(data stored in ACNUC7421 zone)
SWISSPROT: Q47T13_THEFY
ID Q47T13_THEFY Unreviewed; 231 AA.
AC Q47T13;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 08-MAY-2019, entry version 91.
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 OrderedLocusNames=Tfu_0366 {ECO:0000313|EMBL:AAZ54404.1};
OS Thermobifida fusca (strain YX).
OC Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC Thermobifida.
OX NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54404.1, ECO:0000313|Proteomes:UP000000434};
RN [1] {ECO:0000313|Proteomes:UP000000434}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX PubMed=17209016; DOI=10.1128/JB.01899-06;
RA Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA Richardson P., Wilson D.B., Kyrpides N.;
RT "Genome sequence and analysis of the soil cellulolytic actinomycete
RT Thermobifida fusca YX.";
RL J. Bacteriol. 189:2477-2486(2007).
CC -!- FUNCTION: Involved in the cellular defense against the biological
CC effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT)
CC in DNA. Repairs the methylated nucleobase in DNA by
CC stoichiometrically transferring the methyl group to a cysteine
CC residue in the enzyme. This is a suicide reaction: the enzyme is
CC irreversibly inactivated. {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-
CC COMP:10132, Rhea:RHEA-COMP:13555, Rhea:RHEA-COMP:13556,
CC ChEBI:CHEBI:29950, ChEBI:CHEBI:82612, ChEBI:CHEBI:137386,
CC ChEBI:CHEBI:137387; EC=2.1.1.63; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00772};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-
CC [protein] = a 2'-deoxyguanosine in DNA + S-methyl-L-cysteinyl-
CC [protein]; Xref=Rhea:RHEA:24000, Rhea:RHEA-COMP:10131,
CC Rhea:RHEA-COMP:10132, Rhea:RHEA-COMP:11367, Rhea:RHEA-
CC COMP:11368, ChEBI:CHEBI:29950, ChEBI:CHEBI:82612,
CC 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
CC therefore is not strictly catalytic. According to one definition,
CC an enzyme is a biocatalyst that acts repeatedly and over many
CC reaction cycles. {ECO:0000256|HAMAP-Rule:MF_00772}.
CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000256|HAMAP-
CC Rule:MF_00772}.
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DR EMBL; CP000088; AAZ54404.1; -; Genomic_DNA.
DR RefSeq; WP_011290813.1; NC_007333.1.
DR STRING; 269800.Tfu_0366; -.
DR EnsemblBacteria; AAZ54404; AAZ54404; Tfu_0366.
DR KEGG; tfu:Tfu_0366; -.
DR eggNOG; ENOG4105K85; Bacteria.
DR eggNOG; COG0350; LUCA.
DR HOGENOM; HOG000244137; -.
DR KO; K00567; -.
DR OMA; NPKSCRA; -.
DR OrthoDB; 1327994at2; -.
DR BioCyc; TFUS269800:G1G4Q-368-MONOMER; -.
DR Proteomes; UP000000434; 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 CDD; cd06445; ATase; 1.
DR Gene3D; 1.10.10.10; -; 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 Pfam; PF01035; DNA_binding_1; 1.
DR Pfam; PF02870; Methyltransf_1N; 1.
DR SUPFAM; SSF46767; SSF46767; 1.
DR SUPFAM; SSF53155; SSF53155; 1.
DR TIGRFAMs; TIGR00589; ogt; 1.
DR PROSITE; PS00374; MGMT; 1.
PE 3: Inferred from homology;
DR PRODOM; Q47T13.
DR SWISS-2DPAGE; Q47T13.
KW Complete proteome {ECO:0000313|Proteomes:UP000000434};
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 ECO:0000313|EMBL:AAZ54404.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00772,
KW ECO:0000313|EMBL:AAZ54404.1}.
FT DOMAIN 48 115 Methyltransf_1N. {ECO:0000259|Pfam:
FT PF02870}.
FT DOMAIN 119 198 DNA_binding_1. {ECO:0000259|Pfam:
FT PF01035}.
FT ACT_SITE 170 170 Nucleophile; methyl group acceptor.
FT {ECO:0000256|HAMAP-Rule:MF_00772}.
SQ SEQUENCE 231 AA; 24633 MW; F972C1CA6120C305 CRC64;
MRCRAENSLS PPLPHRRTPD TGTSTPAPRT HQGVIVTAEI PARARVHTVV DSPLGPLTLV
AADGALVGLY QEDQRHRPAP DSFGVPDPAP FTEVIAQLTE YFSGQRTVFD LPLAFTGTPF
QTTVWRALLE IPYGQTVSYG ELAARIGKPS ASRAVGLANG RNPISIIVPC HRVVGSSGSL
TGYGGGLARK QWLLALEQRR AHQPPLLDFA DGLDAGEPRS ATLPMGSHHS A
//
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