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OGT_HAEIN
ID   OGT_HAEIN               Reviewed;         179 AA.
AC   P44687;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 2.
DT   25-MAY-2022, entry version 126.
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}; Synonyms=dat1;
GN   OrderedLocusNames=HI_0402;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAC22061.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L42023; AAC22061.1; ALT_INIT; Genomic_DNA.
DR   PIR; G64065; G64065.
DR   RefSeq; NP_438564.1; NC_000907.1.
DR   RefSeq; WP_032828387.1; NC_000907.1.
DR   AlphaFoldDB; P44687; -.
DR   SMR; P44687; -.
DR   STRING; 71421.HI_0402; -.
DR   EnsemblBacteria; AAC22061; AAC22061; HI_0402.
DR   KEGG; hin:HI_0402; -.
DR   PATRIC; fig|71421.8.peg.421; -.
DR   eggNOG; COG0350; Bacteria.
DR   HOGENOM; CLU_000445_52_2_6; -.
DR   PhylomeDB; P44687; -.
DR   Proteomes; UP000000579; 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..179
FT                   /note="Methylated-DNA--protein-cysteine methyltransferase"
FT                   /id="PRO_0000139366"
FT   ACT_SITE        130
FT                   /note="Nucleophile; methyl group acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
SQ   SEQUENCE   179 AA;  20455 MW;  9A83D5AFFC91D896 CRC64;
     MTALYYTYYP SPVGRLLILS DGESITHIDF EKEQYAPNPK WHKQDELPVF QKVRLAFERY
     FNGEVECFSN IPLKPEGTAF QQAIWQALRE IDYGELSTYG ELALRINNPK AVRAVGGAVG
     SNPISIIIPC HRILGKDRTL TGFGGGLEAK RFLLQLEKIP YIDKGTENTK PRFFKKYHE
 
 
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