OGT_PYRSN
ID OGT_PYRSN Reviewed; 173 AA.
AC F4HK38;
DT 16-MAY-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 47.
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=PNA2_0433;
OS Pyrococcus sp. (strain NA2).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus; unclassified Pyrococcus.
OX NCBI_TaxID=342949;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA2;
RX PubMed=21602357; DOI=10.1128/jb.05150-11;
RA Lee H.S., Bae S.S., Kim M.S., Kwon K.K., Kang S.G., Lee J.H.;
RT "Complete genome sequence of hyperthermophilic Pyrococcus sp. strain NA2,
RT isolated from a deep-sea hydrothermal vent area.";
RL J. Bacteriol. 193:3666-3667(2011).
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}.
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; CP002670; AEC51350.1; -; Genomic_DNA.
DR RefSeq; WP_013747906.1; NC_015474.1.
DR AlphaFoldDB; F4HK38; -.
DR SMR; F4HK38; -.
DR STRING; 342949.PNA2_0433; -.
DR EnsemblBacteria; AEC51350; AEC51350; PNA2_0433.
DR GeneID; 10553898; -.
DR KEGG; pyn:PNA2_0433; -.
DR PATRIC; fig|342949.8.peg.430; -.
DR eggNOG; arCOG02724; Archaea.
DR HOGENOM; CLU_000445_52_2_2; -.
DR OMA; KRNPYPI; -.
DR OrthoDB; 122341at2157; -.
DR Proteomes; UP000008293; 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..173
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000417356"
FT ACT_SITE 143
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000250|UniProtKB:O74023"
SQ SEQUENCE 173 AA; 19862 MW; B00C2FB510CA69D3 CRC64;
MISYGRFNIL GRELTIAIVW NNKGIQGITY SLDGIEFLEE QISRIINHLK SRNVRVNLSQ
EESEYPELVF MVLTGYVSNE EAFKELSLEG LTEFEIKVYS WLVKNVKRGE VITYGKVAKA
LKTSPLAIGG AMRRNPYPII VPCHRVIGKR NKFLYTPKPS YKKFLLEVEG WTS
