ID S2ZU24_9ACTN Unreviewed; 163 AA.
AC S2ZU24;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=HMPREF1211_01788 {ECO:0000313|EMBL:EPD67529.1};
OS Streptomyces sp. HGB0020.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD67529.1, ECO:0000313|Proteomes:UP000014410};
RN [1] {ECO:0000313|EMBL:EPD67529.1, ECO:0000313|Proteomes:UP000014410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0020 {ECO:0000313|EMBL:EPD67529.1,
RC ECO:0000313|Proteomes:UP000014410};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptomyces sp. HGB0020.";
RL Submitted (APR-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|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:EPD67529.1}.
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DR EMBL; AGER01000004; EPD67529.1; -; Genomic_DNA.
DR AlphaFoldDB; S2ZU24; -.
DR STRING; 1078086.HMPREF1211_01788; -.
DR PATRIC; fig|1078086.3.peg.1819; -.
DR HOGENOM; CLU_000445_52_2_11; -.
DR Proteomes; UP000014410; 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; 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.
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}; Reference proteome {ECO:0000313|Proteomes:UP000014410};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00772}.
FT DOMAIN 8..74
FT /note="Methylguanine DNA methyltransferase ribonuclease-
FT like"
FT /evidence="ECO:0000259|Pfam:PF02870"
FT DOMAIN 79..158
FT /note="Methylated-DNA-[protein]-cysteine S-
FT methyltransferase DNA binding"
FT /evidence="ECO:0000259|Pfam:PF01035"
FT ACT_SITE 130
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00772"
SQ SEQUENCE 163 AA; 17919 MW; 74F99E99A5DA11A9 CRC64;
MSPVKQHTVI DSPYGPLTLV ADDGVLSGLY MTEQRHRPPQ ETFGEPDERP FAEAEEQLTA
YFEGELKEFT LELRLNGTPF QRTVWDQLRR IPYGETRSYG ELAAALGKPS ASRAVGLANG
RNPIGIIVPC HRVVGTNGNL TGYGGGLDRK QRLLDFEGGS ALF
//
