MGMT_DEBHA
ID MGMT_DEBHA Reviewed; 191 AA.
AC Q6BVY4; B5RSW6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 2.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase;
DE EC=2.1.1.63;
DE AltName: Full=6-O-methylguanine-DNA methyltransferase;
DE Short=MGMT;
DE AltName: Full=DNA repair MTase;
DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase;
GN Name=MGT1; OrderedLocusNames=DEHA2B15752g;
OS Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX NCBI_TaxID=284592;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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:0000250}.
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 -!- 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;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAR65503.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CR382134; CAR65503.1; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_002770134.1; XM_002770088.1.
DR AlphaFoldDB; Q6BVY4; -.
DR SMR; Q6BVY4; -.
DR STRING; 4959.XP_002770134.1; -.
DR EnsemblFungi; CAR65503; CAR65503; DEHA2B15752g.
DR GeneID; 8998265; -.
DR KEGG; dha:DEHA2B15752g; -.
DR eggNOG; KOG4062; Eukaryota.
DR HOGENOM; CLU_000445_52_2_1; -.
DR InParanoid; Q6BVY4; -.
DR OrthoDB; 1573162at2759; -.
DR Proteomes; UP000000599; Chromosome B.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR CDD; cd06445; ATase; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd.
DR InterPro; IPR036217; MethylDNA_cys_MeTrfase_DNAb.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR Pfam; PF01035; DNA_binding_1; 1.
DR SUPFAM; SSF46767; SSF46767; 1.
DR TIGRFAMs; TIGR00589; ogt; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; DNA-binding; Methyltransferase; Nucleus;
KW Reference proteome; Transferase.
FT CHAIN 1..191
FT /note="Methylated-DNA--protein-cysteine methyltransferase"
FT /id="PRO_0000333684"
FT ACT_SITE 151
FT /note="Nucleophile; methyl group acceptor"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /evidence="ECO:0000250"
SQ SEQUENCE 191 AA; 21668 MW; 7D7E32CC743BBC53 CRC64;
MKNIYLLYSI IDVSYTKALI VTNTHGSLYY ASLGDKPEVL IVTMKKDFAR FKNYVLQPIV
GKANSEVSET LEKFRLMAED PRLINTMHKQ IPYEFIFGTE LQRKVWNQLM NTNASETVCY
SQMASNLGMP KSSRVVGAAC GANKIALFVP CHRALTKSGQ ISGYRWGVPL KQRLLKLEQK
PLQKESSLKE K
