ID   Y3399_MYCTO             Reviewed;         348 AA.
AC   P9WFH0; L0TFA0; Q50726;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2017, sequence version 2.
DT   03-AUG-2022, entry version 27.
DE   RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase MT3507;
DE            EC=2.1.1.-;
GN   OrderedLocusNames=MT3507;
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|UniProtKB:Q9CCZ4}.
CC   -!- SIMILARITY: Belongs to the UPF0677 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK47844.1; -; Genomic_DNA.
DR   PIR; D70735; D70735.
DR   RefSeq; WP_003900046.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WFH0; -.
DR   SMR; P9WFH0; -.
DR   EnsemblBacteria; AAK47844; AAK47844; MT3507.
DR   KEGG; mtc:MT3507; -.
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..348
FT                   /note="Putative S-adenosyl-L-methionine-dependent
FT                   methyltransferase MT3507"
FT                   /id="PRO_0000428540"
FT   BINDING         171
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CCZ4"
FT   BINDING         200..201
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250|UniProtKB:Q9CCZ4"
SQ   SEQUENCE   348 AA;  38198 MW;  8C06DE947EFEBFBD CRC64;
     MARPMGKLPS NTRKCAQCAM AEALLEIAGQ TINQKDLGRS GRMTRTDNDT WDLASSVGAT
     ATMIATARAL ASRAENPLIN DPFAEPLVRA VGIDLFTRLA SGELRLEDIG DHATGGRWMI
     DNIAIRTKFY DDFFGDATTA GIRQVVILAA GLDTRAYRLP WPPGTVVYEI DQPAVIKFKT
     RALANLNAEP NAERHAVAVD LRNDWPTALK NAGFDPARPT AFSAEGLLSY LPPQGQDRLL
     DAITALSAPD SRLATQSPLV LDLAEEDEKK MRMKSAAEAW RERGFDLDLT ELIYFDQRND
     VADYLAGSGW QVTTSTGKEL FAAQGLPPFE DDHITRFADR RYISAVLK