ID   Y851_MYCTO              Reviewed;         301 AA.
AC   P9WFI2; L0T7M5; O53841; Q7D977;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 33.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT0851;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT0851;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK45092.1; -; Genomic_DNA.
DR   PIR; F70811; F70811.
DR   RefSeq; WP_003404349.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFI2; -.
DR   SMR; P9WFI2; -.
DR   EnsemblBacteria; AAK45092; AAK45092; MT0851.
DR   GeneID; 45424793; -.
DR   KEGG; mtc:MT0851; -.
DR   PATRIC; fig|83331.31.peg.911; -.
DR   HOGENOM; CLU_056160_2_1_11; -.
DR   Proteomes; UP000001020; 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 MT0851"
FT                   /id="PRO_0000428534"
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;  33416 MW;  5F6C68208D1E6199 CRC64;
     MVRADRDRWD LATSVGATAT MVAAQRALAA DPRYALIDDP YAAPLVRAVG MDVYTRLVDW
     QIPVEGDSEF DPQRMATGMA CRTRFFDQFF LDATHSGIGQ FVILASGLDA RAYRLAWPVG
     SIVYEVDMPE VIEFKTATLS DLGAEPATER RTVAVDLRDD WATALQTAGF DPKVPAAWSA
     EGLLVYLPVE AQDALFDNIT ALSAPGSRLA FEFVPDTAIF ADERWRNYHN RMSELGFDID
     LNELVYHGQR GHVLDYLTRD GWQTSALTVT QLYEANGFAY PDDELATAFA DLTYSSATLM
     R