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Literature summary extracted from

  • Nohara, K.; Orita, I.; Nakamura, S.; Imanaka, T.; Fukui, T.
    Genetic examination and mass balance analysis of pyruvate/amino acid oxidation pathways in the hyperthermophilic archaeon Thermococcus kodakarensis (2014), J. Bacteriol., 196, 3831-3839.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.2.7.7 3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin Thermococcus kodakarensis
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S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin + H+
-
?
1.2.7.7 3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin Thermococcus kodakarensis KUW1
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S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin + H+
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.1 Thermococcus kodakarensis Q5JIJ8 and Q5JIJ7 and Q5JIJ6 Q5JIJ8 i.e. delta subunit, Q5JIJ7 i.e. alpha subunit, Q5JIJ6 i.e. beta subunit
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1.2.7.7 Thermococcus kodakarensis
-
-
-
1.2.7.7 Thermococcus kodakarensis KUW1
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.7 3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin
-
Thermococcus kodakarensis S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin + H+
-
?
1.2.7.7 3-methyl-2-oxobutanoate + CoA + oxidized ferredoxin
-
Thermococcus kodakarensis KUW1 S-(2-methylpropanoyl)-CoA + CO2 + reduced ferredoxin + H+
-
?

Synonyms

EC Number Synonyms Comment Organism
1.2.7.7 2-oxoisovalerate:ferredoxin oxidoreductase
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Thermococcus kodakarensis
1.2.7.7 VOR
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Thermococcus kodakarensis

General Information

EC Number General Information Comment Organism
1.2.7.1 physiological function in a cytosolic hydrogenase-deficient strain, pyruvate:ferredoxin oxidoreductase POR and 2-oxoisovalerate:ferredoxin oxidoreductase VOR specifically function in oxidation of pyruvate and branched-chain amino acids, respectively, and the lack of POR or VOR is compensated for by promoting the oxidation of another substrate driven by the remaining oxidoreductase Thermococcus kodakarensis