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Information on EC 1.2.7.10 - oxalate oxidoreductase for references in articles please use BRENDA:EC1.2.7.10
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EC Tree
IUBMB Comments Contains thiamine diphosphate and [4Fe-4S] clusters. Acceptors include ferredoxin and the nickel-dependent carbon monoxide dehydrogenase (EC 1.2.7.4)
The expected taxonomic range for this enzyme is: Moorella thermoacetica
Synonyms
oxalate:ferredoxin oxidoreductase,
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OOR
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oxalate + oxidized ferredoxin = 2 CO2 + reduced ferredoxin
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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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2-oxobutyrate + methyl viologen
?
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?
2-oxoglutarate + H2O + methyl viologen
?
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?
2-oxovalerate + H2O + methyl viologen
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very low activity
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?
glyoxylate + methyl viologen
?
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-
-
-
?
oxalate + benzyl viologen
CO2 + reduced benzyl viologen
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-
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?
oxalate + cytochrome c
CO2 + reduced cytochrome c
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cytochrome c is the best electron acceptor
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?
oxalate + FAD
CO2 + FADH2
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-
?
oxalate + ferredoxin
CO2 + reduced ferredoxin
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oxalate is the best substrate
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?
oxalate + FMN
CO2 + FMNH2
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-
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?
oxalate + methyl viologen
CO2 + reduced methyl viologen
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-
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?
oxalate + metronidazole
CO2 + reduced metronidazole
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-
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-
?
oxalate + oxidized ferredoxin
CO2 + reduced ferredoxin
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ir
oxaloacetate + H2O + methyl viologen
?
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?
pyruvate + methyl viologen
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?
additional information
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additional information
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cell extracts also catalyze the formate-dependent reduction of NADP+, oxalate-dependent reduction of NADP+ is negligible. Oxalate- or formate-dependent reduction of NAD+ is not observed
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additional information
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OOR does not use formate, coenzyme A, ATP, NAD+, and NADP+ and as a substrate
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oxalate + oxidized ferredoxin
CO2 + reduced ferredoxin
Q2RI41
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ir
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4Fe-4S-center
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the enzyme contains three [Fe4S4] clusters
thiamine diphosphate
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dependent on
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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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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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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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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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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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brenda
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UniProt
brenda
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brenda
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brenda
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OORA_MOOTA
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
395
0
43687
Swiss-Prot
OORB_MOOTA
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
314
0
34234
Swiss-Prot
OORD_MOOTA
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
315
0
33931
Swiss-Prot
A0A140LCX1_9THEO
314
0
34303
TrEMBL
A0A2H5ZTK4_9BACT
332
0
36718
TrEMBL
A0A162MWI5_9FIRM
315
0
33921
TrEMBL
A0A2H5ZSN6_9BACT
407
0
45647
TrEMBL
A0A162MWI8_9FIRM
395
0
43896
TrEMBL
A0A2H5ZTW4_9BACT
392
0
44326
TrEMBL
A0A140LCX0_9THEO
395
0
43861
TrEMBL
A0A1V0RS48_9RHOB
651
0
68661
TrEMBL
A0A140LCW9_9THEO
315
0
34064
TrEMBL
A0A2R8BYB1_9RHOB
658
0
69566
TrEMBL
A0A161QDH4_9FIRM
312
0
34057
TrEMBL
A0A2H5V648_9ARCH
307
0
34340
TrEMBL
A0A223Z084_9EURY
288
0
31594
TrEMBL
A0A2H5ZSK8_9BACT
392
0
44579
TrEMBL
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Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
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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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
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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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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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DEAE-cellulose column chromatography, red agarose column chromatography, phenyl-Sepharose column chromatography, and Q-Sepharose column chromatography
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Daniel, S.; Pilsl, C.; Drake, H.
Oxalate metabolism by the acetogenic bacterium Moorella thermoacetica
FEMS Microbiol. Lett.
231
39-43
2004
Moorella thermoacetica
brenda
Pierce, E.; Becker, D.F.; Ragsdale, S.W.
Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate
J. Biol. Chem.
285
40515-40524
2010
Moorella thermoacetica
brenda
Gibson, M.I.; Brignole, E.J.; Pierce, E.; Can, M.; Ragsdale, S.W.; Drennan, C.L.
The structure of an oxalate oxidoreductase provides insight into microbial 2-oxoacid metabolism
Biochemistry
54
4112-4120
2015
Moorella thermoacetica (Q2RI41)
brenda
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