BRENDA - Enzyme Database show
show all sequences of 1.3.5.4

The function of the subunits of the fumarate reductase complex of Vibrio succinogenes

Unden, G.; Kröger, A.; Eur. J. Biochem. 120, 577-584 (1981)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
25000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
Wolinella succinogenes
31000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
Wolinella succinogenes
79000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
Wolinella succinogenes
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
Wolinella succinogenes
-
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
Wolinella succinogenes
?
additional information
Wolinella succinogenes
the fumarate reductase complex has two different reactive sites, which are essential for its function in the phosphorylative electron transport of the bacterium
?
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Wolinella succinogenes
-
formerly Vibrio succinogenes, fumarate reductase
-
Renatured (Commentary)
Commentary
Organism
the cleavage of the complex causes the complete loss of activity of fumarate reduction by dimethylnaphthohydroquinone, the activity can be restored by coprecipitation of the three subunits of MW: 79000 Da, 31000 Da and 25000 Da
Wolinella succinogenes
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
-
391084
Wolinella succinogenes
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
391084
Wolinella succinogenes
?
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
reaction catalyzed by fumarate reductase complex, the site of the complex reacting with fumarate is situated on the 79000 Da subunit, and the site reacting with dimethylnaphthohydroquinone is cytochrome b
391084
Wolinella succinogenes
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
391084
Wolinella succinogenes
?
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
reaction catalyzed by fumarate reductase complex, the site of the complex reacting with fumarate is situated on the 79000 Da subunit, and the site reacting with dimethylnaphthohydroquinone is cytochrome b
391084
Wolinella succinogenes
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
391084
Wolinella succinogenes
r
additional information
the fumarate reductase complex has two different reactive sites, which are essential for its function in the phosphorylative electron transport of the bacterium
391084
Wolinella succinogenes
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
tetramer
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
Wolinella succinogenes
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
20
-
fumarate
based on the content of the MW 79000 peptide, reduction of fumarate with dimethylnaphthohydroquinone
Wolinella succinogenes
Cofactor
Cofactor
Commentary
Organism
Structure
cytochrome b
has a MW of 25000 Da, a midpoint potential of - 15 mV and is reducible by dimethylnaphthohydroquinone in the absence of the other subunits
Wolinella succinogenes
additional information
measurement of the redox potentials of the sulfur-centers
Wolinella succinogenes
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
cytochrome b
has a MW of 25000 Da, a midpoint potential of - 15 mV and is reducible by dimethylnaphthohydroquinone in the absence of the other subunits
Wolinella succinogenes
additional information
measurement of the redox potentials of the sulfur-centers
Wolinella succinogenes
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
25000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
Wolinella succinogenes
31000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
Wolinella succinogenes
79000
-
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
Wolinella succinogenes
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
Wolinella succinogenes
-
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
Wolinella succinogenes
?
additional information
Wolinella succinogenes
the fumarate reductase complex has two different reactive sites, which are essential for its function in the phosphorylative electron transport of the bacterium
?
-
-
-
Renatured (Commentary) (protein specific)
Commentary
Organism
the cleavage of the complex causes the complete loss of activity of fumarate reduction by dimethylnaphthohydroquinone, the activity can be restored by coprecipitation of the three subunits of MW: 79000 Da, 31000 Da and 25000 Da
Wolinella succinogenes
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
-
391084
Wolinella succinogenes
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
391084
Wolinella succinogenes
?
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
reaction catalyzed by fumarate reductase complex, the site of the complex reacting with fumarate is situated on the 79000 Da subunit, and the site reacting with dimethylnaphthohydroquinone is cytochrome b
391084
Wolinella succinogenes
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
391084
Wolinella succinogenes
?
fumarate + 2,3-dimethyl-1,4-naphthohydroquinone
reaction catalyzed by fumarate reductase complex, the site of the complex reacting with fumarate is situated on the 79000 Da subunit, and the site reacting with dimethylnaphthohydroquinone is cytochrome b
391084
Wolinella succinogenes
succinate + 2,3-dimethyl-1,4-naphthoquinone
-
391084
Wolinella succinogenes
r
additional information
the fumarate reductase complex has two different reactive sites, which are essential for its function in the phosphorylative electron transport of the bacterium
391084
Wolinella succinogenes
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
1 * 79000, FAD-binding subunit, 1 * 31000, Fe-S cluster containing subunit, 2 * 25000, cytochrome b containing subunits, SDS-PAGE
Wolinella succinogenes
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
20
-
fumarate
based on the content of the MW 79000 peptide, reduction of fumarate with dimethylnaphthohydroquinone
Wolinella succinogenes
Other publictions for EC 1.3.5.4
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)
743255
Kassem
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Campylobacter jejuni subsp. jejuni
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168-181
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742846
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Plasticity of the quinone-bin ...
Escherichia coli
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288
24293-24301
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1
1
9
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15
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1
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3
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33
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2
1
9
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15
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3
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33
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743059
Nasiri
Design, synthesis, and biolog ...
Wolinella succinogenes, Wolinella succinogenes DSM 1740
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9530-9541
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4
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724561
Herzog
Hydrogen-bonded networks along ...
Campylobacter jejuni, Helicobacter pylori, Wolinella succinogenes
Biophys. J.
103
1305-1314
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3
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3
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3
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2
3
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6
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6
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3
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3
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2
3
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3
3
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725316
Shimizu
Crystal structure of mitochond ...
Ascaris suum
J. Biochem.
151
589-592
2012
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1
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700278
Juhnke
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Campylobacter jejuni, Wolinella succinogenes
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1088-1101
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1
1
1
1
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707545
Xin
Purification, characterization ...
Chloroflexus aurantiacus
Biochim. Biophys. Acta
1787
86-96
2009
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1
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4
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707949
Garcia
The succinate:menaquinone redu ...
Bacillus cereus
Can. J. Microbiol.
54
456-466
2008
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2
2
1
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3
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1
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2
1
2
1
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1
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1
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1
1
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674532
Maklashina
Fumarate reductase and succina ...
Escherichia coli
J. Biol. Chem.
281
11357-11365
2006
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1
3
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2
5
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5
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6
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5
5
674634
Maklashina
Differences in protonation of ...
Escherichia coli
J. Biol. Chem.
281
26655-26664
2006
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4
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1
2
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7
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7
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707470
Madej
Experimental evidence for prot ...
Bacillus licheniformis
Biochemistry
45
15049-15055
2006
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671694
Fernandes
Quinone reduction by Rhodother ...
Rhodothermus marinus
Biochem. Biophys. Res. Commun.
330
565-570
2005
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654820
Cecchini
Succinate dehydrogenase and fu ...
Escherichia coli
Biochim. Biophys. Acta
1553
140-157
2002
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1
1
1
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3
1
1
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1
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708975
Iverson
Crystallographic studies of th ...
Escherichia coli
J. Biol. Chem.
277
16124-16130
2002
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708368
Schnorpfeil
Generation of a proton potenti ...
Bacillus subtilis
Eur. J. Biochem.
268
3069-3074
2001
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391149
Lancaster
Succinate:quinone oxidoreducta ...
Escherichia coli, Wolinella succinogenes
Biochim. Biophys. Acta
1459
422-431
2000
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708909
Maklashina
Anaerobic expression of Escher ...
Escherichia coli
J. Bacteriol.
180
5989-5996
1998
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708966
Schroder
Identification of active site ...
Escherichia coli
J. Biol. Chem.
266
13572-13579
1991
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391090
Körtner
Wolinella succinogenes fumarat ...
Wolinella succinogenes
Mol. Microbiol.
4
855-860
1990
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391089
Lauterbach
Cloning and expression of the ...
Wolinella succinogenes
Eur. J. Biochem.
166
447-452
1987
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2
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391106
Weiner
A mutant of Escherichia coli f ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
83
2056-2060
1986
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1
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1
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4
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1
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4
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1
1
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391147
Gottfried
Reconstitution of a functional ...
Wolinella succinogenes
Methods Enzymol.
126
387-399
1986
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4
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4
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1
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710440
Cecchini
Oxidation of reduced menaquino ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
83
8898-8902
1986
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1
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1
1
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391094
Unden
-
Redox potentials and kinetic p ...
Wolinella succinogenes
Biochim. Biophys. Acta
767
460-469
1984
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3
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1
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391084
Unden
The function of the subunits o ...
Wolinella succinogenes
Eur. J. Biochem.
120
577-584
1981
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2
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1
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4
1
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391092
Unden
Isolation and functional aspec ...
Wolinella succinogenes
Biochim. Biophys. Acta
591
275-288
1980
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1
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6
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2
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6
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2
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391116
Kröger
The orientation of the substra ...
Wolinella succinogenes
Biochim. Biophys. Acta
589
118-136
1980
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707291
Van der Beek
Fumarate reduction in Proteus ...
Proteus mirabilis
Arch. Microbiol.
110
195-206
1976
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2
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2
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2
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708369
Kroeger
-
The function of menaquinone, c ...
Wolinella succinogenes
Eur. J. Biochem.
69
487-495
1976
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1
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2
1
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1
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1
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1
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