ID A0A7Y5ATZ1_9GAMM Unreviewed; 154 AA. AC A0A7Y5ATZ1; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 13-SEP-2023, entry version 8. 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 ORFNames=HRH59_18410 {ECO:0000313|EMBL:NRQ44517.1}; OS Rheinheimera lutimaris. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae; OC Rheinheimera. OX NCBI_TaxID=2740584 {ECO:0000313|EMBL:NRQ44517.1, ECO:0000313|Proteomes:UP000523161}; RN [1] {ECO:0000313|EMBL:NRQ44517.1, ECO:0000313|Proteomes:UP000523161} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=YQF-2 {ECO:0000313|EMBL:NRQ44517.1, RC ECO:0000313|Proteomes:UP000523161}; RA Yu Q., Qi Y., Pu J.; RT "Rheinheimera sp. nov., a marine bacterium isolated from coastal."; RL Submitted (JUN-2020) to the EMBL/GenBank/DDBJ databases. 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: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-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:0000256|ARBA:ARBA00001286, CC ECO:0000256|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:0000256|ARBA:ARBA00001596, ECO:0000256|HAMAP- CC Rule:MF_00772}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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 {ECO:0000256|HAMAP-Rule:MF_00772}. CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000256|HAMAP- CC Rule:MF_00772}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:NRQ44517.1}. 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; JABSOD010000032; NRQ44517.1; -; Genomic_DNA. DR AlphaFoldDB; A0A7Y5ATZ1; -. DR Proteomes; UP000523161; Unassembled WGS sequence. 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; 3.30.160.70; Methylated DNA-protein cysteine methyltransferase domain; 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; IPR036631; MGMT_N_sf. DR InterPro; IPR036388; WH-like_DNA-bd_sf. DR NCBIfam; TIGR00589; ogt; 1. DR PANTHER; PTHR10815; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1. DR PANTHER; PTHR10815:SF5; METHYLATED-DNA--PROTEIN-CYSTEINE METHYLTRANSFERASE; 1. DR Pfam; PF01035; DNA_binding_1; 1. DR SUPFAM; SSF53155; Methylated DNA-protein cysteine methyltransferase domain; 1. DR SUPFAM; SSF46767; Methylated DNA-protein cysteine methyltransferase, C-terminal domain; 1. DR PROSITE; PS00374; MGMT; 1. PE 3: Inferred from homology; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00772}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_00772}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00772}; KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603, ECO:0000256|HAMAP- KW Rule:MF_00772}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00772}. FT DOMAIN 69..147 FT /note="Methylated-DNA-[protein]-cysteine S- FT methyltransferase DNA binding" FT /evidence="ECO:0000259|Pfam:PF01035" FT ACT_SITE 119 FT /note="Nucleophile; methyl group acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00772" SQ SEQUENCE 154 AA; 16377 MW; 1D4B61974A708E9F CRC64; MFSQFIDSPL GPVQISATDH GISAISFVTT PRLAVPSALT ERAATQLLAY FAGTLTQFDL PLAAQGTTFQ HQVWRELCNV PFGTTCSYGD IARAISNIKA VRAVGAANGR NPVAIVVPCH RVIGANGTLT GYAGGLDKKA WLLKHEQRPQ ALLC //