BRENDA - Enzyme Database
show all sequences of 1.3.1.14

Structure of dihydroorotate dehydrogenase B: electron transfer between two flavin groups bridged by an iron-sulphur cluster

Rowland, P.; Norager, S.; Jensen, K.F.; Larsen, S.; Structure 8, 1227-1238 (2000)

Data extracted from this reference:

Application
Application
Commentary
Organism
medicine
enzyme is a part of the pyrimidine biosynthesis pathway and plays a role as target for the chemotherapy of parasitic and neoplastic diseases
Faecalicatena orotica
medicine
-
Lactococcus lactis
nutrition
applications in the dairy industry
Enterococcus faecalis
nutrition
applications in the dairy industry
Lactococcus lactis
pharmacology
drug design based upon selective enzyme inhibition
Faecalicatena orotica
Crystallization (Commentary)
Crystallization
Organism
hanging-drop vapor diffusion
Lactococcus lactis
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Bacillus subtilis
5829
-
cytosol
-
Enterococcus faecalis
5829
-
cytosol
-
Faecalicatena orotica
5829
-
cytosol
-
Lactococcus lactis
5829
-
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dihydroorotate + NAD+
Lactococcus lactis
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Lactococcus lactis
r
dihydroorotate + NAD+
Enterococcus faecalis
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Enterococcus faecalis
r
dihydroorotate + NAD+
Faecalicatena orotica
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Faecalicatena orotica
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bacillus subtilis
-
-
-
Enterococcus faecalis
-
family IB enzyme, also contains family IA enzyme, milk fermenting bacterium
-
Faecalicatena orotica
-
identical with Clostridium oroticum
-
Lactococcus lactis
-
family IB enzyme, also contains family IA enzyme; milk-fermenting bacterium
-
Purification (Commentary)
Commentary
Organism
-
Lactococcus lactis
Reaction
Reaction
Commentary
Organism
(S)-dihydroorotate + NAD+ = orotate + NADH + H+
electron transfer mechanism
Lactococcus lactis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-dihydroorotate + NAD+
mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+
390569
Lactococcus lactis
orotate + NADH + H+
-
390569
Lactococcus lactis
r
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390569
Bacillus subtilis
orotate + NADH + H+
-
390569
Bacillus subtilis
-
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390569
Lactococcus lactis
orotate + NADH + H+
-
390569
Lactococcus lactis
r
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390569
Enterococcus faecalis
orotate + NADH + H+
-
390569
Enterococcus faecalis
-
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390569
Faecalicatena orotica
orotate + NADH + H+
-
390569
Faecalicatena orotica
r
(S)-dihydroorotate + NAD+
at higher pH values reaction favours direction of dihydroorotate oxidation, whereas at lower pH values direction of orotate reduction is favoured
390569
Lactococcus lactis
orotate + NADH + H+
-
390569
Lactococcus lactis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390569
Lactococcus lactis
orotate + NADH + H+
-
390569
Lactococcus lactis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390569
Enterococcus faecalis
orotate + NADH + H+
-
390569
Enterococcus faecalis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390569
Faecalicatena orotica
orotate + NADH + H+
-
390569
Faecalicatena orotica
r
additional information
-
390569
Faecalicatena orotica
?
-
-
-
-
additional information
NAD+ binding domain in the beta subunit of enzyme, Cys-135 plays a catalytic role and Lys-48 is important for orienting the substrate in the active site and is able to interact with FMN
390569
Lactococcus lactis
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
heterotetramer
alpha subunit is named PyrDB, beta subunit is named PyrK
Bacillus subtilis
heterotetramer
-
Faecalicatena orotica
heterotetramer
alpha2,beta2, alpha subunit with 331 amino acid residues, beta subunit with 262 amino acid residues, two closely interacting PyrDB-PyrK dimers; alpha subunit is named PyrDB, beta subunit is named PyrK
Lactococcus lactis
Cofactor
Cofactor
Commentary
Organism
Structure
4Fe-4S-center
-
Bacillus subtilis
4Fe-4S-center
-
Enterococcus faecalis
4Fe-4S-center
-
Faecalicatena orotica
4Fe-4S-center
two [2Fe-2S] clusters as cofactors, tightly bound to the beta subunit and located in the interface of the two dimers centered between the FMN and FAD group, Cys-226, Cys-231, Cys-234 and Cys-249 binds the iron-sulfur cluster
Lactococcus lactis
FAD
-
Bacillus subtilis
FAD
-
Faecalicatena orotica
FAD
FAD is located on the beta subunit; two tightly bound FAD per heterotetrameric enzyme, FAD is necessary for ability to use NAD+ as electron acceptor, detailed way of binding
Lactococcus lactis
FAD
-
Enterococcus faecalis
FMN
-
Bacillus subtilis
FMN
-
Enterococcus faecalis
FMN
-
Faecalicatena orotica
FMN
FMN is located on the alpha subunit; two tightly bound FMN per heterotetrameric enzyme, detailed way of binding
Lactococcus lactis
Application (protein specific)
Application
Commentary
Organism
medicine
enzyme is a part of the pyrimidine biosynthesis pathway and plays a role as target for the chemotherapy of parasitic and neoplastic diseases
Faecalicatena orotica
medicine
-
Lactococcus lactis
nutrition
applications in the dairy industry
Enterococcus faecalis
nutrition
applications in the dairy industry
Lactococcus lactis
pharmacology
drug design based upon selective enzyme inhibition
Faecalicatena orotica
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
4Fe-4S-center
-
Bacillus subtilis
4Fe-4S-center
-
Enterococcus faecalis
4Fe-4S-center
-
Faecalicatena orotica
4Fe-4S-center
two [2Fe-2S] clusters as cofactors, tightly bound to the beta subunit and located in the interface of the two dimers centered between the FMN and FAD group, Cys-226, Cys-231, Cys-234 and Cys-249 binds the iron-sulfur cluster
Lactococcus lactis
FAD
-
Bacillus subtilis
FAD
-
Faecalicatena orotica
FAD
FAD is located on the beta subunit; two tightly bound FAD per heterotetrameric enzyme, FAD is necessary for ability to use NAD+ as electron acceptor, detailed way of binding
Lactococcus lactis
FAD
-
Enterococcus faecalis
FMN
-
Bacillus subtilis
FMN
-
Enterococcus faecalis
FMN
-
Faecalicatena orotica
FMN
FMN is located on the alpha subunit; two tightly bound FMN per heterotetrameric enzyme, detailed way of binding
Lactococcus lactis
Crystallization (Commentary) (protein specific)
Crystallization
Organism
hanging-drop vapor diffusion
Lactococcus lactis
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
cytosol
-
Bacillus subtilis
5829
-
cytosol
-
Enterococcus faecalis
5829
-
cytosol
-
Faecalicatena orotica
5829
-
cytosol
-
Lactococcus lactis
5829
-
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
dihydroorotate + NAD+
Lactococcus lactis
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Lactococcus lactis
r
dihydroorotate + NAD+
Enterococcus faecalis
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Enterococcus faecalis
r
dihydroorotate + NAD+
Faecalicatena orotica
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
orotate + NADH + H+
-
Faecalicatena orotica
r
Purification (Commentary) (protein specific)
Commentary
Organism
-
Lactococcus lactis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
(S)-dihydroorotate + NAD+
mechanism of dehydrogenation, mechanism of electron transfer: L-dihydroorotate transfers a pair of electrons to FMN via iron-sulfur cluster via FAD to NAD+
390569
Lactococcus lactis
orotate + NADH + H+
-
390569
Lactococcus lactis
r
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390569
Bacillus subtilis
orotate + NADH + H+
-
390569
Bacillus subtilis
-
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390569
Lactococcus lactis
orotate + NADH + H+
-
390569
Lactococcus lactis
r
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390569
Enterococcus faecalis
orotate + NADH + H+
-
390569
Enterococcus faecalis
-
(S)-dihydroorotate + NAD+
NAD+ as ultimate electron acceptor
390569
Faecalicatena orotica
orotate + NADH + H+
-
390569
Faecalicatena orotica
r
(S)-dihydroorotate + NAD+
at higher pH values reaction favours direction of dihydroorotate oxidation, whereas at lower pH values direction of orotate reduction is favoured
390569
Lactococcus lactis
orotate + NADH + H+
-
390569
Lactococcus lactis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390569
Lactococcus lactis
orotate + NADH + H+
-
390569
Lactococcus lactis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390569
Enterococcus faecalis
orotate + NADH + H+
-
390569
Enterococcus faecalis
r
dihydroorotate + NAD+
fourth step and sole redox reaction in the pyrimidine de novo biosynthetic pathway
390569
Faecalicatena orotica
orotate + NADH + H+
-
390569
Faecalicatena orotica
r
additional information
-
390569
Faecalicatena orotica
?
-
-
-
-
additional information
NAD+ binding domain in the beta subunit of enzyme, Cys-135 plays a catalytic role and Lys-48 is important for orienting the substrate in the active site and is able to interact with FMN
390569
Lactococcus lactis
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
heterotetramer
alpha subunit is named PyrDB, beta subunit is named PyrK
Bacillus subtilis
heterotetramer
-
Faecalicatena orotica
heterotetramer
alpha2,beta2, alpha subunit with 331 amino acid residues, beta subunit with 262 amino acid residues, two closely interacting PyrDB-PyrK dimers; alpha subunit is named PyrDB, beta subunit is named PyrK
Lactococcus lactis
Other publictions for EC 1.3.1.14
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)
701809
Kawasaki
b-Type dihydroorotate dehydrog ...
Bifidobacterium bifidum
Appl. Environ. Microbiol.
75
629-636
2009
-
-
-
-
-
-
4
-
-
-
1
-
-
4
-
-
1
-
-
-
-
-
-
1
-
-
-
-
2
1
-
2
-
-
-
-
-
-
2
-
-
-
-
4
-
-
-
-
1
-
-
-
-
1
-
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
674586
Combe
Lys-D48 is required for charge ...
Lactococcus lactis
J. Biol. Chem.
281
17977-17988
2006
-
-
-
-
4
-
-
9
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
9
-
-
-
3
-
-
-
-
-
-
3
-
4
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
9
-
-
-
-
-
-
-
-
-
-
654759
Mohsen
Thermodynamic basis of electro ...
Lactococcus lactis
Biochemistry
43
6498-6510
2004
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
1
-
-
-
-
-
-
-
-
3
-
-
-
-
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-
3
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390568
Argyrou
Dihydroorotate dehydrogenase f ...
Bacillus subtilis, Enterococcus faecalis, Faecalicatena orotica, Lactococcus lactis
Biochemistry
39
10373-10384
2000
6
-
2
-
-
-
-
2
4
-
3
3
-
4
-
-
1
3
-
-
1
1
13
3
1
-
-
3
-
1
-
12
-
-
-
6
-
2
12
-
-
-
-
-
-
2
4
-
3
3
-
-
-
1
-
-
1
1
13
3
1
-
-
3
-
1
-
-
-
-
-
-
-
-
390569
Rowland
Structure of dihydroorotate de ...
Bacillus subtilis, Enterococcus faecalis, Faecalicatena orotica, Lactococcus lactis
Structure
8
1227-1238
2000
-
5
-
1
-
-
-
-
4
-
-
3
-
4
-
-
1
1
-
-
-
-
11
3
-
-
-
-
-
-
-
12
-
-
-
-
5
-
12
1
-
-
-
-
-
-
4
-
-
3
-
-
-
1
-
-
-
-
11
3
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390928
Kahler
Biochemical characterization o ...
Bacillus subtilis, Mus musculus
Arch. Biochem. Biophys.
371
191-201
1999
-
-
1
-
5
-
1
3
-
-
8
1
-
2
-
-
1
1
1
-
-
3
5
1
-
-
-
-
-
-
-
3
2
-
-
-
-
1
3
-
5
-
-
1
2
3
-
-
8
1
-
-
-
1
1
-
-
3
5
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
391244
Marcinkeviciene
Dihydroorotate dehydrogenase B ...
Enterococcus faecalis
Biochemistry
38
13129-13137
1999
-
-
-
-
-
-
-
-
-
-
3
-
-
3
-
-
1
1
-
-
-
-
2
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
3
-
-
-
-
1
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390917
Andersen
Two different dihydroorotate d ...
Lactococcus lactis
J. Bacteriol.
176
3975-3982
1994
-
-
1
-
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-
-
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1
-
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2
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4
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4
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1
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2
1
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1
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4
-
4
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390565
Buntain
-
Latent Inhibitors. Part 4. Irr ...
Faecalicatena orotica
J. Chem. Soc. Perkin Trans. I
1988
3175-3182
1988
-
2
-
-
-
1
12
-
-
-
-
1
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
1
8
-
-
-
2
-
1
-
-
1
-
12
8
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
390564
Friedmann
-
Bestimmung mit Dihydroorotat-D ...
Faecalicatena orotica
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
2
2010-2014
1984
1
-
-
-
-
-
4
2
-
-
-
-
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1
-
-
1
-
-
-
-
1
3
-
-
-
-
1
1
-
-
4
1
-
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1
-
-
4
-
-
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4
1
2
-
-
-
-
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-
-
1
-
-
-
1
3
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
390563
Blattmann
Stereospecificity of the dihyd ...
Faecalicatena orotica
Eur. J. Biochem.
30
130-137
1972
-
-
-
-
-
-
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1
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1
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1
1
2
-
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-
1
-
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-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
1
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
390567
Nelson
Preparation of bovine xanthine ...
Faecalicatena orotica
J. Biol. Chem.
243
5368-5373
1968
-
-
-
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1
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1
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1
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2
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2
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1
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1
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390566
Friedmann
Crystalline dihydroorotic dehy ...
Faecalicatena orotica
J. Biol. Chem.
235
1526-1530
1960
1
-
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1
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-
5
-
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1
-
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1
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-
1
-
-
-
1
1
2
-
2
-
-
1
1
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4
-
-
-
1
-
-
4
1
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1
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2
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2
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390561
Friedmann
Purification and properties of ...
Faecalicatena orotica
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5
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1
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390562
Lieberman
Enzymic synthesis and breakdow ...
Faecalicatena orotica
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1
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