(data stored in SCRATCH zone)

SWISSPROT: B2TEJ3_PARPJ

ID   B2TEJ3_PARPJ            Unreviewed;       210 AA.
AC   B2TEJ3;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 69.
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=Bphyt_4130 {ECO:0000313|EMBL:ACD18514.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18514.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD18514.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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; CP001053; ACD18514.1; -; Genomic_DNA.
DR   RefSeq; WP_012426030.1; NC_010676.1.
DR   STRING; 398527.Bphyt_4130; -.
DR   EnsemblBacteria; ACD18514; ACD18514; Bphyt_4130.
DR   KEGG; bpy:Bphyt_4130; -.
DR   eggNOG; ENOG4105K85; Bacteria.
DR   eggNOG; COG0350; LUCA.
DR   HOGENOM; HOG000244137; -.
DR   KO; K00567; -.
DR   OMA; NPKSCRA; -.
DR   OrthoDB; 1327994at2; -.
DR   BioCyc; BPHY398527:GJEX-4128-MONOMER; -.
DR   Proteomes; UP000001739; Chromosome 2.
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; 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.
PE   3: Inferred from homology;
DR   PRODOM; B2TEJ3.
DR   SWISS-2DPAGE; B2TEJ3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001739};
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:ACD18514.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00772,
KW   ECO:0000313|EMBL:ACD18514.1}.
FT   DOMAIN        3     74       Methyltransf_1N. {ECO:0000259|Pfam:
FT                                PF02870}.
FT   DOMAIN       79    157       DNA_binding_1. {ECO:0000259|Pfam:
FT                                PF01035}.
FT   ACT_SITE    130    130       Nucleophile; methyl group acceptor.
FT                                {ECO:0000256|HAMAP-Rule:MF_00772}.
SQ   SEQUENCE   210 AA;  22828 MW;  63AC15FA5B4A277B CRC64;
     MTYAYKLMDS PVGQLKLVAN GERLAAILWE HDKPNRVRLG ELIEANDRPV LIETERQLNE
     YFAGTRHEFD LPLTFQGTDF QKQVWAALLT IPFGQTRSYS EIATQIGNVN AVRAVGAANG
     KNPISIVAPC HRVIGASGDL TGFAGGLANK MLLLSLEAGQ TSFEAEADGQ TDMFALEQRA
     TVKTQVKSEA QTKPARHAPS RGTQASLFGN
//

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