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Literature summary extracted from

  • Schut, G.; Zadvornyy, O.; Wu, C.; Peters, J.; Boyd, E.; Adams, M.
    The role of geochemistry and energetics in the evolution of modern respiratory complexes from a proton-reducing ancestor (2016), Biochim. Biophys. Acta, 1857, 958-970 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.5.7.2 phylogenetic tree Methanosarcina mazei
1.5.7.2 phylogenetic tree Methanothrix thermoacetophila

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.5.7.2 membrane
-
Methanosarcina mazei 16020
-
1.5.7.2 membrane
-
Methanothrix thermoacetophila 16020
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.5.7.2 methanophenazine + reduced F420 + 2 H+ Methanosarcina mazei
-
reduced methanophenazine + oxidized F420
-
?
1.5.7.2 methanophenazine + reduced ferredoxin + 2 H+ Methanothrix thermoacetophila
-
reduced methanophenazine + oxidized ferredoxin
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.5.7.2 Methanosarcina mazei
-
-
-
1.5.7.2 Methanothrix thermoacetophila
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.5.7.2 methanophenazine + reduced F420 + 2 H+
-
Methanosarcina mazei reduced methanophenazine + oxidized F420
-
?
1.5.7.2 methanophenazine + reduced ferredoxin + 2 H+
-
Methanothrix thermoacetophila reduced methanophenazine + oxidized ferredoxin
-
?

Synonyms

EC Number Synonyms Comment Organism
1.5.7.2 cofactor F420-dependent FPO
-
Methanosarcina mazei
1.5.7.2 F420H2:phenazine oxidoreductase
-
Methanosarcina mazei
1.5.7.2 F420H2:phenazine oxidoreductase
-
Methanothrix thermoacetophila
1.5.7.2 Fd-dependent FPO
-
Methanothrix thermoacetophila
1.5.7.2 ferredoxin-dependent FPO
-
Methanothrix thermoacetophila
1.5.7.2 FPOC
-
Methanosarcina mazei
1.5.7.2 FPOF
-
Methanothrix thermoacetophila

General Information

EC Number General Information Comment Organism
1.5.7.2 evolution evolutionary trajectory of these oxidoreductases from a proton-reducing ancestral respiratory complex (ARC), overview. The diversification of ARC to membrane-bound hydrogenase (MBH), archaeal respiratory complex (MBX), FPO and eventually NADH quinone oxidoreductase (NUO) was driven by the larger energy yields associated with coupling ferredoxin oxidation to the reduction of oxidants with increasing electrochemical potential, including protons, SĀ° and membrane soluble organic compounds such as phenazines and quinone derivatives. Phylogenetic tree. Homology between the subunits of FPOF and FPOC with those in MBX and MBH. Evolution of FPO, detailed overview. FPO is now present only in strictly anaerobic, acetate-utilizing and sulfate-reducing archaea Methanosarcina mazei
1.5.7.2 evolution evolutionary trajectory of these oxidoreductases from a proton-reducing ancestral respiratory complex (ARC), overview. The diversification of ARC to membrane-bound hydrogenase (MBH), archaeal respiratory complex (MBX), FPO and eventually NADH quinone oxidoreductase (NUO) was driven by the larger energy yields associated with coupling ferredoxin oxidation to the reduction of oxidants with increasing electrochemical potential, including protons, SĀ° and membrane soluble organic compounds such as phenazines and quinone derivatives. Phylogenetic tree. Homology between the subunits of FPOF and FPOC with those in MBX and MBH. Evolution of FPO, detailed overview. FPO is now present only in strictly anaerobic, acetate-utilizing and sulfate-reducing archaea Methanothrix thermoacetophila
1.5.7.2 additional information FPO demonstrates the flexible nature of the ARC-related complexes with respect to electron input and energetics reflected by differences in redox carriers and number of ions translocated Methanosarcina mazei
1.5.7.2 additional information FPO demonstrates the flexible nature of the ARC-related complexes with respect to electron input and energetics reflected by differences in redox carriers and number of ions translocated Methanothrix thermoacetophila
1.5.7.2 physiological function the enzyme is a methanophenzine-reducing subunit of a methanogenic respiratory complex (FPO). These complexes also pump ions and have at least 10 homologous subunits in common. FPO uses either ferredoxin or cofactor F420 Methanosarcina mazei
1.5.7.2 physiological function the enzyme is a methanophenzine-reducing subunit of a methanogenic respiratory complex (FPO). These complexes also pump ions and have at least 10 homologous subunits in common. FPO uses either ferredoxin or cofactor F420. The FPO complex is mainly found in acetate-utilizing, methane-producing anaerobic Archaea where it functions to reduce the membrane-associated cofactor methanophenazine using either ferredoxin or the cytoplasmic cofactor F420 Methanothrix thermoacetophila