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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: Archaea, Bacteria
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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
?
-
-
-
-
?
2-oxoglutarate + H2O + methyl viologen
?
-
-
-
-
?
2-oxovalerate + H2O + methyl viologen
?
-
very low activity
-
-
?
glyoxylate + methyl viologen
?
-
-
-
-
?
oxalate + benzyl viologen
CO2 + reduced benzyl viologen
-
-
-
-
?
oxalate + cytochrome c
CO2 + reduced cytochrome c
-
cytochrome c is the best electron acceptor
-
-
?
oxalate + FAD
CO2 + FADH2
-
-
-
-
?
oxalate + ferredoxin
CO2 + reduced ferredoxin
-
oxalate is the best substrate
-
-
?
oxalate + FMN
CO2 + FMNH2
-
-
-
-
?
oxalate + methyl viologen
CO2 + reduced methyl viologen
-
-
-
-
?
oxalate + metronidazole
CO2 + reduced metronidazole
-
-
-
-
?
oxalate + oxidized ferredoxin
CO2 + reduced ferredoxin
-
-
-
ir
oxaloacetate + H2O + methyl viologen
?
-
-
-
-
?
pyruvate + methyl viologen
?
-
-
-
-
?
additional information
?
-
additional information
?
-
-
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
-
-
?
additional information
?
-
-
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
-
-
-
ir
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4Fe-4S-center
-
the enzyme contains three [Fe4S4] clusters
thiamine diphosphate
-
thiamine diphosphate
-
dependent on
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Fe2+
-
the enzyme contains 14 mol iron per mol protein
Mg2+
-
the enzyme contains 0.8 mol Mg2+ per mol protein
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additional information
-
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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Kidney Calculi
The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism.
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0.058
oxalate
-
in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25°C
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0.09
oxalate
-
in 50 mM Tris-HCl, 2 mM dithiothreitol, pH 7.9, at 25°C
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0.03
-
enzyme from glucose-grown cells, at pH 7.9 and 55°C
0.4
-
enzyme from oxalate-grown cells, at pH 7.9 and 55°C
0.6
-
using benzyl viologen as a cosubstrate, in 50 mM Tris-HCl (pH 8.5), at 37°C
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-
-
-
brenda
-
UniProt
brenda
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-
-
brenda
-
-
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
-
A0A645HGT5_9ZZZZ
130
0
15151
TrEMBL
other Location (Reliability: 2 )
A0A6I5ZLM0_9THEO
315
0
34004
TrEMBL
-
A0A1D7XBQ9_MOOTH
314
0
34234
TrEMBL
-
A0A6I5ZPV4_9THEO
290
0
31465
TrEMBL
-
A0A5D3I6V0_MOOTH
391
0
42208
TrEMBL
-
A0A2H5V648_9ARCH
307
0
34340
TrEMBL
-
A0A6I5ZMM3_9THEO
271
0
28688
TrEMBL
-
A0A162MWI8_9FIRM
395
0
43896
TrEMBL
-
A0A6M4H3P2_9PROT
330
0
35674
TrEMBL
-
A0A6I5ZNB3_9THEO
391
0
43057
TrEMBL
-
A0A2H5ZTK4_9BACT
332
0
36718
TrEMBL
-
A0A644T4C3_9ZZZZ
289
0
31274
TrEMBL
other Location (Reliability: 2 )
A0A2H5ZSN6_9BACT
407
0
45647
TrEMBL
-
A0A645ISU2_9ZZZZ
73
0
8913
TrEMBL
other Location (Reliability: 1 )
A0A533QS60_9PROT
216
0
23405
TrEMBL
-
A0A140LCW9_9FIRM
315
0
34064
TrEMBL
-
A0A5D3IGM6_MOOTH
395
0
43715
TrEMBL
-
A0A2H5WJK3_9BACT
400
0
44288
TrEMBL
-
A0A517DQL7_9FIRM
230
0
24727
TrEMBL
-
A0A644U1D7_9ZZZZ
296
0
31897
TrEMBL
other Location (Reliability: 3 )
A0A1V0RS48_9RHOB
651
0
68661
TrEMBL
-
A0A161QDH4_9FIRM
312
0
34057
TrEMBL
-
A0A645B1H7_9ZZZZ
354
0
38523
TrEMBL
other Location (Reliability: 2 )
A0A140LCX1_9FIRM
314
0
34303
TrEMBL
-
A0A1D7XBP3_MOOTH
315
0
33931
TrEMBL
-
A0A140LCX0_9FIRM
395
0
43861
TrEMBL
-
A0A6I5ZM46_9THEO
395
0
43820
TrEMBL
-
A0A517DQM1_9FIRM
414
0
45312
TrEMBL
-
A0A162MWI5_9FIRM
315
0
33921
TrEMBL
-
A0A223Z084_9EURY
288
0
31594
TrEMBL
-
A0A517DQW2_9FIRM
320
0
34770
TrEMBL
-
A0A2R8BYB1_9RHOB
658
0
69566
TrEMBL
-
A0A644U6R9_9ZZZZ
296
0
32191
TrEMBL
other Location (Reliability: 1 )
A0A6I5ZLH2_9THEO
314
0
34169
TrEMBL
-
A0A2H5ZTW4_9BACT
392
0
44326
TrEMBL
-
A0A6H2H623_9BURK
700
0
74935
TrEMBL
-
A0A517DQL8_9FIRM
96
0
10623
TrEMBL
-
A0A2H5ZSK8_9BACT
392
0
44579
TrEMBL
-
A0A645IT55_9ZZZZ
120
0
14100
TrEMBL
other Location (Reliability: 2 )
A0A644ST03_9ZZZZ
313
0
34521
TrEMBL
other Location (Reliability: 4 )
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226900
-
analytical ultracentrifugation
32000
-
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
-
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
-
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
-
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
-
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
-
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
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heterotrimer
-
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
heterotrimer
-
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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1.2.7.10 oxalate oxidoreductase
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