ID   OGT_PYRAB               Reviewed;         172 AA.
AC   Q9V1N7; G8ZI25;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 108.
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 {ECO:0000250|UniProtKB:O74023}; OrderedLocusNames=PYRAB03900;
GN   ORFNames=PAB0260;
OS   Pyrococcus abyssi (strain GE5 / Orsay).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=272844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GE5 / Orsay;
RX   PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA   Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA   Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA   Weissenbach J., Zivanovic Y., Forterre P.;
RT   "An integrated analysis of the genome of the hyperthermophilic archaeon
RT   Pyrococcus abyssi.";
RL   Mol. Microbiol. 47:1495-1512(2003).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=GE5 / Orsay;
RX   PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA   Gao J., Wang J.;
RT   "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT   Pyrococcus furiosus DSM 3638.";
RL   Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49312.1; -; Genomic_DNA.
DR   EMBL; HE613800; CCE69768.1; -; Genomic_DNA.
DR   PIR; A75154; A75154.
DR   RefSeq; WP_010867512.1; NC_000868.1.
DR   AlphaFoldDB; Q9V1N7; -.
DR   SMR; Q9V1N7; -.
DR   STRING; 272844.PAB0260; -.
DR   EnsemblBacteria; CAB49312; CAB49312; PAB0260.
DR   GeneID; 1495281; -.
DR   KEGG; pab:PAB0260; -.
DR   PATRIC; fig|272844.11.peg.411; -.
DR   eggNOG; arCOG02724; Archaea.
DR   HOGENOM; CLU_000445_52_2_2; -.
DR   OMA; KRNPYPI; -.
DR   OrthoDB; 122341at2157; -.
DR   PhylomeDB; Q9V1N7; -.
DR   Proteomes; UP000000810; Chromosome.
DR   Proteomes; UP000009139; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; IPR015236; MGMT_N.
DR   InterPro; IPR036631; MGMT_N_sf.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF01035; DNA_binding_1; 1.
DR   Pfam; PF09153; DUF1938; 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..172
FT                   /note="Methylated-DNA--protein-cysteine methyltransferase"
FT                   /id="PRO_0000139381"
FT   ACT_SITE        142
FT                   /note="Nucleophile; methyl group acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O74023"
SQ   SEQUENCE   172 AA;  19713 MW;  BEE0E6A7B436384E CRC64;
     MLSCESFKIK GREIIICVIW EEGIQGIVYS LDGREFLEKQ LSRLISMLNK RGVSLSLKER
     HSKYPELVFN VLTGKISNEE GFEELSLEGL TDFEIRVYSW LVKNVKRGEV ITYGKVAKEL
     KTSALAIGGA MKRNPYPIVV PCHRVVGKKD PWLYTPKPEY KKFLLEVEGW TS