OGT_THEKO
ID OGT_THEKO Reviewed; 174 AA.
AC O74023;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 128.
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, ECO:0000269|PubMed:9613574};
DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE Short=MGMT {ECO:0000255|HAMAP-Rule:MF_00772, ECO:0000303|PubMed:9613574};
DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE AltName: Full=Pk-MGMT {ECO:0000303|PubMed:10497033};
GN Name=ogt {ECO:0000255|HAMAP-Rule:MF_00772};
GN Synonyms=mgtk {ECO:0000303|PubMed:9613574}; OrderedLocusNames=TK1971;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=9613574; DOI=10.1007/s004380050708;
RA Mendez-Leclere M., Nishioka M., Yuasa T., Fujiwara S., Takagi M.,
RA Imanaka T.;
RT "The O6-methylguanine-DNA methyltransferase from the hyperthermophilic
RT archaeon Pyrococcus sp. KOD1: a thermostable repair enzyme.";
RL Mol. Gen. Genet. 258:69-77(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND ACTIVE SITE.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=10497033; DOI=10.1006/jmbi.1999.3100;
RA Hashimoto H., Inoue T., Nishioka M., Fujiwara S., Takagi M., Imanaka T.,
RA Kai Y.;
RT "Hyperthermostable protein structure maintained by intra and inter-helix
RT ion-pairs in archaeal O6-methylguanine-DNA methyltransferase.";
RL J. Mol. Biol. 292:707-716(1999).
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, ECO:0000269|PubMed:9613574}.
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 ECO:0000269|PubMed:9613574};
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 ECO:0000269|PubMed:9613574};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Activity is stable at 90 degrees Celsius for at least 30 minutes.
CC {ECO:0000269|PubMed:9613574};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772,
CC ECO:0000269|PubMed:9613574}.
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:0000305}.
CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000255|HAMAP-
CC Rule:MF_00772, ECO:0000305}.
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DR EMBL; D86335; BAA29044.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD86160.1; -; Genomic_DNA.
DR PIR; T44680; T44680.
DR RefSeq; WP_011250921.1; NC_006624.1.
DR PDB; 1MGT; X-ray; 1.80 A; A=1-174.
DR PDBsum; 1MGT; -.
DR AlphaFoldDB; O74023; -.
DR SMR; O74023; -.
DR STRING; 69014.TK1971; -.
DR EnsemblBacteria; BAD86160; BAD86160; TK1971.
DR GeneID; 3234736; -.
DR KEGG; tko:TK1971; -.
DR PATRIC; fig|69014.16.peg.1925; -.
DR eggNOG; arCOG02724; Archaea.
DR HOGENOM; CLU_000445_52_2_2; -.
DR InParanoid; O74023; -.
DR OMA; KRNPYPI; -.
DR OrthoDB; 122341at2157; -.
DR PhylomeDB; O74023; -.
DR EvolutionaryTrace; O74023; -.
DR Proteomes; UP000000536; 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:0006307; P:DNA dealkylation involved in DNA repair; IEA:UniProtKB-UniRule.
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 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; IPR023546; MGMT.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; DNA damage; DNA repair; Methyltransferase;
KW Reference proteome; Transferase.
FT CHAIN 1..174
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139385"
FT ACT_SITE 141
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00772,
FT ECO:0000305|PubMed:10497033"
FT STRAND 2..9
FT /evidence="ECO:0007829|PDB:1MGT"
FT STRAND 12..32
FT /evidence="ECO:0007829|PDB:1MGT"
FT HELIX 33..49
FT /evidence="ECO:0007829|PDB:1MGT"
FT HELIX 63..71
FT /evidence="ECO:0007829|PDB:1MGT"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:1MGT"
FT HELIX 91..103
FT /evidence="ECO:0007829|PDB:1MGT"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:1MGT"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:1MGT"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:1MGT"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:1MGT"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:1MGT"
FT HELIX 157..166
FT /evidence="ECO:0007829|PDB:1MGT"
SQ SEQUENCE 174 AA; 19517 MW; 1AD95478CE2EF72F CRC64;
MLSVEKFRVG ERVVWIGVIF SGRVQGIAFA FDRGTLMKRI HDLAEHLGKR GVSISLDVQP
SDYPEKVFKV LIGELDNASF LRELSFEGVT PFEKKVYEWL TKNVKRGSVI TYGDLAKALN
TSPRAVGGAM KRNPYPIVVP CHRVVAHDGI GYYSSGIEEK KFLLEIEGVK EWTS
