ID A0A076HSV7_9BACT Unreviewed; 164 AA.
AC A0A076HSV7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=N008_09515 {ECO:0000313|EMBL:AII52213.1};
OS Hymenobacter sp. APR13.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1356852 {ECO:0000313|EMBL:AII52213.1, ECO:0000313|Proteomes:UP000028590};
RN [1] {ECO:0000313|EMBL:AII52213.1, ECO:0000313|Proteomes:UP000028590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APR13 {ECO:0000313|EMBL:AII52213.1,
RC ECO:0000313|Proteomes:UP000028590};
RA Li P., Jiang J., Kwok A.H.Y., Lou X., Xu D., Leung F.C.C.;
RT "Complete genome sequence assembly of Hymenobacter sp. APR13.";
RL Submitted (JUL-2013) 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|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|HAMAP-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 ---------------------------------------------------------------------------
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; CP006587; AII52213.1; -; Genomic_DNA.
DR RefSeq; WP_044015516.1; NZ_CP006587.1.
DR AlphaFoldDB; A0A076HSV7; -.
DR STRING; 1356852.N008_09515; -.
DR KEGG; hym:N008_09515; -.
DR eggNOG; COG0350; Bacteria.
DR HOGENOM; CLU_000445_52_2_10; -.
DR OrthoDB; 9802228at2; -.
DR Proteomes; UP000028590; 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; 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; 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:SF13; 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.
PE 3: Inferred from homology;
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 Methyltransferase {ECO:0000256|HAMAP-Rule:MF_00772};
KW Reference proteome {ECO:0000313|Proteomes:UP000028590};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00772}.
FT DOMAIN 77..156
FT /note="Methylated-DNA-[protein]-cysteine S-
FT methyltransferase DNA binding"
FT /evidence="ECO:0000259|Pfam:PF01035"
FT ACT_SITE 128
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00772"
SQ SEQUENCE 164 AA; 17753 MW; BC2E24937775F674 CRC64;
MNDTQAYLST PLGCLRLQGS DAGLAVVEFL EADAAPAPTP PAAVATPLRE AHRQLQAYFG
RELRDFQLTY DVQQGTDFQR RVWAALPAVS YGRTASYLDL ARQLGNPGAV RAVGAANGQN
PLGLVWPCHR IIGAGGQLTG YAGGLWRKKW LLDFEQPTVQ TALF
//