OGT_THEGJ
ID OGT_THEGJ Reviewed; 174 AA.
AC C5A3L5;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=TGAM_0325;
OS Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=593117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15229 / JCM 11827 / EJ3;
RX PubMed=19558674; DOI=10.1186/gb-2009-10-6-r70;
RA Zivanovic Y., Armengaud J., Lagorce A., Leplat C., Guerin P., Dutertre M.,
RA Anthouard V., Forterre P., Wincker P., Confalonieri F.;
RT "Genome analysis and genome-wide proteomics of Thermococcus gammatolerans,
RT the most radioresistant organism known amongst the Archaea.";
RL Genome Biol. 10:R70.1-R70.23(2007).
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; CP001398; ACS32827.1; -; Genomic_DNA.
DR RefSeq; WP_015857945.1; NC_012804.1.
DR AlphaFoldDB; C5A3L5; -.
DR SMR; C5A3L5; -.
DR STRING; 593117.TGAM_0325; -.
DR PaxDb; C5A3L5; -.
DR EnsemblBacteria; ACS32827; ACS32827; TGAM_0325.
DR GeneID; 7987791; -.
DR KEGG; tga:TGAM_0325; -.
DR PATRIC; fig|593117.10.peg.322; -.
DR eggNOG; arCOG02724; Archaea.
DR HOGENOM; CLU_000445_52_2_2; -.
DR OMA; KRNPYPI; -.
DR OrthoDB; 122341at2157; -.
DR Proteomes; UP000001488; 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..174
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_1000212907"
FT ACT_SITE 141
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000250|UniProtKB:O74023"
SQ SEQUENCE 174 AA; 19818 MW; 10595E6FD7317439 CRC64;
MLAVERFGVN GRDIWIGVIF HGRIQGISFA FTRGELLERI RNLAEFLRGR DVRVSLDVQP
SNYTELVYRV LIGELENEKA LPELSFEGVT PFERRVYEWL TKNVKRGTVI TYGSLAKALE
TSPRAVGGAM KRNPYPIIVP CHRVVSREGI GHYNLGIEEK KFLLELEGVK EWTG
