EzCatDB: D00517
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DB codeD00517
RLCP classification3.770.220000.47 : Transfer
CATH domainDomain 13.30.160.70 : Double Stranded RNA Binding Domain
Domain 21.10.10.10 : Arc Repressor Mutant, subunit ACatalytic domain
E.C.2.1.1.63

CATH domainRelated DB codes (homologues)
1.10.10.10 : Arc Repressor Mutant, subunit AD00510,D00452,D00077,T00055,T00113

Enzyme Name
UniProtKBKEGG

O74023Q58924Q973C7
Protein nameMethylated-DNA--protein-cysteine methyltransferaseMethylated-DNA--protein-cysteine methyltransferaseMethylated-DNA--protein-cysteine methyltransferasemethylated-DNA---[protein]-cysteine S-methyltransferase
SynonymsEC 2.1.1.63
6-O-methylguanine-DNA methyltransferase
MGMT
O-6-methylguanine-DNA-alkyltransferase
Pk-MGMT
EC 2.1.1.63
6-O-methylguanine-DNA methyltransferase
MGMT
O-6-methylguanine-DNA-alkyltransferase
EC 2.1.1.63
6-O-methylguanine-DNA methyltransferase
MGMT
O-6-methylguanine-DNA-alkyltransferase
RefSeqYP_184384.1 (Protein)
NC_006624.1 (DNA/RNA sequence)
NP_248537.1 (Protein)
NC_000909.1 (DNA/RNA sequence)
NP_376877.1 (Protein)
NC_003106.2 (DNA/RNA sequence)
PfamPF01035 (DNA_binding_1)
PF09153 (DUF1938)
[Graphical view]
PF01035 (DNA_binding_1)
[Graphical view]
PF01035 (DNA_binding_1)
[Graphical view]


UniProtKB:Accession NumberO74023Q58924Q973C7
Entry nameOGT_PYRKOOGT_METJAOGT_SULTO
ActivityDNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- cysteine.DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- cysteine.DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- cysteine.
Subunit


Subcellular locationCytoplasm.Cytoplasm (By similarity).Cytoplasm (By similarity).
Cofactor



Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC04250C02743C00039C03800
CompoundDNA (containing 6-O-methylguanine)Protein L-cysteineDNAProtein S-methyl-L-cysteine
Typeamine group,carbohydrate,nucleic acidspeptide/protein,sulfhydryl groupnucleic acidspeptide/protein,sulfide group
ChEBI



PubChem



            
1mgtA01UnboundUnboundUnboundUnbound
2g7hA01UnboundUnboundUnboundUnbound
1wrjA01UnboundUnboundUnboundUnbound
1mgtA02UnboundUnboundUnboundUnbound
2g7hA02UnboundUnboundUnboundUnbound
1wrjA02UnboundUnboundUnboundUnbound

Active-site residues
resource
see D00077
pdbCatalytic residues
         
1mgtA01 
2g7hA01 
1wrjA01 
1mgtA02TYR 112;ASN 133;CYS 141;HIS 142;GLU 167
2g7hA02TYR  99;ASN 120;CYS 128;HIS 129;GLU 154
1wrjA02TYR  91;ASN 112;CYS 120;HIS 121;GLU 146

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]p.713
[7]Fig.5, p.159-1607

references
[1]
PubMed ID1581542
JournalChem Res Toxicol
Year1992
Volume5
Pages8-9
AuthorsKohda K, Terashima I, Sawada N, Nozaki I, Yasuda M, Kawazoe Y
TitleSynthesis and O-demethylation rate of cis-[Pt(NH3)2(O6,9-dimethylguanine-7)2]Cl2
[2]
PubMed ID1554415
JournalMol Carcinog
Year1992
Volume5
Pages161-9
AuthorsSantibanez-Koref M, Elder RH, Fan CY, Cawkwell L, McKie JH, Douglas KT, Margison GP, Rafferty JA
TitleIsolation and partial characterization of murine O6-alkylguanine-DNA-alkyltransferase: comparative sequence and structural properties.
[3]
PubMed ID7727387
JournalBiochemistry
Year1994
Volume33
Pages11364-71
AuthorsSpratt TE, Campbell CR
TitleSynthesis of oligodeoxynucleotides containing analogs of O6-methylguanine and reaction with O6-alkylguanine-DNA alkyltransferase
[4]
CommentsX-ray crystallography
PubMed ID10497033
JournalJ Mol Biol
Year1999
Volume292
Pages707-16
AuthorsHashimoto H, Inoue T, Nishioka M, Fujiwara S, Takagi M, Imanaka T, Kai Y
TitleHyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase.
Related PDB1mgt
[5]
PubMed ID10749683
JournalBiochem J
Year2000
Volume347
Pages527-34
AuthorsXu-Welliver M, Kanugula S, Loktionova NA, Crone TM, Pegg AE
TitleConserved residue lysine165 is essential for the ability of O6-alkylguanine-DNA alkyltransferase to react with O6-benzylguanine.
[6]
PubMed ID10749682
JournalBiochem J
Year2000
Volume347
Pages519-26
AuthorsXu-Welliver M, Pegg AE
TitlePoint mutations at multiple sites including highly conserved amino acids maintain activity, but render O6-alkylguanine-DNA alkyltransferase insensitive to O6-benzylguanine.
[7]
PubMed ID10946226
JournalMutat Res
Year2000
Volume460
Pages151-63
AuthorsDaniels DS, Tainer JA
TitleConserved structural motifs governing the stoichiometric repair of alkylated DNA by O(6)-alkylguanine-DNA alkyltransferase.
[8]
PubMed ID11488906
JournalEur J Biochem
Year2001
Volume268
Pages4144-50
AuthorsShiraki K, Nishikori S, Fujiwara S, Hashimoto H, Kai Y, Takagi M, Imanaka T
TitleComparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterpart.
[9]
PubMed ID11398466
JournalMethods Enzymol
Year2001
Volume334
Pages239-48
AuthorsTakagi M, Kai Y, Imanaka T
TitleMethylguanine methyltransferase from Thermococcus kodakaraensis KOD1
[10]
PubMed ID12093287
JournalBiochemistry
Year2002
Volume41
Pages8689-97
AuthorsLuu KX, Kanugula S, Pegg AE, Pauly GT, Moschel RC
TitleRepair of oligodeoxyribonucleotides by O(6)-alkylguanine-DNA alkyltransferase
[11]
PubMed ID16826543
JournalMagn Reson Chem
Year2006
Volume44 Spec No
PagesS71-82
AuthorsRoberts A, Pelton JG, Wemmer DE
TitleStructural studies of MJ1529, an O6-methylguanine-DNA methyltransferase.
Related PDB2g7h

comments
The catalytic domain of this enzyme (from Archaea) is homologous to that of its homologue from human (D00077 in EzCatDB). Moreover, since the catalytic residues are conserved in this enzyme, the catalytic mechanism must be the same as that of its homologoue, as well.

createdupdated
2003-04-252009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
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Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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