Y1229_MYCTA
ID Y1229_MYCTA Reviewed; 224 AA.
AC A5U1R8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Putative O-methyltransferase MRA_1229;
DE EC=2.1.1.-;
GN OrderedLocusNames=MRA_1229;
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 -!- 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=ABQ72968.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000611; ABQ72968.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_003911448.1; NZ_CP016972.1.
DR AlphaFoldDB; A5U1R8; -.
DR SMR; A5U1R8; -.
DR STRING; 419947.MRA_1229; -.
DR EnsemblBacteria; ABQ72968; ABQ72968; MRA_1229.
DR GeneID; 45425190; -.
DR KEGG; mra:MRA_1229; -.
DR eggNOG; COG4122; Bacteria.
DR HOGENOM; CLU_067676_2_0_11; -.
DR Proteomes; UP000001988; Chromosome.
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..224
FT /note="Putative O-methyltransferase MRA_1229"
FT /id="PRO_0000380104"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 75..76
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 149
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ SEQUENCE 224 AA; 23033 MW; 7C1B06934AE8E060 CRC64;
MDGTPGHDDM PGQPAPSRGE SLWAHAEGSI SEDVILAGAR ERATDIGAGA VTPAVGALLC
LLAKLSGGKA VAEVGTGAGV SGLWLLSGMR DDGVLTTIDI EPEHLRLARQ AFAEAGIGPS
RTRLISGRAQ EVLTRLADAS YDLVFIDADP IDQPDYVAEG VRLLRSGGVI VVHRAALGGR
AGDPGARDAE VIAVREAARL IAEDERLTPA LVPLGDGVLA AVRD