ID   Y733_MYCTA              Reviewed;         301 AA.
AC   A5U0B1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MRA_0733;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MRA_0733;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
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; CP000611; ABQ72461.1; -; Genomic_DNA.
DR   RefSeq; WP_003403687.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U0B1; -.
DR   SMR; A5U0B1; -.
DR   STRING; 419947.MRA_0733; -.
DR   EnsemblBacteria; ABQ72461; ABQ72461; MRA_0733.
DR   KEGG; mra:MRA_0733; -.
DR   eggNOG; COG3315; Bacteria.
DR   HOGENOM; CLU_923843_0_0_11; -.
DR   OMA; FFIKMMD; -.
DR   OrthoDB; 847145at2; -.
DR   Proteomes; UP000001988; 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 MRA_0733"
FT                   /id="PRO_0000361230"
FT   BINDING         130
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         159..160
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   301 AA;  32247 MW;  EE44495196D2A279 CRC64;
     MPRAHDDNWD LASSVGATAT MVAAGRALAT KDPRGLINDP FAEPLVRAVG LDFFTKLIDG
     ELDIATTGNL SPGRAQAMID GIAVRTKYFD DYFRTATDGG VRQVVILAAG LDARAYRLPW
     PAGTVVYEID QPQVIDFKTT TLAGIGAKPT AIRRTVYIDL RADWPAALQA AGLDSTAPTA
     WLAEGMLIYL PPDPRTGCST TAPNSVLRAA RSLPNLSRAL WISTQAGYEK WRIRFASTAW
     TSTWRRWCIP ANAATSSTTC APRAGTLRAQ CGPTYSGAMV CPFPPHTTTI RSAKSSSSAV
     V