ID D2Q9M5_BIFDB Unreviewed; 169 AA. AC D2Q9M5; DT 02-MAR-2010, integrated into UniProtKB/TrEMBL. DT 02-MAR-2010, sequence version 1. DT 08-MAY-2019, entry version 58. DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772}; DE EC=2.1.1.63 {ECO:0000256|HAMAP-Rule:MF_00772}; DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772}; DE Short=MGMT {ECO:0000256|HAMAP-Rule:MF_00772}; DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000256|HAMAP-Rule:MF_00772}; GN Name=ogt {ECO:0000313|EMBL:ADB09511.1}; GN OrderedLocusNames=BDP_0854 {ECO:0000313|EMBL:ADB09511.1}; OS Bifidobacterium dentium (strain ATCC 27534 / DSM 20436 / JCM 1195 / OS Bd1). OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae; OC Bifidobacterium. OX NCBI_TaxID=401473 {ECO:0000313|EMBL:ADB09511.1, ECO:0000313|Proteomes:UP000008693}; RN [1] {ECO:0000313|EMBL:ADB09511.1, ECO:0000313|Proteomes:UP000008693} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27534 / DSM 20436 / JCM 1195 / Bd1 RC {ECO:0000313|Proteomes:UP000008693}; RX PubMed=20041198; DOI=10.1371/journal.pgen.1000785; RA Ventura M., Turroni F., Zomer A., Foroni E., Giubellini V., RA Bottacini F., Canchaya C., Claesson M.J., He F., Mantzourani M., RA Mulas L., Ferrarini A., Gao B., Delledonne M., Henrissat B., RA Coutinho P., Oggioni M., Gupta R.S., Zhang Z., Beighton D., RA Fitzgerald G.F., O'Toole P.W., van Sinderen D.; RT "The Bifidobacterium dentium Bd1 genome sequence reflects its genetic RT adaptation to the human oral cavity."; RL PLoS Genet. 5:E1000785-E1000785(2009). CC -!- FUNCTION: Involved in the cellular defense against the biological CC effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) CC in DNA. Repairs the methylated nucleobase in DNA by CC stoichiometrically transferring the methyl group to a cysteine CC residue in the enzyme. This is a suicide reaction: the enzyme is CC irreversibly inactivated. {ECO:0000256|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- CC COMP:10132, Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:82612, ChEBI:CHEBI:137386, CC ChEBI:CHEBI:137387; EC=2.1.1.63; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00772}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl- CC [protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl- CC [protein]; Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131, CC Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:11367, Rhea:RHEA- CC COMP:11368, ChEBI:CHEBI:29950, ChEBI:CHEBI:82612, CC ChEBI:CHEBI:85445, ChEBI:CHEBI:85448; EC=2.1.1.63; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00772}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00772}. CC -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and CC therefore is not strictly catalytic. According to one definition, CC an enzyme is a biocatalyst that acts repeatedly and over many CC reaction cycles. {ECO:0000256|HAMAP-Rule:MF_00772}. CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000256|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; CP001750; ADB09511.1; -; Genomic_DNA. DR RefSeq; WP_003840644.1; NC_013714.1. DR EnsemblBacteria; ADB09511; ADB09511; BDP_0854. DR GeneID; 31606065; -. DR KEGG; bde:BDP_0854; -. DR eggNOG; ENOG4105K85; Bacteria. DR eggNOG; COG0350; LUCA. DR HOGENOM; HOG000244137; -. DR KO; K00567; -. DR OMA; NPKSCRA; -. DR BioCyc; BDEN401473:G1GG5-847-MONOMER; -. DR Proteomes; UP000008693; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. 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 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 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008693}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00772}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00772}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_00772}; KW Hydrolase {ECO:0000313|EMBL:ADB09511.1}; KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772, KW ECO:0000313|EMBL:ADB09511.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008693}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00772, KW ECO:0000313|EMBL:ADB09511.1}. FT DOMAIN 78 164 DNA_binding_1. {ECO:0000259|Pfam: FT PF01035}. FT ACT_SITE 135 135 Nucleophile; methyl group acceptor. FT {ECO:0000256|HAMAP-Rule:MF_00772}. SQ SEQUENCE 169 AA; 18627 MW; F139322B50F493E7 CRC64; MDKFKTHYDS PIGGITMIAD GEALLGLWFD GHTEDADDDN AVWTDDLPIF GLAFRWLDEY FAGRKPKVHV PIRLEGTPFR EEIWALLREV PYGETVSYGE LAHRLESKHA DGRKVSARAV GGAVHHNPVG IIVPCHRVIG ADGSLTGYAG GLDVKARLLR LEGVLEKPD //