;  22734 MW;  2B397A303AB6B6BE CRC64;
     MASTDDPAGQ RPSRAEAIVA HAEQSISEDA IVAAARERAV DIGAGAVTPA VGALLSVLAR
     LTEAKAVVEV GTGAGVSGLW LLSGMREDGV LTTIDVEPEH QRIAKQAFIE AGIGPSRTRL
     ISGRAQEVLT RLADESYDLV FIDGDPADQP QFVVEGVRLL RPGGAIVVHR AALGGRAGDA
     AANDAEVSAV REAARLIAED ERLTPVLVPL GDGLLVAARD