OGT_SACS2
ID OGT_SACS2 Reviewed; 151 AA.
AC Q97VW7;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 107.
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};
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=SSO2487;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
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 -!- 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 -!- 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; AE006641; AAK42623.1; -; Genomic_DNA.
DR PIR; H90420; H90420.
DR RefSeq; WP_010923891.1; NC_002754.1.
DR PDB; 4ZYD; X-ray; 2.68 A; A=1-151.
DR PDB; 4ZYE; X-ray; 1.85 A; A=1-151.
DR PDB; 4ZYG; X-ray; 2.80 A; A/B=1-151.
DR PDB; 4ZYH; X-ray; 2.60 A; A=1-151.
DR PDB; 5LLQ; X-ray; 2.70 A; A/B=1-151.
DR PDB; 6GA0; X-ray; 2.00 A; A=1-151.
DR PDBsum; 4ZYD; -.
DR PDBsum; 4ZYE; -.
DR PDBsum; 4ZYG; -.
DR PDBsum; 4ZYH; -.
DR PDBsum; 5LLQ; -.
DR PDBsum; 6GA0; -.
DR AlphaFoldDB; Q97VW7; -.
DR SMR; Q97VW7; -.
DR STRING; 273057.SSO2487; -.
DR EnsemblBacteria; AAK42623; AAK42623; SSO2487.
DR GeneID; 7808242; -.
DR GeneID; 7940155; -.
DR GeneID; 8760125; -.
DR KEGG; sso:SSO2487; -.
DR PATRIC; fig|273057.12.peg.2568; -.
DR eggNOG; arCOG02724; Archaea.
DR HOGENOM; CLU_000445_52_2_2; -.
DR InParanoid; Q97VW7; -.
DR OMA; QANRANE; -.
DR PhylomeDB; Q97VW7; -.
DR BRENDA; 2.1.1.63; 6163.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IEA:UniProtKB-UniRule.
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; IPR036631; MGMT_N_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01035; DNA_binding_1; 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..151
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139387"
FT ACT_SITE 119
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:4ZYE"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:4ZYE"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:4ZYE"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:5LLQ"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:4ZYE"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:4ZYE"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:4ZYE"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:4ZYE"
FT HELIX 101..109
FT /evidence="ECO:0007829|PDB:4ZYE"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4ZYE"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:4ZYE"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:4ZYE"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:4ZYD"
FT HELIX 135..144
FT /evidence="ECO:0007829|PDB:4ZYE"
SQ SEQUENCE 151 AA; 17037 MW; 8457864CD5BC8F99 CRC64;
MLVYGLYKSP LGYITVAKDD KGFIMLDFCD CVEGNSRDDS SFTEFFHKLD LYFEGKPINL
REPINLKTYP FRLSVFKEVM KIPWGKVMTY KQIADSLGTS PRAVGMALSK NPILLIIPCH
RVIAENGIGG YSRGVKLKRA LLELEGVKIP E
