ID H1Q1C7_9BACT Unreviewed; 166 AA.
AC H1Q1C7;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
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=HMPREF9140_00715 {ECO:0000313|EMBL:EHO72308.1};
OS Prevotella micans F0438.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=883158 {ECO:0000313|EMBL:EHO72308.1, ECO:0000313|Proteomes:UP000016023};
RN [1] {ECO:0000313|EMBL:EHO72308.1, ECO:0000313|Proteomes:UP000016023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0438 {ECO:0000313|EMBL:EHO72308.1,
RC ECO:0000313|Proteomes:UP000016023};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Baranova O.V.,
RA Blanton J.M., Wade W.G., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Heiman D., Howarth C., Larimer J., Lui A., MacDonald P.J.P.,
RA McCowen C., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Stolte C., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella micans F0438.";
RL Submitted (DEC-2011) 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 -!- 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:EHO72308.1}.
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DR EMBL; AGWK01000021; EHO72308.1; -; Genomic_DNA.
DR AlphaFoldDB; H1Q1C7; -.
DR STRING; 883158.HMPREF9140_00715; -.
DR PATRIC; fig|883158.3.peg.730; -.
DR eggNOG; COG0350; Bacteria.
DR HOGENOM; CLU_000445_52_2_10; -.
DR Proteomes; UP000016023; 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; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR InterPro; IPR008332; MethylG_MeTrfase_N.
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 Pfam; PF02870; Methyltransf_1N; 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:UP000016023};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00772}.
FT DOMAIN 4..80
FT /note="Methylguanine DNA methyltransferase ribonuclease-
FT like"
FT /evidence="ECO:0000259|Pfam:PF02870"
FT DOMAIN 86..165
FT /note="Methylated-DNA-[protein]-cysteine S-
FT methyltransferase DNA binding"
FT /evidence="ECO:0000259|Pfam:PF01035"
FT ACT_SITE 137
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00772"
SQ SEQUENCE 166 AA; 18574 MW; 8F73E3FBF9B88DE6 CRC64;
MIIHTEIYHS PCGDLLLGAC EEKLCLCDWT SEKHRPKTDC KLRKLLNAEF VDTPSEITRR
AAYELEEYFA GRRRTFNIPL LFAGTDFQKK VWSALLDVPF GETKSYAWLA KKIGNPKAVR
AVGLANGANN ISIFAPCHRI IGSNGSLVGY GGGLEIKRFL LNLENK
//
