BRENDA - Enzyme Database
show all sequences of 3.1.3.23

Characterization and regulation of a bacterial sugar phosphatase of the haloalkanoate dehalogenase superfamily, AraL, from Bacillus subtilis

Godinho, L.M.; de Sa-Nogueira, I.; FEBS J. 278, 2511-2524 (2011)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
araL gene, the fourth cistron of the transcriptional unit araABDLMNPQ-abfA, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli
Bacillus subtilis
Engineering
Amino acid exchange
Commentary
Organism
G12D
strain IQB849 carrying a single-base substitution C to A introduced in the hairpin region displaying an augment in araL'-'lacZ expression of about 30fold in the presence of inducer, the point mutation increases the free energy of the mRNA secondary structure
Bacillus subtilis
additional information
a translational fusion of the 5'-end of the araL gene to the lacZ reporter gene from Escherichia coli is constructed and integrated into the Bacillus subtilis chromosome. The construct comprises the araL ribosome-binding site, the initiation codon and a fusion between codon 10 of araL and codon 7 of Escherichia coli lacZ
Bacillus subtilis
T9K/G12D
the double point mutation, C to A and G to T, introduced a compensatory T in the other part of the stem, thus regenerating the stem-loop structure in strain IQB857 and drastically reducing the expression of araL'-'lacZ
Bacillus subtilis
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
24.96
-
D-glucose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
27.36
-
D-arabinose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
29.14
-
D-xylulose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
34.89
-
D-fructose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
40.74
-
D-galactose 1-phosphate
pH 7.0, 37C
Bacillus subtilis
40.78
-
D-fructose 1,6-bisphosphate
pH 7.0, 37C
Bacillus subtilis
50
-
4-nitrophenyl phosphate
pH 7.0, 37C
Bacillus subtilis
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Mg2+
absolutely required for catalysis, optimal at 15 mM
Bacillus subtilis
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28900
-
x * 28900, about, sequence calculation
Bacillus subtilis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bacillus subtilis
AraL shows low specificity and catalytic activity towards several sugar phosphates, which are metabolic intermediates of the glycolytic and pentose phosphate pathways, substrate specificity, overview
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
araL gene
-
Purification (Commentary)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 95% homogeneity
Bacillus subtilis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-nitrophenyl phosphate + H2O
AraL is a phosphatase displaying activity towards the synthetic substrate 4-nitrophenyl phosphate, although there is no evidence that pNPPase activity is physiologically relevant
714982
Bacillus subtilis
4-nitrophenol + phosphate
-
-
-
?
D-arabinose 5-phosphate + H2O
-
714982
Bacillus subtilis
D-arabinose + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
-
714982
Bacillus subtilis
?
-
-
-
?
D-fructose 6-phosphate + H2O
-
714982
Bacillus subtilis
D-fructose + phosphate
-
-
-
?
D-galactose 1-phosphate + H2O
-
714982
Bacillus subtilis
D-galactose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
-
714982
Bacillus subtilis
D-glucose + phosphate
-
-
-
?
D-xylulose 5-phosphate + H2O
-
714982
Bacillus subtilis
D-xylulose + phosphate
-
-
-
?
additional information
AraL shows low specificity and catalytic activity towards several sugar phosphates, which are metabolic intermediates of the glycolytic and pentose phosphate pathways, substrate specificity, overview
714982
Bacillus subtilis
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
?
x * 28900, about, sequence calculation
Bacillus subtilis
Temperature Optimum [C]
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
65
-
recombinant enzyme
Bacillus subtilis
Temperature Range [C]
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
25
70
optimal activity at 37C, no activity at 25C, profile, overview
Bacillus subtilis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.012
-
4-nitrophenyl phosphate
pH 7.0, 37C
Bacillus subtilis
1.49
-
D-fructose 1,6-bisphosphate
pH 7.0, 37C
Bacillus subtilis
2.49
-
D-glucose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
2.75
-
D-xylulose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
2.817
-
D-fructose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
2.92
-
D-arabinose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
4.28
-
D-galactose 1-phosphate
pH 7.0, 37C
Bacillus subtilis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
recombinant enzyme
Bacillus subtilis
pH Range
pH Minimum
pH Maximum
Commentary
Organism
4
9
although, at pH 8 and pH 9, the enzyme activity is considerably lower than at pH 7.0, the values are higher than at pH 6.0, no activity below pH 4.0, profile, overview
Bacillus subtilis
Cloned(Commentary) (protein specific)
Commentary
Organism
araL gene, the fourth cistron of the transcriptional unit araABDLMNPQ-abfA, DNA and amino acid sequence determination and analysis, overexpression of the His-tagged enzyme in Escherichia coli
Bacillus subtilis
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
G12D
strain IQB849 carrying a single-base substitution C to A introduced in the hairpin region displaying an augment in araL'-'lacZ expression of about 30fold in the presence of inducer, the point mutation increases the free energy of the mRNA secondary structure
Bacillus subtilis
additional information
a translational fusion of the 5'-end of the araL gene to the lacZ reporter gene from Escherichia coli is constructed and integrated into the Bacillus subtilis chromosome. The construct comprises the araL ribosome-binding site, the initiation codon and a fusion between codon 10 of araL and codon 7 of Escherichia coli lacZ
Bacillus subtilis
T9K/G12D
the double point mutation, C to A and G to T, introduced a compensatory T in the other part of the stem, thus regenerating the stem-loop structure in strain IQB857 and drastically reducing the expression of araL'-'lacZ
Bacillus subtilis
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
24.96
-
D-glucose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
27.36
-
D-arabinose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
29.14
-
D-xylulose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
34.89
-
D-fructose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
40.74
-
D-galactose 1-phosphate
pH 7.0, 37C
Bacillus subtilis
40.78
-
D-fructose 1,6-bisphosphate
pH 7.0, 37C
Bacillus subtilis
50
-
4-nitrophenyl phosphate
pH 7.0, 37C
Bacillus subtilis
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Mg2+
absolutely required for catalysis, optimal at 15 mM
Bacillus subtilis
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
28900
-
x * 28900, about, sequence calculation
Bacillus subtilis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
additional information
Bacillus subtilis
AraL shows low specificity and catalytic activity towards several sugar phosphates, which are metabolic intermediates of the glycolytic and pentose phosphate pathways, substrate specificity, overview
?
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to over 95% homogeneity
Bacillus subtilis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-nitrophenyl phosphate + H2O
AraL is a phosphatase displaying activity towards the synthetic substrate 4-nitrophenyl phosphate, although there is no evidence that pNPPase activity is physiologically relevant
714982
Bacillus subtilis
4-nitrophenol + phosphate
-
-
-
?
D-arabinose 5-phosphate + H2O
-
714982
Bacillus subtilis
D-arabinose + phosphate
-
-
-
?
D-fructose 1,6-bisphosphate + H2O
-
714982
Bacillus subtilis
?
-
-
-
?
D-fructose 6-phosphate + H2O
-
714982
Bacillus subtilis
D-fructose + phosphate
-
-
-
?
D-galactose 1-phosphate + H2O
-
714982
Bacillus subtilis
D-galactose + phosphate
-
-
-
?
D-glucose 6-phosphate + H2O
-
714982
Bacillus subtilis
D-glucose + phosphate
-
-
-
?
D-xylulose 5-phosphate + H2O
-
714982
Bacillus subtilis
D-xylulose + phosphate
-
-
-
?
additional information
AraL shows low specificity and catalytic activity towards several sugar phosphates, which are metabolic intermediates of the glycolytic and pentose phosphate pathways, substrate specificity, overview
714982
Bacillus subtilis
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
?
x * 28900, about, sequence calculation
Bacillus subtilis
Temperature Optimum [C] (protein specific)
Temperature Optimum [C]
Temperature Optimum Maximum [C]
Commentary
Organism
65
-
recombinant enzyme
Bacillus subtilis
Temperature Range [C] (protein specific)
Temperature Minimum [C]
Temperature Maximum [C]
Commentary
Organism
25
70
optimal activity at 37C, no activity at 25C, profile, overview
Bacillus subtilis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.012
-
4-nitrophenyl phosphate
pH 7.0, 37C
Bacillus subtilis
1.49
-
D-fructose 1,6-bisphosphate
pH 7.0, 37C
Bacillus subtilis
2.49
-
D-glucose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
2.75
-
D-xylulose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
2.817
-
D-fructose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
2.92
-
D-arabinose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
4.28
-
D-galactose 1-phosphate
pH 7.0, 37C
Bacillus subtilis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7
-
recombinant enzyme
Bacillus subtilis
pH Range (protein specific)
pH Minimum
pH Maximum
Commentary
Organism
4
9
although, at pH 8 and pH 9, the enzyme activity is considerably lower than at pH 7.0, the values are higher than at pH 6.0, no activity below pH 4.0, profile, overview
Bacillus subtilis
General Information
General Information
Commentary
Organism
metabolism
context of araL within the arabinose metabolic operon araABDLMNPQ-abfA, as involved in the transport of L-arabinose oligomers. the ability of AraL to catabolize several secondary metabolites, related to detoxification of accidental accumulation of phosphorylated metabolites, requires regulation at the genetic level. Production of AraL is regulated by a structure in the translation initiation region of the mRNA, which most probably blocks access to the ribosome-binding site, preventing protein synthesis, existence of a genetic regulatory mechanism controlling the production of AraL, overview
Bacillus subtilis
physiological function
putative physiological role of the enzyme AraL in the detoxification of accidental accumulation of phosphorylated metabolites
Bacillus subtilis
General Information (protein specific)
General Information
Commentary
Organism
metabolism
context of araL within the arabinose metabolic operon araABDLMNPQ-abfA, as involved in the transport of L-arabinose oligomers. the ability of AraL to catabolize several secondary metabolites, related to detoxification of accidental accumulation of phosphorylated metabolites, requires regulation at the genetic level. Production of AraL is regulated by a structure in the translation initiation region of the mRNA, which most probably blocks access to the ribosome-binding site, preventing protein synthesis, existence of a genetic regulatory mechanism controlling the production of AraL, overview
Bacillus subtilis
physiological function
putative physiological role of the enzyme AraL in the detoxification of accidental accumulation of phosphorylated metabolites
Bacillus subtilis
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00024
-
4-nitrophenyl phosphate
pH 7.0, 37C
Bacillus subtilis
0.0365
-
D-fructose 1,6-bisphosphate
pH 7.0, 37C
Bacillus subtilis
0.0807
-
D-fructose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
0.0943
-
D-xylulose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
0.0998
-
D-glucose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
0.102
-
D-galactose 1-phosphate
pH 7.0, 37C
Bacillus subtilis
0.106
-
D-arabinose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.00024
-
4-nitrophenyl phosphate
pH 7.0, 37C
Bacillus subtilis
0.0365
-
D-fructose 1,6-bisphosphate
pH 7.0, 37C
Bacillus subtilis
0.0807
-
D-fructose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
0.0943
-
D-xylulose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
0.0998
-
D-glucose 6-phosphate
pH 7.0, 37C
Bacillus subtilis
0.102
-
D-galactose 1-phosphate
pH 7.0, 37C
Bacillus subtilis
0.106
-
D-arabinose 5-phosphate
pH 7.0, 37C
Bacillus subtilis
Other publictions for EC 3.1.3.23
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
750977
Zeng
Essential roles of the sppRA ...
Streptococcus mutans
J. Bacteriol.
201
e00586
2019
-
-
1
-
-
-
1
2
-
2
-
-
-
1
-
-
-
-
-
-
-
1
3
1
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
-
2
-
2
-
-
-
-
-
-
-
-
-
1
3
1
-
-
-
-
1
-
-
-
2
1
1
2
-
-
749666
Maleki
Identification of a new phosp ...
Pseudomonas fluorescens, Pseudomonas fluorescens SBW25
Appl. Environ. Microbiol.
83
e02361
2017
-
-
1
-
-
-
2
2
-
1
-
-
-
5
-
-
-
-
-
-
-
-
8
1
-
-
-
2
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
2
-
2
-
1
-
-
-
-
-
-
-
-
-
-
8
1
-
-
-
2
-
-
-
-
-
1
1
-
2
2
730458
Guggisberg
A sugar phosphatase regulates ...
Plasmodium falciparum
Nat. Commun.
5
4467
2014
-
-
1
1
1
-
-
-
1
1
1
1
-
3
-
-
1
-
-
-
-
-
16
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
1
-
-
-
-
-
1
1
1
1
-
-
-
1
-
-
-
-
16
1
-
-
-
-
-
-
-
-
-
2
2
-
-
-
730667
Caparros-Martin
The kinetic analysis of the su ...
Arabidopsis thaliana
Planta
240
479-487
2014
-
-
1
-
5
-
-
22
-
1
1
-
-
2
-
-
1
-
-
-
-
-
8
1
-
-
-
17
1
-
-
-
-
-
-
-
-
1
-
-
5
-
-
-
-
22
-
1
1
-
-
-
-
1
-
-
-
-
8
1
-
-
-
17
1
-
-
-
-
-
-
-
23
23
714982
Godinho
Characterization and regulatio ...
Bacillus subtilis
FEBS J.
278
2511-2524
2011
-
-
1
-
3
-
-
7
-
1
1
1
-
3
-
-
1
-
-
-
-
-
8
1
1
1
-
7
1
1
-
-
-
-
-
-
-
1
-
-
3
-
-
-
-
7
-
1
1
1
-
-
-
1
-
-
-
-
8
1
1
1
-
7
1
1
-
-
-
2
2
-
7
7
94728
Ye
-
Inducer expulsion and the occu ...
Enterococcus faecalis, Streptococcus pyogenes
Microbiology
142
585-592
1996
-
-
-
-
-
-
-
-
-
-
-
2
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
94725
Cook
Properties of two sugar phosph ...
Streptococcus equinus
J. Bacteriol.
177
7007-7009
1995
1
-
-
-
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
-
-
-
-
7
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
94727
Ye
Purification and characterizat ...
Lactococcus lactis
J. Biol. Chem.
270
16740-16744
1995
1
-
-
-
-
-
-
1
1
5
-
-
-
1
-
-
-
-
-
-
-
-
10
-
-
-
1
-
1
1
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
1
1
5
-
-
-
-
-
-
-
-
-
-
10
-
-
-
1
-
1
1
-
-
-
-
-
-
-
-
94726
Choy
Survey, purification, and prop ...
Escherichia acidilactici, Escherichia coli, Klebsiella aerogenes, Neisseria meningitidis, Saccharomyces cerevisiae
Can. J. Biochem. Cell Biol.
61
1292-1303
1983
-
-
-
-
-
-
-
-
-
-
7
-
-
31
-
-
5
-
-
-
7
-
35
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
7
-
-
-
-
5
-
-
7
-
35
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
94724
Lau
Effects of fluoride on sugar p ...
Escherichia coli, Neisseria meningitidis
Int. J. Biochem.
14
565-567
1982
-
-
-
-
-
-
2
-
1
-
-
-
-
5
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-
2
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
1
-
-
-
-
-
-
2
-
-
-
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1
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-
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-
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94723
Lee
-
Molecular weight and some phys ...
Escherichia coli, Neisseria meningitidis
J. Biol. Chem.
250
3729-3737
1975
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1
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-
11
16
-
-
4
-
-
2
-
-
1
-
-
-
1
1
32
1
-
-
4
-
1
1
3
-
-
-
-
-
-
-
-
1
-
-
-
11
-
16
-
-
4
-
-
-
-
1
-
-
1
1
32
1
-
-
4
-
1
1
3
-
-
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-
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-
-
94722
Lee
Sugar phosphate phosphohydrola ...
Neisseria meningitidis
J. Biol. Chem.
242
2264-2271
1967
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3
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3
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1
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20
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3
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1
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20
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