OGT_MYCBO
ID OGT_MYCBO Reviewed; 165 AA.
AC P0A697; A0A1R3XY02; Q10627; X2BHK8;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
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};
GN OrderedLocusNames=BQ2027_MB1349C;
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: 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; LT708304; SIT99952.1; -; Genomic_DNA.
DR RefSeq; NP_855003.1; NC_002945.3.
DR RefSeq; WP_003406857.1; NC_002945.4.
DR AlphaFoldDB; P0A697; -.
DR SMR; P0A697; -.
DR EnsemblBacteria; SIT99952; SIT99952; BQ2027_MB1349C.
DR GeneID; 45425292; -.
DR PATRIC; fig|233413.5.peg.1479; -.
DR OMA; INNPKSC; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-UniRule.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Cytoplasm; DNA damage; DNA repair; Methyltransferase; Transferase.
FT CHAIN 1..165
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139370"
FT ACT_SITE 126
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
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
