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Information on EC 1.5.7.2 - coenzyme F420 oxidoreductase (ferredoxin) and Organism(s) Methanosarcina mazei and UniProt Accession Q8PZ67

for references in articles please use BRENDA:EC1.5.7.2
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EC Tree
IUBMB Comments
The enzyme from the archaeon Methanosarcina mazei contains iron-sulfur centres and FAD.
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Methanosarcina mazei
UNIPROT: Q8PZ67
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The taxonomic range for the selected organisms is: Methanosarcina mazei
The expected taxonomic range for this enzyme is: Methanosarcinales
Synonyms
fpof protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fd:F420 oxidoreductase
-
cofactor F420-dependent FPO
-
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F420H2:phenazine oxidoreductase
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-
SYSTEMATIC NAME
IUBMB Comments
coenzyme F420:ferredoxin oxidoreductase
The enzyme from the archaeon Methanosarcina mazei contains iron-sulfur centres and FAD.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
show the reaction diagram
reduced coenzyme F420 + 2 oxidized ferredoxin
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
-
-
r
methanophenazine + reduced F420 + 2 H+
reduced methanophenazine + oxidized F420
show the reaction diagram
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-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
reduced coenzyme F420 + 2 oxidized ferredoxin
show the reaction diagram
FpoF can function as an ferredoxin:F420 oxidoreductase when reduced ferredoxin accumulates in the cytoplasm. As a soluble single subunit it is involved in the reoxidation of reduced ferredoxin in the cytoplasm, whereby reduced F420 is produced that is then reoxidized by the complete Fpo complex
-
-
r
reduced coenzyme F420 + 2 oxidized ferredoxin
oxidized coenzyme F420 + 2 reduced ferredoxin + 2 H+
show the reaction diagram
when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
-
-
r
methanophenazine + reduced F420 + 2 H+
reduced methanophenazine + oxidized F420
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
presence of 1.0 mol FAD per mol protein
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Iron-sulfur cluster
presence of two FeS clusters, 8.7 mol of nonheme iron and 5.1 mol of acid-labile sulfur per mol of protein
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.002
oxidized coenzyme F420
pH 7.0, temperature not specified in the publication
0.0005
reduced ferredoxin
pH 7.0, temperature not specified in the publication
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
as a soluble single subunit it is involved in the reoxidation of reduced ferredoxin in the cytoplasm, whereby reduced F420 is produced that is then reoxidized by the complete Fpo complex
Manually annotated by BRENDA team
when the Fpo protein is connected to the membrane integral Fpo complex, it functions as an electron input module of the Fpo complex
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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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, S° 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
physiological function
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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
additional information
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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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli DH5alpha
phylogenetic tree
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Welte, C.; Deppenmeier, U.
Re-evaluation of the function of the F420 dehydrogenase in electron transport of Methanosarcina mazei
FEBS J.
278
1277-1287
2011
Methanosarcina mazei (Q8PZ67), Methanosarcina mazei DSM 3647 (Q8PZ67)
Manually annotated by BRENDA team
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
Biochim. Biophys. Acta
1857
958-970
2016
Methanosarcina mazei, Methanothrix thermoacetophila
Manually annotated by BRENDA team