DB code: D00517

RLCP classification 3.770.220000.47 : Transfer
CATH domain 3.30.160.70 : Double Stranded RNA Binding Domain
1.10.10.10 : Arc Repressor Mutant, subunit A Catalytic domain
E.C. 2.1.1.63
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
1.10.10.10 : Arc Repressor Mutant, subunit A D00510 D00452 D00077 T00055 T00113

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
O74023 Methylated-DNA--protein-cysteine methyltransferase
EC 2.1.1.63
6-O-methylguanine-DNA methyltransferase
MGMT
O-6-methylguanine-DNA-alkyltransferase
Pk-MGMT
YP_184384.1 (Protein)
NC_006624.1 (DNA/RNA sequence)
PF01035 (DNA_binding_1)
PF09153 (DUF1938)
[Graphical View]
Q58924 Methylated-DNA--protein-cysteine methyltransferase
EC 2.1.1.63
6-O-methylguanine-DNA methyltransferase
MGMT
O-6-methylguanine-DNA-alkyltransferase
NP_248537.1 (Protein)
NC_000909.1 (DNA/RNA sequence)
PF01035 (DNA_binding_1)
[Graphical View]
Q973C7 Methylated-DNA--protein-cysteine methyltransferase
EC 2.1.1.63
6-O-methylguanine-DNA methyltransferase
MGMT
O-6-methylguanine-DNA-alkyltransferase
NP_376877.1 (Protein)
NC_003106.2 (DNA/RNA sequence)
PF01035 (DNA_binding_1)
[Graphical View]

KEGG enzyme name
methylated-DNA---[protein]-cysteine S-methyltransferase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O74023 OGT_PYRKO DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- cysteine. Cytoplasm.
Q58924 OGT_METJA DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- cysteine. Cytoplasm (By similarity).
Q973C7 OGT_SULTO DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- cysteine. Cytoplasm (By similarity).

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C04250 C02743 C00039 C03800
E.C.
Compound DNA (containing 6-O-methylguanine) Protein L-cysteine DNA Protein S-methyl-L-cysteine
Type amine group,carbohydrate,nucleic acids peptide/protein,sulfhydryl group nucleic acids peptide/protein,sulfide group
ChEBI
PubChem
1mgtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2g7hA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1wrjA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1mgtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
2g7hA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound
1wrjA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
see D00077

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1mgtA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
2g7hA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1wrjA01 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain
1mgtA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 112;ASN 133;CYS 141;HIS 142;GLU 167
2g7hA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 99;ASN 120;CYS 128;HIS 129;GLU 154
1wrjA02 Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain TYR 91;ASN 112;CYS 120;HIS 121;GLU 146

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[4]
p.713
[7]
Fig.5, p.159-160 7

References
[1]
Resource
Comments
Medline ID
PubMed ID 1581542
Journal Chem Res Toxicol
Year 1992
Volume 5
Pages 8-9
Authors Kohda K, Terashima I, Sawada N, Nozaki I, Yasuda M, Kawazoe Y
Title Synthesis and O-demethylation rate of cis-[Pt(NH3)2(O6,9-dimethylguanine-7)2]Cl2
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 1554415
Journal Mol Carcinog
Year 1992
Volume 5
Pages 161-9
Authors Santibanez-Koref M, Elder RH, Fan CY, Cawkwell L, McKie JH, Douglas KT, Margison GP, Rafferty JA
Title Isolation and partial characterization of murine O6-alkylguanine-DNA-alkyltransferase: comparative sequence and structural properties.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 7727387
Journal Biochemistry
Year 1994
Volume 33
Pages 11364-71
Authors Spratt TE, Campbell CR
Title Synthesis of oligodeoxynucleotides containing analogs of O6-methylguanine and reaction with O6-alkylguanine-DNA alkyltransferase
Related PDB
Related UniProtKB
[4]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10497033
Journal J Mol Biol
Year 1999
Volume 292
Pages 707-16
Authors Hashimoto H, Inoue T, Nishioka M, Fujiwara S, Takagi M, Imanaka T, Kai Y
Title Hyperthermostable protein structure maintained by intra and inter-helix ion-pairs in archaeal O6-methylguanine-DNA methyltransferase.
Related PDB 1mgt
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10749683
Journal Biochem J
Year 2000
Volume 347
Pages 527-34
Authors Xu-Welliver M, Kanugula S, Loktionova NA, Crone TM, Pegg AE
Title Conserved residue lysine165 is essential for the ability of O6-alkylguanine-DNA alkyltransferase to react with O6-benzylguanine.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 10749682
Journal Biochem J
Year 2000
Volume 347
Pages 519-26
Authors Xu-Welliver M, Pegg AE
Title Point mutations at multiple sites including highly conserved amino acids maintain activity, but render O6-alkylguanine-DNA alkyltransferase insensitive to O6-benzylguanine.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 10946226
Journal Mutat Res
Year 2000
Volume 460
Pages 151-63
Authors Daniels DS, Tainer JA
Title Conserved structural motifs governing the stoichiometric repair of alkylated DNA by O(6)-alkylguanine-DNA alkyltransferase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11488906
Journal Eur J Biochem
Year 2001
Volume 268
Pages 4144-50
Authors Shiraki K, Nishikori S, Fujiwara S, Hashimoto H, Kai Y, Takagi M, Imanaka T
Title Comparative analyses of the conformational stability of a hyperthermophilic protein and its mesophilic counterpart.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11398466
Journal Methods Enzymol
Year 2001
Volume 334
Pages 239-48
Authors Takagi M, Kai Y, Imanaka T
Title Methylguanine methyltransferase from Thermococcus kodakaraensis KOD1
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12093287
Journal Biochemistry
Year 2002
Volume 41
Pages 8689-97
Authors Luu KX, Kanugula S, Pegg AE, Pauly GT, Moschel RC
Title Repair of oligodeoxyribonucleotides by O(6)-alkylguanine-DNA alkyltransferase
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 16826543
Journal Magn Reson Chem
Year 2006
Volume 44 Spec No
Pages S71-82
Authors Roberts A, Pelton JG, Wemmer DE
Title Structural studies of MJ1529, an O6-methylguanine-DNA methyltransferase.
Related PDB 2g7h
Related UniProtKB

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.

Created Updated
2003-04-25 2009-02-26