Y3432_MYCBO
ID Y3432_MYCBO Reviewed; 348 AA.
AC P59986; A0A1R3Y422; X2BNB9;
DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2017, sequence version 3.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Putative S-adenosyl-L-methionine-dependent methyltransferase Mb3432;
DE EC=2.1.1.-;
GN OrderedLocusNames=BQ2027_MB3432;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU02061.1; -; Genomic_DNA.
DR RefSeq; NP_857073.1; NC_002945.3.
DR RefSeq; WP_003900046.1; NC_002945.4.
DR AlphaFoldDB; P59986; -.
DR SMR; P59986; -.
DR EnsemblBacteria; SIU02061; SIU02061; BQ2027_MB3432.
DR PATRIC; fig|233413.5.peg.3767; -.
DR OMA; PFADDHI; -.
DR Proteomes; UP000001419; 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 Mb3432"
FT /id="PRO_0000104117"
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