Information on EC 1.2.7.10 - oxalate oxidoreductase

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The expected taxonomic range for this enzyme is: Moorella thermoacetica

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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)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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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-
-
-
?
oxalate + metronidazole
CO2 + reduced metronidazole
show the reaction diagram
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-
-
-
?
oxalate + oxidized ferredoxin
CO2 + reduced ferredoxin
show the reaction diagram
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-
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ir
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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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
oxalate + oxidized ferredoxin
CO2 + reduced ferredoxin
show the reaction diagram
Q2RI41
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ir
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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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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
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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 25°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.09
oxalate
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in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25°C
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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 55°C
0.4
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enzyme from oxalate-grown cells, at pH 7.9 and 55°C
0.6
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using benzyl viologen as a cosubstrate, in 50 mM Tris-HCl (pH 8.5), at 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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)
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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
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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
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 8-11% (w/v) PEG 3000 and 3-4% (w/v) Tacsimate (pH 7.0)
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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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LINKS TO OTHER DATABASES (specific for EC-Number 1.2.7.10)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)