ID OGT_METJA Reviewed; 167 AA.
AC Q58924;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 130.
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:16826543};
DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
DE Short=MGMT {ECO:0000255|HAMAP-Rule:MF_00772};
DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000255|HAMAP-Rule:MF_00772};
GN Name=ogt {ECO:0000255|HAMAP-Rule:MF_00772}; OrderedLocusNames=MJ1529;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP STRUCTURE BY NMR, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16826543; DOI=10.1002/mrc.1823;
RA Roberts A., Pelton J.G., Wemmer D.E.;
RT "Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase.";
RL Magn. Reson. Chem. 44:S71-S82(2006).
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}.
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:16826543};
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:16826543};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}.
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 -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000255|HAMAP-
CC Rule:MF_00772}.
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DR EMBL; L77117; AAB99547.1; -; Genomic_DNA.
DR PIR; H64490; H64490.
DR RefSeq; WP_010871053.1; NC_000909.1.
DR PDB; 2G7H; NMR; -; A=1-167.
DR PDBsum; 2G7H; -.
DR AlphaFoldDB; Q58924; -.
DR BMRB; Q58924; -.
DR SMR; Q58924; -.
DR STRING; 243232.MJ_1529; -.
DR PaxDb; 243232-MJ_1529; -.
DR EnsemblBacteria; AAB99547; AAB99547; MJ_1529.
DR GeneID; 1452437; -.
DR KEGG; mja:MJ_1529; -.
DR eggNOG; arCOG02724; Archaea.
DR HOGENOM; CLU_000445_52_2_2; -.
DR InParanoid; Q58924; -.
DR OrthoDB; 372118at2157; -.
DR PhylomeDB; Q58924; -.
DR EvolutionaryTrace; Q58924; -.
DR Proteomes; UP000000805; 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; 3.30.160.460; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00589; ogt; 1.
DR PANTHER; PTHR46460; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR PANTHER; PTHR46460:SF1; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1.
DR Pfam; PF01035; DNA_binding_1; 1.
DR SUPFAM; SSF46767; Methylated DNA-protein cysteine methyltransferase, C-terminal domain; 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..167
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139377"
FT ACT_SITE 128
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:2G7H"
FT STRAND 8..23
FT /evidence="ECO:0007829|PDB:2G7H"
FT HELIX 31..34
FT /evidence="ECO:0007829|PDB:2G7H"
FT TURN 44..47
FT /evidence="ECO:0007829|PDB:2G7H"
FT HELIX 48..58
FT /evidence="ECO:0007829|PDB:2G7H"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:2G7H"
FT HELIX 82..88
FT /evidence="ECO:0007829|PDB:2G7H"
FT HELIX 99..105
FT /evidence="ECO:0007829|PDB:2G7H"
FT HELIX 110..118
FT /evidence="ECO:0007829|PDB:2G7H"
FT TURN 123..125
FT /evidence="ECO:0007829|PDB:2G7H"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:2G7H"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:2G7H"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2G7H"
FT HELIX 145..155
FT /evidence="ECO:0007829|PDB:2G7H"
SQ SEQUENCE 167 AA; 19431 MW; 7FC44483D31F6EF2 CRC64;
MIIQIEEYFI GMIFKGNQLV RNTIPLRREE IFNFMDGEVV SNPEDEHLKV AEIILKLYFA
EIDDKKVREL ISYKLEVPEF TKKVLDIVKD IEFGKTLTYG DIAKKLNTSP RAVGMALKRN
PLPLIIPCHR VVAKNSLGGY SYGLDKKKFI LERERLNMVS FKFNKVY
//
