OGT_PYRAE
ID OGT_PYRAE Reviewed; 148 AA.
AC O93728;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000250|UniProtKB:O74023};
DE EC=2.1.1.63 {ECO:0000250|UniProtKB:O74023};
DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000250|UniProtKB:O74023};
DE Short=MGMT {ECO:0000250|UniProtKB:O74023};
DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000250|UniProtKB:O74023};
GN Name=ogt; OrderedLocusNames=PAE2012;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RA Slupska M.M., Pedriquez L., Miller J.H.;
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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:0000250|UniProtKB:O74023}.
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:0000250|UniProtKB:O74023};
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:0000250|UniProtKB:O74023};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O74023}.
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 {ECO:0000250|UniProtKB:O74023}.
CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000250|UniProtKB:O74023}.
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DR EMBL; U82384; AAD09231.2; -; Genomic_DNA.
DR EMBL; AE009441; AAL63882.1; -; Genomic_DNA.
DR AlphaFoldDB; O93728; -.
DR SMR; O93728; -.
DR STRING; 178306.PAE2012; -.
DR PRIDE; O93728; -.
DR EnsemblBacteria; AAL63882; AAL63882; PAE2012.
DR KEGG; pai:PAE2012; -.
DR PATRIC; fig|178306.9.peg.1487; -.
DR eggNOG; arCOG02724; Archaea.
DR HOGENOM; CLU_1754770_0_0_2; -.
DR InParanoid; O93728; -.
DR OMA; VTTYKLY; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd06445; ATase; 1.
DR Gene3D; 1.10.10.10; -; 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; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01035; DNA_binding_1; 1.
DR SUPFAM; SSF46767; SSF46767; 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..148
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139382"
FT ACT_SITE 90
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000250|UniProtKB:O74023"
SQ SEQUENCE 148 AA; 16456 MW; 53E9E4348002E6BD CRC64;
MICSQYGPVV VGWDGSKTFV NPSRCSKRVG LAEFLELINI DEIDKRLLYL LGIPRGYVTT
YKLYAEVLGT SPRHVGWLMA RNPLPVILPC HRVVKSDFSL GGYTGGVEVK KKLLAYEGAL
CGDRPCRVVR PRMIDDVRDA LFKSLGLA
