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Enzyme Nomenclature
Information on EC 2.7.1.29 - glycerone kinase
for references in articles please use BRENDA:EC2.7.1.29
Word Map on EC 2.7.1.29
- 2.7.1.29
- 1,3-propanediol
- freundii
-
dissimilation
-
citrobacter
-
dhal
- pt
-
hemiaminal
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Specify your search results
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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EC NUMBER 
COMMENTARY 
2.7.1.29
-
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RECOMMENDED NAME
GeneOntology No.
glycerone kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + glycerone = ADP + glycerone phosphate
-
-
-
-
ATP + glycerone = ADP + glycerone phosphate
covalent substrate-binding and random bi bi kinetic mechanism
-
ATP + glycerone = ADP + glycerone phosphate
substrates and products are bound in hemiaminal linkage to the active site histidine, thereby not activating the cataltically reacting hydroxyl group
-
ATP + glycerone = ADP + glycerone phosphate
nucleotide binding structure, mechanism, and function, overview
-
ATP + glycerone = ADP + glycerone phosphate
nucleotide binding structure, mechanism, and function, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
ATP:glycerone phosphotransferase
-
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CAS REGISTRY NUMBER
COMMENTARY
9027-47-8
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
ATP + acetol
ADP + acetol phosphate
-
i.e. 1-hydroxy-2-propanone
-
?
ATP + DL-glyceraldehyde
ADP + DL-glyceraldehyde 3-phosphate
-
D,L-glyceraldehyde binds strongly to the enzyme, slow product release
-
-
?
phospho-DhaM + 3,4-dihydroxy-2-butanone
dephospho-DhaM + 3-hydroxy-2-butanone-4-phosphate
-
-
?
phospho-DhaM + erythrose
dephospho-DhaM + erythrose 4-phosphate
-
-
?
phospho-DhaM + glyceraldehyde
dephospho-DhaM + glyceraldehyde 2-phosphate
-
-
?
phosphoenolpyruvate + DL-glyceraldehyde
pyruvate + DL-glyceraldehyde 3-phosphate
-
-
-
-
?
phosphorylated DhaM domain of dihydroxyacetone kinase + dihydroxyacetone
dephospho-DhaM + dihydroxyacetone phosphate
enzyme complex uses the PEP:sugar phosphotransferase protein DhaM instead of ATP as phosphoryl donor
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
essential for methanol assimilation
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
involved in detoxification of dihydroxyacetone
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
-
?
ATP + DL-glyceraldehyde
ADP + glyceraldehyde 3-phosphate
-
25% of the activity with dihydroxyacetone
-
?
ATP + DL-glyceraldehyde
ADP + glyceraldehyde 3-phosphate
-
25% of the activity with dihydroxyacetone
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
CTP + dihydroxyacetone
CDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
CTP + dihydroxyacetone
CDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
CTP + dihydroxyacetone
CDP + dihydroxyacetone phosphate
-
lower than 1% of the activity with ATP
-
?
GTP + dihydroxyacetone
GDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
GTP + dihydroxyacetone
GDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
GTP + dihydroxyacetone
GDP + dihydroxyacetone phosphate
-
lower than 1% of the activity with ATP
-
?
ITP + dihydroxyacetone
IDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
ITP + dihydroxyacetone
IDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
ITP + dihydroxyacetone
IDP + dihydroxyacetone phosphate
-
11.2% of activity with ATP
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
regulation involving de-/phosphorylation, and the 3 subunits with ADP and transcription factor DhaR, overview
-
-
?
UTP + dihydroxyacetone
UDP + dihydroxyacetone phosphate
-
25% of activity with ATP
-
?
UTP + dihydroxyacetone
UDP + dihydroxyacetone phosphate
-
3.1% of the activity with ATP
-
?
additional information
?
-
-
no activity with glycerol, hydroxyacetone, hydroxypyruvic acid, chloro-3-hydroxyacetone, and methylglyoxal
-
-
-
additional information
?
-
the enzyme does not show activity with GTP, CTP, TTP and UTP, inorganic triphosphate, and polyphosphate
-
-
-
additional information
?
-
the enzyme does not show activity with GTP, CTP, TTP and UTP, inorganic triphosphate, and polyphosphate
-
-
-
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
-
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
-
additional information
?
-
-
no activity with glycerol, hydroxyacetone, hydroxypuruvic acid, chloro-3-hydroxyacetone, and methylglyoxal
-
-
-
additional information
?
-
-
the enzyme is part of a multicomponent enyzme system, the phosphoenolpyruvate:sugar phosphotransferase system PTS
-
-
-
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
-
second step in assimilation of formaldehyde via the xylulose monophosphate, i.e. dihydroxyacetone cycle during growth of yeast on methanol
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
Q1KLC3
-
-
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
O74192
essential for methanol assimilation
-
?
ATP + dihydroxyacetone
ADP + dihydroxyacetone phosphate
P43550, P54838
involved in detoxification of dihydroxyacetone
-
?
ATP + glycerone
ADP + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
-
-
i.e. dihydroxyacetone phosphate
-
?
phosphoenolpyruvate + glycerone
pyruvate + glycerone phosphate
P76015
regulation involving de-/phosphorylation, and the 3 subunits with ADP and transcription factor DhaR, overview
-
-
?
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
-
additional information
?
-
-
the enzyme is involved in the pathway for glycerol oxidation
-
-
-
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
subunit DhaL contains ADP as cofactor for phosphate double displacement from subunit DhaM to dihydroxyacetone phosphate, evolution of the binding site, conversion of a substrate binding site into a cofactor binding site, overview, complexing with the enzyme increases the thermal unfolding temperature
ADP
-
subunit DhaL contains ADP as cofactor for phosphate double displacement from subunit DhaM to dihydroxyacetone phosphate, evolution of the binding site, conversion of a substrate binding site into a cofactor binding site, overview, complexing with the enzyme increases the thermal unfolding temperature
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
Ca2+
-
can partially replace Mg2+ in activation, 30.3% of activity with Mg2+
Co2+
-
can partially replace Mg2+ in activation, 57.3% of activity with Mg2+
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
both components of the MgATP complex inhibit the kinase at excess concentration
-
additional information
-
glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal are no inhibitors
-
additional information
-
no inhibition by glycerol, hydroxyacetone, hydroxypuruvic acid, and methylglyoxal
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the DhaR transcription factor stimulates the transcription of the dhaKLM operon from a sigma70 promotor and autorepresses expression of DhaR
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00122
dihydroxyacetone
-
pH and temperature not specified in the publication
0.008
dihydroxyacetone
-
apparent value, Km above 0.008 mM, wild type enzyme, in 50 mM potassium phosphate pH 7.5, at 22°C
0.045
dihydroxyacetone
pH 7.5, 30°C, DhaK-DhaL-DhaM complex; pH 7.5, 30°C, DhaK-DhaL-DhaM complex; pH 7.5, 30°C, DhaK-DhaL-DhaM complex
0.302
dihydroxyacetone
-
apparent value, mutant enzyme H56A, in 50 mM potassium phosphate pH 7.5, at 22°C
2.2
dihydroxyacetone
-
apparent value, mutant enzyme H56N, in 50 mM potassium phosphate pH 7.5, at 22°C
additional information
additional information
-
substrate binding constants and reaction kinetics, overview
-
additional information
additional information
-
substrate binding constants and reaction kinetics, overview
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.6
dihydroxyacetone
-
apparent value, mutant enzyme H56A, in 50 mM potassium phosphate pH 7.5, at 22°C
2.8
dihydroxyacetone
pH 7.5, 30°C, DhaK-DhaL-DhaM complex; pH 7.5, 30°C, DhaK-DhaL-DhaM complex; pH 7.5, 30°C, DhaK-DhaL-DhaM complex
3.72
dihydroxyacetone
-
apparent value, mutant enzyme H56N, in 50 mM potassium phosphate pH 7.5, at 22°C
8.45
dihydroxyacetone
-
apparent value, Km above 0.008 mM, wild type enzyme, in 50 mM potassium phosphate pH 7.5, at 22°C
24.13
dihydroxyacetone
-
pH and temperature not specified in the publication
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.7
dihydroxyacetone
-
apparent value, mutant enzyme H56N, in 50 mM potassium phosphate pH 7.5, at 22°C
5.3
dihydroxyacetone
-
apparent value, mutant enzyme H56A, in 50 mM potassium phosphate pH 7.5, at 22°C
954
dihydroxyacetone
-
apparent value, Km above 0.008 mM, wild type enzyme, in 50 mM potassium phosphate pH 7.5, at 22°C
19800
dihydroxyacetone
-
pH and temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
62245
2 * 62245, recombinant enzyme, deduced from amino acid sequence
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homodimer
trimer
additional information
dimer
2 * 62000, recombinant enzyme, SDS-PAGE; 2 * 62245, recombinant enzyme, deduced from amino acid sequence
trimer
-
enzyme exists of 3 subunit DhaK, DhaM, and DhaL: DhaK contains the dihydroxyacetone phosphate binding site, DhaL contains ADP as cofactor for phosphate double displacement from DhaM to dihydroxyacetone phosphate, and DhaM provides a phospho-histidine relay between phosphoenolpyruvate and DhaL-ADP
trimer
-
enzyme exists of 3 subunit DhaK, DhaM, and DhaL: DhaK contains the dihydroxyacetone phosphate binding site, DhaL contains ADP as cofactor for phosphate double displacement from DhaM to dihydroxyacetone phosphate, and DhaM provides a phospho-histidine relay between phosphoenolpyruvate and DhaL-ADP
additional information
approx. 18000 Da, monomeric state is suggested; approx. 35000 Da, monomeric state is suggested; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
approx. 18000 Da, monomeric state is suggested; approx. 35000 Da, monomeric state is suggested; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
additional information
approx. 18000 Da, monomeric state is suggested; approx. 35000 Da, monomeric state is suggested; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM; enzyme comlex is present in an approx. 1/1/1 ratio of DhaK, DhaL and DhaM
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of enzyme complex with an ATP analogue and dihydroxyacetone at 2.5 A resolution
apoenzyme, from solution containing 80 mM sodium acetate, pH 5.0, 160 mM ammonium sulfate, 17% w/v PEG 4000, 15% w/v methylpentanediol, hanging drop vapour diffusion method, apoenzyme-crystals are soaked in 2 mM glyceraldehyde or 5 mM dihydroxyacetone phosphate and flash frozen at -168°C, X-ray diffraction structure determination and analysis at 2.0 and 1.9 A resolution, respectively
-
DhaK and DhaK-dihydroxacetone complex are crystallized from 80 mM sodium acetate, pH 5.0, 160 mM ammonium sulfate, 17% polyethylene glycol 4000, 15% 2-methyl-2,4-pentanediol using hanging drop vapor diffusion, crystals diffract to 1.75 A resolution
DhaK-DhaL complex bound to ADP anddihydroxyacetone, hanging drop vapor diffusion method, using 0.1 M HEPES pH 7.5, 3.5 M sodium formate or 0.1 M sodium citrate pH 5.6, 20% (w/v)PEG 8000, at 19°C
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
65
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
glycerol, most effective stabilizer, EDTA and MgCl2 stabilize to a lesser extent, inactivated during ammonium sulfate precipitation
-
not affected by 2 M glycerol
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate, butyl-Toyopearl, UNO-Q6, recombinant enzyme
DEAE-cellulose, Superdex 75; DEAE-cellulose, Superdex 75; HighQ anion exchange, Superdex 200
polyethylene glycol 6000, polyethyleneimine, DEAE-Sepharose, Sepharose CL-6B
-
streptomycin sulfate, ammonium sulfate, Cibacron blue F3G-ASephadex g-200, DEAE cellulose, partially purified
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli NM522 cells
expressed in Escherichia coli strain BL21(DE3) and in chloroplasts from Nicotiana tabacum cultivar Xanthi
-
overexpression in Escherichia coli; overexpression in Escherichia coli; overexpression in Escherichia coli
phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
the enzyme has nearly no activity changes under continuous cultivation from 0.5 to 3.0 M NaCl but the activity increases significantly with further increased salinities and achieves the maximum under 4.5 M NaCl
-
inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
-
inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
-
inactivation of the gene lin0370 causes 20fold-elevated expression level of the dhaK-2 gene
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H56A
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
H56N
-
the mutant shows severely reduced catalytic efficiency compared to the wild type enzyme
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LINKS TO OTHER DATABASES (specific for EC-Number 2.7.1.29)
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