Y1220_MYCTU
ID Y1220_MYCTU Reviewed; 224 AA.
AC P9WJZ7; L0T607; O33219; Q7D8K9;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 04-FEB-2015, sequence version 2.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Probable O-methyltransferase Rv1220c {ECO:0000305};
DE Short=MtbOMT {ECO:0000303|PubMed:28580918};
DE EC=2.1.1.-;
GN OrderedLocusNames=Rv1220c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [4] {ECO:0007744|PDB:5X7F}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 10-224 IN COMPLEX WITH
RP S-ADENOSYL-L-METHIONINE, PROBABLE FUNCTION, NO METAL COFACTOR, SUBUNIT, AND
RP PROBABLE ACTIVE SITE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=28580918; DOI=10.1107/s2053230x17006057;
RA Yan Q., Shaw N., Qian L., Jiang D.;
RT "Crystal structure of Rv1220c, a SAM-dependent O-methyltransferase from
RT Mycobacterium tuberculosis.";
RL Acta Crystallogr. F Struct. Biol. Commun. 73:315-320(2017).
CC -!- FUNCTION: Probably specifically methylates an O atom of its substrate.
CC {ECO:0000305|PubMed:28580918}.
CC -!- COFACTOR:
CC Note=Does not seem to have metal cofactors; no metal ions were found
CC via inductively coupled plasma atomic emission spectroscopy, and the
CC residues that bind metal in homologs are not conserved.
CC {ECO:0000269|PubMed:28580918};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:28580918}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
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 -!- CAUTION: It is not clear if Met-1 or Met-10 is the start codon.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP43976.1; Type=Erroneous initiation; Note=Truncated N-terminus.;
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DR EMBL; AL123456; CCP43976.1; ALT_INIT; Genomic_DNA.
DR PIR; G70507; G70507.
DR RefSeq; NP_215736.1; NC_000962.3.
DR RefSeq; WP_003911448.1; NZ_NVQJ01000039.1.
DR PDB; 5X7F; X-ray; 2.00 A; A=10-224.
DR PDBsum; 5X7F; -.
DR AlphaFoldDB; P9WJZ7; -.
DR SMR; P9WJZ7; -.
DR STRING; 83332.Rv1220c; -.
DR PaxDb; P9WJZ7; -.
DR GeneID; 45425190; -.
DR GeneID; 888419; -.
DR KEGG; mtu:Rv1220c; -.
DR PATRIC; fig|83332.12.peg.1368; -.
DR TubercuList; Rv1220c; -.
DR eggNOG; COG4122; Bacteria.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008171; F:O-methyltransferase activity; IEA:InterPro.
DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..224
FT /note="Probable O-methyltransferase Rv1220c"
FT /id="PRO_0000380105"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:28580918"
FT BINDING 51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01019,
FT ECO:0000269|PubMed:28580918, ECO:0007744|PDB:5X7F"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:5X7F"
FT BINDING 80..81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:5X7F"
FT BINDING 81
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:28580918,
FT ECO:0007744|PDB:5X7F"
FT BINDING 99..100
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:5X7F"
FT BINDING 99
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:28580918,
FT ECO:0007744|PDB:5X7F"
FT BINDING 104
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:28580918,
FT ECO:0007744|PDB:5X7F"
FT BINDING 129..130
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:5X7F"
FT BINDING 129
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:28580918,
FT ECO:0007744|PDB:5X7F"
FT BINDING 147
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000269|PubMed:28580918,
FT ECO:0007744|PDB:5X7F"
FT BINDING 156
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0007744|PDB:5X7F"
FT HELIX 21..27
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 34..45
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:5X7F"
FT STRAND 68..74
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 80..86
FT /evidence="ECO:0007829|PDB:5X7F"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 102..114
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:5X7F"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:5X7F"
FT STRAND 141..146
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:5X7F"
FT STRAND 164..174
FT /evidence="ECO:0007829|PDB:5X7F"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:5X7F"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:5X7F"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:5X7F"
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
