Information on EC 6.2.1.13 - Acetate-CoA ligase (ADP-forming)

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The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota

EC NUMBER
COMMENTARY hide
6.2.1.13
-
RECOMMENDED NAME
GeneOntology No.
Acetate-CoA ligase (ADP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + acetate + CoA = ADP + phosphate + acetyl-CoA
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
acetate formation from acetyl-CoA II
-
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acetyl CoA biosynthesis
-
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Glycolysis / Gluconeogenesis
-
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L-glutamate degradation V (via hydroxyglutarate)
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Metabolic pathways
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Microbial metabolism in diverse environments
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Propanoate metabolism
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pyruvate fermentation to acetate III
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Pyruvate metabolism
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SYSTEMATIC NAME
IUBMB Comments
Acetate:CoA ligase (ADP-forming)
Also acts on propanoate and, very slowly, on butanoate.
CAS REGISTRY NUMBER
COMMENTARY hide
62009-85-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
strain WB, clone 6, ATCC 30957
SwissProt
Manually annotated by BRENDA team
strain DSM 5350
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Manually annotated by BRENDA team
strain DSM 3757
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-
Manually annotated by BRENDA team
strain DSM 1137
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-
Manually annotated by BRENDA team
enzyme form ACS1; enzyme form ACS2
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Manually annotated by BRENDA team
strain DSM 4184
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-
Manually annotated by BRENDA team
gene acs
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-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
ADP + phosphate + butanoyl-CoA
ATP + butanoate + CoA
show the reaction diagram
ADP + phosphate + butyryl-CoA
ATP + butyrate + CoA
show the reaction diagram
ADP + phosphate + indoleacetyl-CoA
ATP + indoleacetate + CoA
show the reaction diagram
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r, isoenzyme ACS II is active, ACS I not
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-
-
ADP + phosphate + isobutyryl-CoA
ATP + isobutyrate + CoA
show the reaction diagram
-
-
-
-
r
ADP + phosphate + phenylacetyl-CoA
ATP + phenylacetate + CoA
show the reaction diagram
ADP + phosphate + propanoyl-CoA
ATP + propanoate + CoA
show the reaction diagram
45% of the activity relative to acetyl-CoA
-
?
ADP + phosphate + propionyl-CoA
ATP + propionate + CoA
show the reaction diagram
ADP + phosphate + succinyl-CoA
ATP + succinate + CoA
show the reaction diagram
ATP + 2-methylbutyrate + CoA
ADP + phosphate + 2-methylbutyryl-CoA
show the reaction diagram
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75% activity compared to acetate
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-
?
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
ATP + butyrate + CoA
ADP + phosphate + butyryl-CoA
show the reaction diagram
ATP + imidazole-4-acetate + CoA
ADP + phosphate + imidazole-4-acetyl-CoA
show the reaction diagram
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17% activity compared to acetate
-
-
?
ATP + isobutyrate + CoA
ADP + phosphate + isobutyryl-CoA
show the reaction diagram
ATP + isopentanioate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
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34% of the activity relative to acetate
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-
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ATP + isovalerate + CoA
ADP + phosphate + isovaleryl-CoA
show the reaction diagram
ATP + n-butyrate + CoA
ADP + phosphate + n-butyryl-CoA
show the reaction diagram
ATP + pentanoate + CoA
ADP + phosphate + valeryl-CoA
show the reaction diagram
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36% of the activity relative to acetate
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-
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ATP + phenylacetate + CoA
ADP + phosphate + phenylacetyl-CoA
show the reaction diagram
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10% activity compared to acetate
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-
?
ATP + propionate + CoA
ADP + phosphate + propionyl-CoA
show the reaction diagram
ATP + thioglycolate + CoA
ADP + phosphate + thioglycolyl-CoA
show the reaction diagram
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110% activity compared to acetate
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-
?
dADP + phosphate + acetyl-CoA
dATP + acetate + CoA
show the reaction diagram
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40% of the activity relative to ADP
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GDP + phosphate + acetyl-CoA
GTP + acetate + CoA
show the reaction diagram
GTP + acetate + CoA
GDP + phosphate + acetyl-CoA
show the reaction diagram
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11% of the activity with ATP
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-
?
IDP + phosphate + acetyl-CoA
ITP + acetate + CoA
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ADP + phosphate + acetyl-CoA
?
show the reaction diagram
ADP + phosphate + acetyl-CoA
ATP + acetate + CoA
show the reaction diagram
ATP + acetate + CoA
ADP + phosphate + acetyl-CoA
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP
E7FI45 and E7FHP1
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NADH
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oxidation to NAD+ by assay system lactate dehydrogenase and pyruvate kinase
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Isobutyrate
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10 mM, complete inhibition
NaCl
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2-3 M, 40% loss of activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.5 - 5.3
acetate
0.0039 - 0.45
acetyl-CoA
0.015 - 0.283
ADP
0.07 - 1
ATP
0.0139 - 0.41
CoA
1.09
dADP
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-
0.132 - 0.236
GDP
0.43
GTP
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isoenzyme ACS I
0.457
Isobutyrate
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isoenzyme ACS I
0.012 - 0.04
isobutyryl-CoA
0.004 - 0.11
phenylacetyl-CoA
0.1 - 2
phosphate
5.2 - 8.55
Propionate
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
67
acetate
Pyrococcus furiosus
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isoenzyme ACS II
42 - 157
acetyl-CoA
115 - 203
ADP
68 - 82
ATP
65 - 73
CoA
21 - 411
GDP
27
GTP
Pyrococcus furiosus
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isoenzyme ACS II
66
indoleacetate
Pyrococcus furiosus
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isoenzyme ACS II
22 - 55
Isobutyrate
8 - 121
isobutyryl-CoA
89
phenylacetate
Pyrococcus furiosus
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isoenzyme ACS II
138
phenylacetyl-CoA
Pyrococcus furiosus
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isoenzyme ACS II
117 - 182
phosphate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.04
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pH 9.0, at 37C, oxic conditions, during exponential growth phase on glucose
0.3
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50C, pH not specified in the publication, enzyme from lactate-grown cells
0.45
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pH 9.0, at 37C, oxic conditions, purified enzyme
30
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isoenzyme ACS II
64.6
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isoenzyme ACS I
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
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pH 5.5: about 40% of maximal activity, pH 7.5: about 20% of maximal activity
6 - 11
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6: about 60% of maximal activity, 11: about 40% of maximal activity, isoenzyme ACS I
6 - 8
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about 50% of maximal activity at pH 6 and 8
6.5 - 8.5
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pH 6.5: about 60% of maximal activity, pH 8.5: about 60% of maximal activity
7 - 11
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7: about 60% of maximal activity, 11: about 65% of maximal activity, isoenzyme ACS II
7.3 - 7.8
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the pH optimum is at pH 7.5, with remaining activities of about 40% at pH 7.3 and 59% at pH 7.8
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 30
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isoenzyme ACS1
80
E7FI45 and E7FHP1
assay at, catalytic arsenolysis of acetyl-CoA
87
Q9Y8L0, Q9Y8L1
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
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20C: about 75% of maximal activity, 40C: about 45% of maximal activity, isoenzyme ACS1
25 - 55
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25C: about 45% of maximal activity, 55C: about 40% of maximal activity, isoenzyme ACS2
25
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isoenzymes ACS I and ACS II are inactive at
30 - 50
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30C: about 50% of maximal activity, 50C: about 80% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.2
estimation from sequence of cDNA
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
78000
estimation from sequence of cDNA
140000 - 150000
140000
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gel filtration
145000
150000 - 165000
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native PAGE
150000
E7FI45 and E7FHP1
gel filtration
166000
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gel filtration
300000
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native enzyme, gel filtration
317000
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recombinant enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 70000, isoenzyme ACS1, SDS-PAGE; x * 77000, isoenzyme ACS2, SDS-PAGE
dimer
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2 * 87000, SDS-PAGE
heterotetramer
homotetramer
monomer
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
phosphoprotein
E7FI45 and E7FHP1
His257alpha and His71beta are sites of transient phosphorylation
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme, sitting-drop vapour-diffusion method, crystals belong to monoclinic space group C2, with unit-cell parameters a = 131.3, b = 186.1, c = 121.5, beta = 122.6, and diffract at 2.0 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
90
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half-life: 105 min
110
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half-life is 30 min
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
requires high salt concentrations for long-term stability
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salts stabilize against heat inactivation. In presence of 1 M KCl the enzyme does not lose activity after 2 h incubation
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sensitivity towards heat inactivation is increased with storage at -20C
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stability for more than 48 requires high salt concentrations, i.e., 1-2 M of KCl or NaCl
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
stable to oxygen for 24 h
-
626
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 1-2 mg/ml enzyme, in 20 mM Tris/HCl, pH 8.0, 2 mM MgCl2, 150 mM NaCl, stable for several weeks
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on ice stable for 2 d
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
about 10fold, 15 min at 80C and subsequent anion-exchange chromatography
Q9Y8L0, Q9Y8L1
gel filtration on a Superdex TM200 column
ion-exchange chromatography
isoenzymes ACS I and ACS II
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Ni-NTA affinity chromatography, phenyl Sepharose column chromatography, Q-Sepharose column chromatography, and Superdex 200 gel filtration
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partial, isoenzyme ACS1; partial, isoenzyme ACS2
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recombinant wild-type and mutant enzyme subunits from Escherichia coli strain BL21(DE3) by heat precipitation at 90C for 30 min, followed by reconstitution of holoenzyme through hydrophobic interaction chromatography ultrafiltration, and gel filtration, the chromatographic steps are then repeated; wild-type end mutant enzymes
E7FI45 and E7FHP1
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
acdIa and acdIb genes encoding alpha- and beta-subunit of ACD, expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
E7FI45 and E7FHP1
expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
overexpression in Escherichia coli
Q9Y8L0, Q9Y8L1
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme is induced 10fold during growth on D-glucose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D212betaE
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 2-4% of the wild-type activity, phosphorylation of the mutant is reduced
E218alphaD
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. The mutant shows 1-10% of the wild-type activity, phopshorylation of the mutant is reduced
E218alphaQ
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, phopshorylation of the mutant is reduced
E218Dalpha
E7FI45 and E7FHP1
1-10% of wild-type activity
H257alphaD
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is not phosphorylated at both the alpha- and beta-subunit
H257Dalpha
E7FI45 and E7FHP1
mutant shows no activity in either direction
H71betaA
E7FI45 and E7FHP1
site-directed mutagenesis, comparison of the wild-type CD spectrum with the mutant CD spectrum, structure and reaction kinetics, overview. Inactive mutant, which is impaired in phosphorylation of the beta subunit
G266S
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the Acs mutant does not cause growth arrest in contrast to the wild-type enzyme
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed mixed and incubated on ice; equal amounts of Escherichia coli extracts containing alpha and beta subunits separately expressed, mixed and incubated on ice
Q9Y8L0, Q9Y8L1
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