OGT_SALTY
ID OGT_SALTY Reviewed; 171 AA.
AC P0A2U0; P37429; Q56015;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=STM1659;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29631 / TA 1538;
RX PubMed=7883708; DOI=10.1128/jb.177.6.1511-1519.1995;
RA Yamada M., Sedgwick B., Sofuni T., Nohmi T.;
RT "Construction and characterization of mutants of Salmonella typhimurium
RT deficient in DNA repair of O6-methylguanine.";
RL J. Bacteriol. 177:1511-1519(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 57-171.
RA Lee A.A., Miller C.G., Lombardo M.;
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U23465; AAC43323.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20577.1; -; Genomic_DNA.
DR EMBL; U05668; AAA16267.1; -; Unassigned_DNA.
DR RefSeq; NP_460618.1; NC_003197.2.
DR RefSeq; WP_000945036.1; NC_003197.2.
DR AlphaFoldDB; P0A2U0; -.
DR SMR; P0A2U0; -.
DR STRING; 99287.STM1659; -.
DR PaxDb; P0A2U0; -.
DR EnsemblBacteria; AAL20577; AAL20577; STM1659.
DR GeneID; 1253177; -.
DR KEGG; stm:STM1659; -.
DR PATRIC; fig|99287.12.peg.1753; -.
DR HOGENOM; CLU_000445_52_2_6; -.
DR OMA; SACAMNA; -.
DR PhylomeDB; P0A2U0; -.
DR BioCyc; SENT99287:STM1659-MON; -.
DR Proteomes; UP000001014; 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; Reference proteome;
KW Transferase.
FT CHAIN 1..171
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139372"
FT ACT_SITE 139
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
FT CONFLICT 104..121
FT /note="QVMHYGQLAAQLGRPGAA -> RSCTMVNWRRNWDDRAVR (in Ref. 3;
FT AAA16267)"
FT /evidence="ECO:0000305"
FT CONFLICT 146..147
FT /note="NG -> KR (in Ref. 3; AAA16267)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 171 AA; 19008 MW; F1CBBD2A2ADBDAD9 CRC64;
MLRLLEEKIA TPLGPLWVVC DEQFRLRAIE WEQYRDRMEQ LLNIHYRHEG YERVSATNPG
GLSDKLADYF AGNLAVIDTL ETATGGTPFQ REVWQALRAI PCGQVMHYGQ LAAQLGRPGA
ARAVGAANGA NPISIVVPCH RVIGRNGTLT GYAGGVQRKE WLLRHEGYLL L
