OGT_MYCTU
ID OGT_MYCTU Reviewed; 165 AA.
AC P9WJW5; L0T9A0; P0A696; Q10627;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE EC=2.1.1.63 {ECO:0000255|HAMAP-Rule:MF_00772};
DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE Short=MGMT {ECO:0000255|HAMAP-Rule:MF_00772};
DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
GN Name=ogt {ECO:0000255|HAMAP-Rule:MF_00772}; OrderedLocusNames=Rv1316c;
GN ORFNames=MTCY130.01c;
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 [GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RA Bourn W.R., Harington A., Wiid I., van Helden P.D.;
RT "Mycobacterium tuberculosis 3-methyladenine glycosidase and O6-
RT methylguanine methyltransferase genes.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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).
CC -!- FUNCTION: Involved in the cellular defense against the biological
CC effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in
CC DNA. Repairs the methylated nucleobase in DNA by stoichiometrically
CC transferring the methyl group to a cysteine residue in the enzyme. This
CC is a suicide reaction: the enzyme is irreversibly inactivated.
CC {ECO:0000255|HAMAP-Rule:MF_00772}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein]
CC = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:11367, Rhea:RHEA-COMP:11368, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a
CC thymidine in DNA + S-methyl-L-cysteinyl-[protein];
CC Xref=Rhea:RHEA:53428, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:10132,
CC Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, ChEBI:CHEBI:29950,
CC ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, ChEBI:CHEBI:137387;
CC EC=2.1.1.63; Evidence={ECO:0000255|HAMAP-Rule:MF_00772};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}.
CC -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and therefore is
CC not strictly catalytic. According to one definition, an enzyme is a
CC biocatalyst that acts repeatedly and over many reaction cycles.
CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000255|HAMAP-
CC Rule:MF_00772}.
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DR EMBL; U65786; AAB06752.1; -; Genomic_DNA.
DR EMBL; AL123456; CCP44073.1; -; Genomic_DNA.
DR PIR; H70768; H70768.
DR RefSeq; NP_215832.1; NC_000962.3.
DR RefSeq; WP_003406857.1; NZ_NVQJ01000059.1.
DR PDB; 4BHB; X-ray; 1.80 A; A=3-165.
DR PDB; 4BHC; X-ray; 2.80 A; A=3-165.
DR PDB; 4WX9; X-ray; 3.00 A; A/B/C=1-165.
DR PDB; 4WXC; X-ray; 2.60 A; A=1-165.
DR PDB; 4WXD; X-ray; 2.30 A; A=1-165.
DR PDBsum; 4BHB; -.
DR PDBsum; 4BHC; -.
DR PDBsum; 4WX9; -.
DR PDBsum; 4WXC; -.
DR PDBsum; 4WXD; -.
DR AlphaFoldDB; P9WJW5; -.
DR SMR; P9WJW5; -.
DR STRING; 83332.Rv1316c; -.
DR PaxDb; P9WJW5; -.
DR DNASU; 886913; -.
DR GeneID; 45425292; -.
DR GeneID; 886913; -.
DR KEGG; mtu:Rv1316c; -.
DR TubercuList; Rv1316c; -.
DR eggNOG; COG0350; Bacteria.
DR OMA; INNPKSC; -.
DR PhylomeDB; P9WJW5; -.
DR BRENDA; 2.1.1.63; 3445.
DR BRENDA; 6.3.4.21; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IDA:MTBBASE.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0051409; P:response to nitrosative stress; IDA:MTBBASE.
DR CDD; cd06445; ATase; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_00772; OGT; 1.
DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS.
DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR InterPro; IPR008332; MethylG_MeTrfase_N.
DR InterPro; IPR023546; MGMT.
DR InterPro; IPR036631; MGMT_N_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01035; DNA_binding_1; 1.
DR Pfam; PF02870; Methyltransf_1N; 1.
DR SUPFAM; SSF46767; SSF46767; 1.
DR SUPFAM; SSF53155; SSF53155; 1.
DR TIGRFAMs; TIGR00589; ogt; 1.
DR PROSITE; PS00374; MGMT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; Methyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..165
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139369"
FT ACT_SITE 126
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:4BHB"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:4BHB"
FT STRAND 22..27
FT /evidence="ECO:0007829|PDB:4BHB"
FT HELIX 35..39
FT /evidence="ECO:0007829|PDB:4BHB"
FT STRAND 40..42
FT /evidence="ECO:0007829|PDB:4WXC"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:4WXC"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:4BHB"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:4BHB"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:4BHB"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:4BHB"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:4BHB"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:4BHB"
FT TURN 139..141
FT /evidence="ECO:0007829|PDB:4BHB"
FT HELIX 142..154
FT /evidence="ECO:0007829|PDB:4BHB"
FT HELIX 161..164
FT /evidence="ECO:0007829|PDB:4BHB"
SQ SEQUENCE 165 AA; 17858 MW; 081F482D1E796E64 CRC64;
MIHYRTIDSP IGPLTLAGHG SVLTNLRMLE QTYEPSRTHW TPDPGAFSGA VDQLNAYFAG
ELTEFDVELD LRGTDFQQRV WKALLTIPYG ETRSYGEIAD QIGAPGAARA VGLANGHNPI
AIIVPCHRVI GASGKLTGYG GGINRKRALL ELEKSRAPAD LTLFD
