Information on EC 1.2.7.10 - oxalate oxidoreductase

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The expected taxonomic range for this enzyme is: Moorella thermoacetica

EC NUMBER
COMMENTARY hide
1.2.7.10
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RECOMMENDED NAME
GeneOntology No.
oxalate oxidoreductase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
oxalate + oxidized ferredoxin = 2 CO2 + reduced ferredoxin
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
oxalate degradation I
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SYSTEMATIC NAME
IUBMB Comments
oxalate:ferredoxin oxidoreductase
Contains thiamine diphosphate and [4Fe-4S] clusters. Acceptors include ferredoxin and the nickel-dependent carbon monoxide dehydrogenase (EC 1.2.7.4)
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxobutyrate + methyl viologen
?
show the reaction diagram
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-
-
-
?
2-oxoglutarate + H2O + methyl viologen
?
show the reaction diagram
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-
-
-
?
2-oxovalerate + H2O + methyl viologen
?
show the reaction diagram
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very low activity
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-
?
glyoxylate + methyl viologen
?
show the reaction diagram
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-
-
-
?
oxalate + benzyl viologen
CO2 + reduced benzyl viologen
show the reaction diagram
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-
-
-
?
oxalate + cytochrome c
CO2 + reduced cytochrome c
show the reaction diagram
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cytochrome c is the best electron acceptor
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-
?
oxalate + FAD
CO2 + FADH2
show the reaction diagram
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-
-
-
?
oxalate + ferredoxin
CO2 + reduced ferredoxin
show the reaction diagram
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oxalate is the best substrate
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-
?
oxalate + FMN
CO2 + FMNH2
show the reaction diagram
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-
-
-
?
oxalate + methyl viologen
CO2 + reduced methyl viologen
show the reaction diagram
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-
-
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?
oxalate + metronidazole
CO2 + reduced metronidazole
show the reaction diagram
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-
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?
oxaloacetate + H2O + methyl viologen
?
show the reaction diagram
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-
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?
pyruvate + methyl viologen
?
show the reaction diagram
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4Fe-4S-center
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the enzyme contains three [Fe4S4] clusters
thiamine diphosphate
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dependent on
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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the enzyme contains 14 mol iron per mol protein
Mg2+
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the enzyme contains 0.8 mol Mg2+ per mol protein
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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addition of CoA, acetyl-CoA, or succinyl-CoA to the assay has a minimal effect on the oxalate-dependent reduction of benzyl viologen
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.058
oxalate
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in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
oxalate
Moorella thermoacetica
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in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.03
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enzyme from glucose-grown cells, at pH 7.9 and 55C
0.4
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enzyme from oxalate-grown cells, at pH 7.9 and 55C
0.6
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using benzyl viologen as a cosubstrate, in 50 mM Tris-HCl (pH 8.5), at 37C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
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1 * 36000 + 1 * 43000 + 1 * 32000, the active protein consists of three peptides in 1:0.8:1 stoichiometry, with estimated sizes of 36000, 43000, and 32000 Da, SDS-PAGE, SDS-PAGE
33900
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1 * 34200 + 1 * 33900 + 1 * 43700, the active protein consists of three peptides with estimated sizes of 34200, 339000, and 43700 Da, calculated from amino acid sequence
34200
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1 * 34200 + 1 * 33900 + 1 * 43700, the active protein consists of three peptides with estimated sizes of 34200, 339000, and 43700 Da, calculated from amino acid sequence
36000
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1 * 36000 + 1 * 43000 + 1 * 32000, the active protein consists of three peptides in 1:0.8:1 stoichiometry, with estimated sizes of 36000, 43000, and 32000 Da, SDS-PAGE, SDS-PAGE
43000
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1 * 36000 + 1 * 43000 + 1 * 32000, the active protein consists of three peptides in 1:0.8:1 stoichiometry, with estimated sizes of 36000, 43000, and 32000 Da, SDS-PAGE, SDS-PAGE
43700
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1 * 34200 + 1 * 33900 + 1 * 43700, the active protein consists of three peptides with estimated sizes of 34200, 339000, and 43700 Da, calculated from amino acid sequence
226900
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analytical ultracentrifugation
236000
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gel filtration
243000
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native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterotrimer
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1 * 34200 + 1 * 33900 + 1 * 43700, the active protein consists of three peptides with estimated sizes of 34200, 339000, and 43700 Da, calculated from amino acid sequence; 1 * 36000 + 1 * 43000 + 1 * 32000, the active protein consists of three peptides in 1:0.8:1 stoichiometry, with estimated sizes of 36000, 43000, and 32000 Da, SDS-PAGE, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose column chromatography, red agarose column chromatography, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
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