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Information on EC 2.1.1.63 - methylated-DNA-[protein]-cysteine S-methyltransferase and Organism(s) Archaeoglobus fulgidus and UniProt Accession O27970

for references in articles please use BRENDA:EC2.1.1.63
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EC Tree
IUBMB Comments
This protein is involved in the repair of methylated DNA. Unlike EC 3.2.2.20, DNA-3-methyladenine glycosidase I and EC 3.2.2.21, DNA-3-methyladenine glycosidase II, which remove the methylated base leaving an apurinic/apyrimidinic site, this enzyme transfers the methyl group from the methylated DNA to an internal cysteine residue, leaving an intact nucleotide. Since the methyl transfer is irreversible, the enzyme can only catalyse a single turnover.
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This record set is specific for:
Archaeoglobus fulgidus
UNIPROT: O27970
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Word Map
The taxonomic range for the selected organisms is: Archaeoglobus fulgidus
The enzyme appears in selected viruses and cellular organisms
Synonyms
o6-methylguanine-dna methyltransferase, atase, o6-alkylguanine-dna alkyltransferase, ada protein, o6-methylguanine dna methyltransferase, o6-methylguanine-dna-methyltransferase, o6-methylguanine methyltransferase, o6-alkylguanine dna alkyltransferase, o6-mgmt, methylguanine dna methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
O6-alkylguanine-DNA alkyltransferase
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Ada protein
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-
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MGMT
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-
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O6-methylguanine-DNA methyltransferase
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O6-MGMT
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methyl group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
DNA-6-O-methylguanine/DNA-4-O-methylthymine:[protein]-L-cysteine S-methyltransferase
This protein is involved in the repair of methylated DNA. Unlike EC 3.2.2.20, DNA-3-methyladenine glycosidase I and EC 3.2.2.21, DNA-3-methyladenine glycosidase II, which remove the methylated base leaving an apurinic/apyrimidinic site, this enzyme transfers the methyl group from the methylated DNA to an internal cysteine residue, leaving an intact nucleotide. Since the methyl transfer is irreversible, the enzyme can only catalyse a single turnover.
CAS REGISTRY NUMBER
COMMENTARY hide
77271-19-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
DNA containing 6-O-methylguanine + [protein]-L-cysteine
DNA lacking 6-O-methylguanine + [protein]-S-methyl-L-cysteine
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DNA containing 6-O-methylguanine + [protein]-L-cysteine
DNA lacking 6-O-methylguanine + [protein]-S-methyl-L-cysteine
show the reaction diagram
DNA-repair protein that protects cells from killing and mutagenesis by alkylating agents
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
O6-benzylguanine
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80 - 100
80°C: optimum, 100°C: substantial repair activity at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16718
x * 16718, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 16718, calculation from nucleotide sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
half-life: 24 h
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, stored at, storage at -20°C or at -80°C results in protein precipitation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed at high levels in Escherichia coli fused to an N-terminal polyhistidine tag that allows a single-step isolation and purification by metal-affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed at high levels in Escherichia coli fused to an N-terminal polyhistidine tag that allows a single-step isolation and purification by metal-affinity chromatography
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kanugula, S.; Pegg, A.E.
Alkylation damage repair protein O6-alkylguanine-DNA alkyltransferase from the hyperthermophiles Aquifex aeolicus and Archaeoglobus fulgidus
Biochem. J.
375
449-455
2003
Archaeoglobus fulgidus (O27970), Archaeoglobus fulgidus, Aquifex aeolicus (O67467), Aquifex aeolicus
Manually annotated by BRENDA team