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Y1703_MYCTU
ID   Y1703_MYCTU             Reviewed;         233 AA.
AC   L0TAD5;
DT   03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT   03-AUG-2022, sequence version 2.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Probable O-methyltransferase Rv1703c {ECO:0000305};
DE            EC=2.1.1.- {ECO:0000255|PROSITE-ProRule:PRU01019};
GN   OrderedLocusNames=Rv1703c {ECO:0000312|EMBL:CCP44468.1};
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] {ECO:0007744|PubMed:21969609}
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   [3]
RP   PROTEIN SEQUENCE OF 7-49, AND SEQUENCE REVISION TO N-TERMINUS.
RC   STRAIN=H37Rv;
RX   PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA   Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA   Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT   "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT   annotated encoding genes.";
RL   Genomics 114:292-304(2022).
CC   -!- FUNCTION: Specifically methylates an O atom of its substrate.
CC       {ECO:0000305}.
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=CCP44468.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR   EMBL; AL123456; CCP44468.1; ALT_INIT; Genomic_DNA.
DR   SMR; L0TAD5; -.
DR   STRING; 83332.Rv1703c; -.
DR   PaxDb; L0TAD5; -.
DR   PRIDE; L0TAD5; -.
DR   TubercuList; Rv1703c; -.
DR   eggNOG; COG4122; Bacteria.
DR   InParanoid; L0TAD5; -.
DR   OMA; YPSHLEY; -.
DR   PhylomeDB; L0TAD5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0008171; F:O-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   Direct protein sequencing; Metal-binding; Methyltransferase;
KW   Reference proteome; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..233
FT                   /note="Probable O-methyltransferase Rv1703c"
FT                   /id="PRO_0000455998"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         79..80
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         102
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         157
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         159
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         185
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
FT   BINDING         186
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01019"
SQ   SEQUENCE   233 AA;  25205 MW;  74EDA15F29441D83 CRC64;
     MAAGIRNITT TGQIGDGREA AAVDYVLAHA GAGNIDDVLA TIDKFAYEKS MLINVGDEKG
     TLLDAAVRRA DPALALELGT YLGYGALRIA RAAPEARVYS VELAEANASN ARRIWAHAGV
     DDRVVCVVGT IGDGGRTLDA LTEHGFATGT LDFVFLDHDK KAYLPDLQSI LDRGWLHPGS
     IVVADNVRVP GAPKYRAYMR RQQGMSWNTI EHKTHLEYQT LVPDLVLESE YLG
 
 
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