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Literature summary for 1.2.7.1 extracted from

  • Kletzin, A.; Adams, M.W.W.
    Molecular and phylogenetic chararcterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritima (1996), J. Bacteriol., 178, 248-257.
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus Q51804 and Q51805 and Q51803 and Q51799 Q51804 i.e. subunit PorA, Q51805 i.e. subunit PorB, Q51803 i.e. subunit PorD, Q51799 i.e. subunit PorG
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Thermotoga maritima O05651 and Q56317 and O05650 and Q56316 O05651 i.e. subunit PorA, Q56317 i.e. subunit PorB, O05650 i.e. subunit PorC, Q56316 i.e. subunit PorD
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Thermotoga maritima DSM 3109 O05651 and Q56317 and O05650 and Q56316 O05651 i.e. subunit PorA, Q56317 i.e. subunit PorB, O05650 i.e. subunit PorC, Q56316 i.e. subunit PorD
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Cofactor

Cofactor Comment Organism Structure
thiamine diphosphate the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain Thermotoga maritima
thiamine diphosphate the beta subunit contains four conserved cysteines in addition to a thiamine diphosphate-binding domain Pyrococcus furiosus
[4Fe-4S]-center the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP Thermotoga maritima
[4Fe-4S]-center the delta subunit contains two ferredoxin-type [4Fe-4S] cluster binding motifs, CXXCXXCXXXCP Pyrococcus furiosus

Expression

Organism Comment Expression
Pyrococcus furiosus the operon organization for Pyrococcus furiosus pyruvate ferredoxin oxidoreductase POR and 2-oxoisovalerate ferredoxin oxidoreductase VOR is porG-vorDAB-porDAB, wherein the gamma subunit is shared by the two enzymes additional information