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Information on EC 2.1.1.113 - site-specific DNA-methyltransferase (cytosine-N4-specific)
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EC Tree
2.1.1.113 site-specific DNA-methyltransferase (cytosine-N4-specific)Specify your search results
Word Map
- 2.1.1.113
- endonuclease
-
restriction-modification
- mtases
- sphaericus
- deoxycytidylate
-
n6-adenine
- n6-methyladenine
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
modification methylase, m.pvuii, m.ngomxv, m.bcnia, m.pspgi, sll0729, m.bcnib, m2.mboii, n4-cytosine methyltransferase, m.smai, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
cytosine-N5-methyltransferase
-
-
-
-
DNA-(N4-cytosine)-methyltransferase
DNA[cytosine-N4]methyltransferase
-
-
-
-
DraR1
HP_1368
M.BsoBI
M.CbeI
M.CsyAIP
M.CsyBIP
M.MthZI
M.NgoMXV
M.Pac25I
M.PhoIIIP
M.PspGI
M.PvuII
M.StyCIP
m4C-forming Mtase
-
-
-
-
m4C-MTase
modification methylase
N4-cytosine methyltransferase
N4mC MTase
ORF16000P
restriction-modification system
-
-
-
-
SuaI
additional information
-
this is a large group of enzymes most of which, with enzymes of similar specificity listed as EC 3.1.21.3, 4 or 5, form so-called "restriction-modification systems". A complete listing of all these enzymes has been produced by R.J. Roberts, this list is updated annually
DNA-(N4-cytosine)-methyltransferase
-
-
-
-
modification methylase
-
-
-
-
N4mC MTase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N4-methylcytosine
S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N4-methylcytosine
the product inhibition pattern consistent with a steady-state random bi-bi mechanism in which the dominant order of substrate binding and product release: S-adenosyl-L-methionine, methylated DNA, DNAMe, S-adenosyl-L-homocysteine
-
S-adenosyl-L-methionine + DNA cytosine = S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
methyl group transfer
-
-
-
-
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CAS REGISTRY NUMBER
COMMENTARY
169592-50-1
-
90371-46-3
-
92228-39-2
-
98982-80-0
-
99637-25-9
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5
?
-
-
-
-
?
S-adenosyl-L-methionine + 5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'
?
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
20-mer oligodeoxynucleotide duplex containing the palindromic recognition site GGATCC. The enzyme catalyzes methyl group transfer to the internal cytosine residue in the palindromic recognition site GGATCC. The enzyme transfers the methyl group to the exocyclic NH2-group without formation of a transient covalent bond
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'. The target base is the internal cytosine in the recognition sequence
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
20-mer duplex 5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5' containing a palindromic recognition site GGATCC
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
M.BcnIA and M.BcnIB act on 5'-CC(C/G)GG-3' sites in double-stranded DNA. M.BcnIA can also, with a comparable efficiency, modify the specific targets in single-stranded DNA
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
substrate is pNH20 plasmid DNA. M2.MboII modifies the internal cytosine in the recognition sequence 39-CTTCT-59, yielding N4-methylcytosine, and moreover is able to methylate double- and single-stranded DNA, single-stranded DNA is preferred. Determination and analysis of the methylation pattern of M2.MboII, overview
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
substrate is pNH20 plasmid DNA. M2.NcuI modifies the internal cytosine in the recognition sequence yielding N4-methylcytosine, and moreover is able to methylate double- and single-stranded DNA, single-stranded DNA is preferred. Determination of the methylation position, overview
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the enzyme generates N4-methylcytosine in duplex 5'-CAGCTG-3' DNA. PvuII methyltransferase is catalytically competent with one and with two bound molecules of S-adenosyl-L-methionine
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the enzyme catalyzes the transfer of the methyl group from S-adenosyl-L-methionine to the exocyclic aminoN4 nitrogen of the central cytosine in its recognition sequence 5'-CAGCTG-3'
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the enzyme modifies the second cytosine in CAGCTG sequences, also methylates adenine residues in CAGATG/CAGCTG substrates in which the target cytosine is replaced by adenine in one strand of the recognition sequence
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
substrate is methylated plasmid DNA. M.PspGI is a type IIP methyltransferase and enhances fluorescence of 2-aminopurine in DNA if it replaces the second C in the sequence
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage. SuaI is the only restriction-modification system detected in SUlfolobus acidocaldarius and the N4 methylation of the inner C in the recognition site is necessary and sufficient to protect against it
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage. SuaI is the only restriction-modification system detected in SUlfolobus acidocaldarius and the N4 methylation of the inner C in the recognition site is necessary and sufficient to protect against it
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
methylation of second cytosine of 5'-CCCGGG-3' recognition sequence
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
target sequences
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
target sequences
-
?
additional information
?
-
-
integrity of ATCC sequence is critical
-
-
?
additional information
?
-
-
the enzyme also displays promiscuous activity catalyzing methylation of adenine at the N6 position in DNA
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
additional information
?
-
-
the enzyme also displays promiscuous activity catalyzing methylation of adenine at the N6 position in DNA
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + DNA cytosine
S-adenosyl-L-homocysteine + DNA N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
-
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage. SuaI is the only restriction-modification system detected in SUlfolobus acidocaldarius and the N4 methylation of the inner C in the recognition site is necessary and sufficient to protect against it
-
-
?
S-adenosyl-L-methionine + [DNA]-cytosine
S-adenosyl-L-homocysteine + [DNA]-N4-methylcytosine
-
the SuaI restriction-modification system uses N4 methylation of the inner C of the recognition sequence GGCC in genomic DNA of Sulfolobus acidocaldarius to protect the recognition sequence from cleavage. SuaI is the only restriction-modification system detected in SUlfolobus acidocaldarius and the N4 methylation of the inner C in the recognition site is necessary and sufficient to protect against it
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzyme's catalytic activity is strongly stimulated by addition of Ca2+ or Mg2+, but not by Mn2+, Co2+ or Cd2+, however, divalent metal ions are not required for its base-flipping activity
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-homocysteine
-
competitive with regard to S-adenosylmethionine and non-competitive with respect to unmethylated 20-mer duplex
additional information
-
no apparent substrate inhibition at concentrations 100fold higher than the Km for DNA and 20fold higher than Km for S-adenosyl-L-methionine
-
additional information
-
no substrate inhibition even at concentrations many times higher than the Km-values
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme's catalytic activity is strongly stimulated by addition of Ca2+ or Mg2+, but not by Mn2+, Co2+ or Cd2+
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00035
5'-CAGTTTAGGATCCATTTCAC-3'/3'-GTCAAATCCTAGGTAAAAGAG-5'
-
-
-
0.000196
5'-GTGAAAT*GGATCC*TAAACTG-3'/3'-CACTTTA*CCTAGG*ATTTGAC-5'
-
-
-
additional information
additional information
-
Km-values for several oligonucleotides
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Kcat-values for several oligonucleotides
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3200
additional information
genetic organization of novel restriction-modification (R-M) system, tail-to-tail gene orientation with 12 base pairs overlapping, protection and activity assays, classified as member of beta-class of m4C-methyltransferases, predicted amino acid sequence reveals 41.9% identity with SmaI, no SmaI-like restriction activity in cell extracts of the Xcv7-1 strain
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
pv. vesicatoria, strains Xcv7-1, Xv2 and Xv64 and ATCC 35937 strain
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
metabolism
-
the enzyme is part of the MboII restriction-modification, R-M, system of Moraxella bovis strain ATCC 10900 consisting of a restriction endonuclease gene and two methyltransferase genes
metabolism
-
the enzyme is part of the Ncul restriction-modification, R-M, system consisting of a restriction endonuclease gene and two methyltransferase genes
metabolism
cytosine N4-methylation is required for DNA transformation
metabolism
-
cytosine N4-methylation is required for DNA transformation
-
physiological function
enzyme recognizes the 5'TCTTC3'x02 sequence and methylates the first cytosine residue. A deletion strain displays lower adherence to host gastric adenocarcinoma cells and reduced potential to induce inflammation and apoptosis. The deletion strain exhibits reduced capacity for natural transformation, and a total of 102 genes belonging to virulence, ribosome assembly and cellular components are differentially expressed
physiological function
-
enzyme recognizes the motif CCGCGG and methylates the second cytosine residue to give C4mCGCGG. N4-cytosine is the major methylated form in Deinococcus radiodurans. Cells deficient in 4mC modification display higher spontaneous rifampin mutation frequency and enhanced DNA recombination and transformation efficiency. Genes involved in the maintenance of genomic stability are differentially expressed in DraR1 mutant strains
physiological function
mutation of gene sll0729 leads to lowered chlorophyll/phycocyanin ratio and slower growth. Prolonged cultivation reveals instability of the initially obtained phenotype and appearance of suppressor mutants. The suppressor strains show smaller cell size, lowered DNA content per cell, and decreased tolerance against UV compared to wild type. Suppressor cells show decreased levels of DNA topoisomerase 4 subunit A
physiological function
-
enzyme recognizes the motif CCGCGG and methylates the second cytosine residue to give C4mCGCGG. N4-cytosine is the major methylated form in Deinococcus radiodurans. Cells deficient in 4mC modification display higher spontaneous rifampin mutation frequency and enhanced DNA recombination and transformation efficiency. Genes involved in the maintenance of genomic stability are differentially expressed in DraR1 mutant strains
-
physiological function
-
enzyme recognizes the 5'TCTTC3'x02 sequence and methylates the first cytosine residue. A deletion strain displays lower adherence to host gastric adenocarcinoma cells and reduced potential to induce inflammation and apoptosis. The deletion strain exhibits reduced capacity for natural transformation, and a total of 102 genes belonging to virulence, ribosome assembly and cellular components are differentially expressed
-
Show AA Sequence and Transmembrane Helices (9014 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18300
truncated protein predicted due to translation termination codon in the open reading frame
30000
32111
-
1 * 30000, about, recombinant enzyme, SDS-PAGE, 1 * 32111, sequence calculation
32676
-
1 * 30000, about, recombinant enzyme, 1 * 32676, sequence calculation
50000
-
x * 50355, sequence calculation, x * 50000, recombinant enzyme, SDS-PAGE
50355
-
x * 50355, sequence calculation, x * 50000, recombinant enzyme, SDS-PAGE
30000
-
1 * 30000, about, recombinant enzyme, 1 * 32676, sequence calculation
30000
-
1 * 30000, about, recombinant enzyme, SDS-PAGE, 1 * 32111, sequence calculation
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
additional information
-
enzyme in a free state exists as a dimer. Introduction of substoichiometric amounts of DNA into the reaction mixture results in pronounced multimerization of the enzyme. However, addition of SAM in saturating concentration at an excess of the oligonucleotide duplex over BamHI Mtase converts most of the enzyme into a monomeric state
?
-
x * 50355, sequence calculation, x * 50000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 30000, about, recombinant enzyme, SDS-PAGE, 1 * 32111, sequence calculation
monomer
-
1 * 30000, about, recombinant enzyme, 1 * 32676, sequence calculation
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
determination of the structure of PvuII methyltransferase complexed with S-adenosyl-L-methionine by multiwavelength anomalous diffraction using a crystal of the selenomethionine substituted protein
-
native and selenomethionyl M.PvuII crystallized separately as binary complexs of the methyl donor S-adenosyl-L-methionine in the monoclinic space group P2. Hanging-drop vapor-diffusion technique
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gel filtration, recombinant protein for in vitro methyltransferase activity assay
purified from E. coli cells expressing the genes for M.BcnIA and M.BcnIB
-
recombinant M2.MboII 3.6fold to electrophoretic homogeneity using a four-step chromatographic procedure, involving adsorption and hydroxylapatite chromatography followed by hydroophobic interaction and heparin affinity chromatography, from Escherichia coli
-
recombinant M2.NcuI 3.6fold to electrophoretic homogeneity using a four-step chromatographic procedure, involving adsorption and hydroxylapatite chromatography followed by hydrophobic interaction and heparin affinity chromatography, from Escherichia coli
-
recombinant wild-type enzyme from Escherichia coli by adsorption chromatography and dialysis to homogeneity
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
expressed in Escherichia coli ER2796 cells
gene mboIIR, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli using the constitutive promoter, PtetA
-
gene ncuIM2, DNA and amino acid sequence determination and analysis, expression in Escherichia coli
-
obtained from genomic library, amplified in Escherichia coli XL1-Blue, strain ER2566 for expression of the M.XveII carrying a C-terminal His6-tag
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Klimasauskas, S.; Timinskas, A.; Menkevicius, S.; Butkiene, D.; Butkus, V.; Janulaitis, A.
Sequence motifs characteristic of DNA[cytosine-N4]methyltransferases: similarity to adenine and cytosine-C5 DNA-methylases
Nucleic Acids Res.
17
9823-9832
1989
Citrobacter freundii, Kocuria varians, Citrobacter freundii RFL9, Kocuria varians RFL19
brenda
Roberts, R.J.; Macelis, D.
Restriction enzymes and their isoschizomers
Nucleic Acids Res.
20
2167-2180
1992
Bacteria
brenda
Malygin, E.G.; Zinoviev, V.V.; Evdokimov, A.A.; Lindstrom, W.M., Jr.; Reich, N.O.; Hattman, S.
DNA-(cytosine-N4)- and (adenine-N6)-methyltransferases have different kinetic mechanisms but the same reaction route: a comparison of M.BamHI and T4 Dam
J. Biol. Chem.
20
1-31
2003
Bacillus amyloliquefaciens
-
brenda
O'Gara, M.; Adams, G.M.; Gong, W.; Kobayashi, R.; Blumenthal, R.M.; Cheng, X.
Expression, purification, mass spectrometry, crystallization and multiwavelength anomalous diffraction of selenomethionyl PvuII DNA methyltransferase (cytosine-N4-specific)
Eur. J. Biochem.
247
1009-1018
1997
Proteus vulgaris
brenda
Zinoviev, V.V.; Evdokimov, A.A.; Malygin, E.G.
DNA-(N4-Cytosine)-methyltransferase from Bacillus amyloliquefaciens: mechanism of action derived from steady-state kinetics
Mol. Biol. (Mosk.)
37
116-124
2003
Bacillus amyloliquefaciens
-
brenda
Lindstrom, W.M., Jr.; Malygin, E.G.; Ovechkina, L.G.; Zinoviev, V.V.; Reich, N.O.
Functional analysis of BamHI DNA cytosine-N4 methyltransferase
J. Mol. Biol.
325
711-720
2003
Bacillus amyloliquefaciens
brenda
Adams, G.M.; Blumenthal, R.M.
The PvuII DNA (cytosine-N4)-methyltransferase comprises two trypsin-defined domains, each of which binds a molecule of S-adenosyl-L-methionine
Biochemistry
36
8284-8292
1997
Proteus vulgaris
brenda
Bujnicki, J.M.; Radlinska, M.
Molecular evolution of DNA-(cytosine-N4) methyltransferases: evidence for their polyphyletic origin
Nucleic Acids Res.
27
4501-4509
1999
Cenarchaeum symbiosum, Cenarchaeum symbiosum (O74074), Helicobacter pylori, Helicobacter pylori (Q9ZLF1), Lactobacillus phage phig1e, Methanocaldococcus jannaschii, Pseudomonas alcaligenes, Pyrococcus horikoshii, Salmonella enterica subsp. enterica serovar Typhi, Xanthomonas citri pv. malvacearum, Streptomyces fimbriatus (O52513), Streptomyces caespitosus (O52692), Saccharopolyspora sp. (O52711), Methanothermobacter wolfeii (O59647), Bacillus subtilis (O68556), Bacillus subtilis (Q45489), Gordonia rubripertincta (O85488), Pyrococcus sp. (O93645), Trichormus variabilis (P0A462), Proteus hauseri (P11409), Serratia marcescens (P14230), Citrobacter freundii (P14243), Citrobacter freundii (Q04845), Kocuria varians (P14244), Bacillus amyloliquefaciens (P18051), Bacillus amyloliquefaciens (P23941), Methanothermobacter thermautotrophicus (P29568), Xanthomonas campestris pv. cyanopsidis (P30774), Geobacillus stearothermophilus (P70986), Curtobacterium albidum (P71101), Halobacterium phage phiH (Q38204), Neisseria gonorrhoeae (Q9AKV2), Methanothermobacter thermautotrophicus Z-250 (P29568), Neisseria gonorrhoeae ME11 (Q9AKV2), Citrobacter freundii RFL9 (P14243), Bacillus amyloliquefaciens H (P23941), Citrobacter freundii 4111 (Q04845), Geobacillus stearothermophilus JN2091 (P70986), Kocuria varians RFL19 (P14244), Cenarchaeum symbiosum B (O74074), Cenarchaeum symbiosum A, Pseudomonas alcaligenes NCIB 986, Salmonella enterica subsp. enterica serovar Typhi CT18, Pyrococcus horikoshii OT-3
brenda
Gong, W.; O'Gara, M.; Blumenthal, R.M.; Cheng, X.
Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment
Nucleic Acids Res.
25
2702-2715
1997
Proteus vulgaris
brenda
Merkiene, E.; Vilkaitis, G.; Klimasauskas, S.
A pair of single-strand and double-strand DNA cytosine-N4 methyltransferases from Bacillus centrosporus
Biol. Chem.
379
569-571
1998
Brevibacillus centrosporus
brenda
Jeltsch, A.
The cytosine N4-methyltransferase M.PvuII also modifies adenine residues
Biol. Chem.
382
707-710
2001
Proteus vulgaris
brenda
Malygin, E.G.; Ovechkina, L.G.; Zinoviev, V.V.; Lindstrem, U.M.; Reich, N.O.
DNA-(N4-cytosine)-methyltransferase from Bacillus amyloliquefaciens: kinetic and substrate-binding properties
Mol. Biol. (Mosk.)
35
35-44
2001
Bacillus amyloliquefaciens
-
brenda
Zinoviev, V.V.; Yakishchik, S.I.; Evdokimov, A.A.; Malygin, E.G.; Hattman, S.
Symmetry elements in DNA structure important for recognition/methylation by DNA [amino]-methyltransferases
Nucleic Acids Res.
32
3930-3934
2004
Bacillus amyloliquefaciens
brenda
Yu, Y.J.; Yang, M.T.
A novel restriction-modification system from Xanthomonas campestris pv. vesicatoria encodes a m4C-methyltransferase and a nonfunctional restriction endonuclease
FEMS Microbiol. Lett.
272
83-90
2007
Xanthomonas campestris (Q3BWM2)
brenda
Carpenter, M.A.; Bhagwat, A.S.
DNA base flipping by both members of the PspGI restriction-modification system
Nucleic Acids Res.
36
5417-5425
2008
Pyrococcus sp. GI-H
brenda
Furmanek-Blaszk, B.; Boratynski, R.; Zolcinska, N.; Sektas, M.
M1.Mboll and M2.Mboll type IIS methyltransferases: different specificities, the same target
Microbiology
155
1111-1121
2009
Moraxella bovis, Moraxella cuniculi
brenda
Aranda, J.; Roca, M.; Lopez-Canut, V.; Tunon, I.
Theoretical study of the catalytic mechanism of DNA-(N4-cytosine)-methyltransferase from the bacterium Proteus vulgaris
J. Phys. Chem. B
114
8467-8473
2010
Proteus vulgaris
brenda
Clark, T.A.; Murray, I.A.; Morgan, R.D.; Kislyuk, A.O.; Spittle, K.E.; Boitano, M.; Fomenkov, A.; Roberts, R.J.; Korlach, J.
Characterization of DNA methyltransferase specificities using single-molecule, real-time DNA sequencing
Nucleic Acids Res.
40
e29
2012
Acetobacter aceti, Geobacillus stearothermophilus, uncultured bacterium, Cereibacter sphaeroides
brenda
Grogan, D.W.
Cytosine methylation by the SuaI restriction-modification system: implications for genetic fidelity in a hyperthermophilic archaeon
J. Bacteriol.
185
4657-4661
2003
Sulfolobus acidocaldarius, Sulfolobus acidocaldarius DG185
brenda
Aranda, J.; Roca, M.; Tunon, I.
Substrate promiscuity in DNA methyltransferase M.PvuII. A mechanistic insight
Org. Biomol. Chem.
10
5395-5400
2012
Proteus vulgaris
brenda
Furuta, Y.; Namba-Fukuyo, H.; Shibata, T.F.; Nishiyama, T.; Shigenobu, S.; Suzuki, Y.; Sugano, S.; Hasebe, M.; Kobayashi, I.
Methylome diversification through changes in DNA methyltransferase sequence specificity
PLoS Genet.
10
e1004272
2014
Helicobacter pylori
brenda
Chung, D.; Farkas, J.; Huddleston, J.R.; Olivar, E.; Westpheling, J.
Methylation by a unique alpha-class N4-cytosine methyltransferase is required for DNA transformation of Caldicellulosiruptor bescii DSM6725
PLoS ONE
7
e43844
2012
Caldicellulosiruptor bescii (B9MK94), Caldicellulosiruptor bescii, Caldicellulosiruptor bescii DSM 6725 (B9MK94)
brenda
Gaertner, K.; Klaehn, S.; Watanabe, S.; Mikkat, S.; Scholz, I.; Hess, W.R.; Hagemann, M.
Cytosine N4-methylation via M.Ssp6803II is involved in the regulation of transcription, fine-tuning of DNA replication and DNA repair in the cyanobacterium Synechocystis sp. PCC 6803
Front. Microbiol.
10
1233
2019
Synechocystis sp. PCC 6803 (P74637)
brenda
Li, S.; Cai, J.; Lu, H.; Mao, S.; Dai, S.; Hu, J.; Wang, L.; Hua, X.; Xu, H.; Tian, B.; Zhao, Y.; Hua, Y.
N4-Cytosine DNA methylation is involved in the maintenance of genomic stability in Deinococcus radiodurans
Front. Microbiol.
10
1905
2019
Deinococcus radiodurans, Deinococcus radiodurans R1
brenda
Kumar, S.; Karmakar, B.C.; Nagarajan, D.; Mukhopadhyay, A.K.; Morgan, R.D.; Rao, D.N.
N4-cytosine DNA methylation regulates transcription and pathogenesis in Helicobacter pylori
Nucleic Acids Res.
46
3429-3445
2018
Helicobacter pylori (O25921), Helicobacter pylori 26695 (O25921)
brenda
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