OGT_SULTO
ID OGT_SULTO Reviewed; 156 AA.
AC Q973C7; F9VNS2;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=STK_09670;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS).
RA Kuroda M., Tsunoda M., Nakamura K.T.;
RT "Crystal structure of O6-methylguanine methyltransferase from Sulfolobus
RT tokodaii.";
RL Submitted (OCT-2004) to the PDB data bank.
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}.
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; BA000023; BAK54430.1; -; Genomic_DNA.
DR RefSeq; WP_010978968.1; NC_003106.2.
DR PDB; 1WRJ; X-ray; 2.00 A; A=1-156.
DR PDB; 7CSM; X-ray; 1.25 A; A=1-156.
DR PDB; 7D4V; X-ray; 1.78 A; A=1-156.
DR PDB; 7DKN; X-ray; 1.79 A; A=1-156.
DR PDB; 7DQQ; X-ray; 2.60 A; A=1-156.
DR PDB; 7DQR; X-ray; 1.74 A; A=1-156.
DR PDB; 7DQT; X-ray; 1.13 A; A=1-156.
DR PDB; 7E1P; X-ray; 1.63 A; A=1-156.
DR PDBsum; 1WRJ; -.
DR PDBsum; 7CSM; -.
DR PDBsum; 7D4V; -.
DR PDBsum; 7DKN; -.
DR PDBsum; 7DQQ; -.
DR PDBsum; 7DQR; -.
DR PDBsum; 7DQT; -.
DR PDBsum; 7E1P; -.
DR AlphaFoldDB; Q973C7; -.
DR SMR; Q973C7; -.
DR STRING; 273063.STK_09670; -.
DR PRIDE; Q973C7; -.
DR EnsemblBacteria; BAK54430; BAK54430; STK_09670.
DR GeneID; 1458939; -.
DR KEGG; sto:STK_09670; -.
DR PATRIC; fig|273063.9.peg.1082; -.
DR eggNOG; arCOG02724; Archaea.
DR OMA; QANRANE; -.
DR OrthoDB; 122341at2157; -.
DR EvolutionaryTrace; Q973C7; -.
DR Proteomes; UP000001015; 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..156
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000139388"
FT ACT_SITE 120
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00772"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7DQT"
FT STRAND 12..18
FT /evidence="ECO:0007829|PDB:7DQT"
FT STRAND 20..29
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 43..53
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:7DQT"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:7DQT"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:7DQT"
FT HELIX 150..154
FT /evidence="ECO:0007829|PDB:7DQT"
SQ SEQUENCE 156 AA; 17950 MW; 07239C0E302A25AD CRC64;
MIVYGLYKSP FGPITVAKNE KGFVMLDFCD CAERSSLDND YFTDFFYKLD LYFEGKKVDL
TEPVDFKPFN EFRIRVFKEV MRIKWGEVRT YKQVADAVKT SPRAVGTALS KNNVLLIIPC
HRVIGEKSLG GYSRGVELKR KLLELEGIDV AKFIEK
