MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion TypeSimple ReactionsChemical ReactionsProtein-Modification Reactions
Reactions Classified By SubstrateMacromolecule ReactionsProtein-ReactionsProtein-Modification Reactions

EC Number:

Enzymes and Genes:

Clostridium acetobutylicum: NADPH-ferredoxin oxidoreductaseInferred from experiment
Escherichia coli K-12 substr. MG1655: flavodoxin NADP+ reductaseInferred from experiment: fpr
Saccharomyces cerevisiae: adrenodoxin oxidoreductaseInferred from experiment: ARH1
Synechococcus elongatus PCC 7942: ferredoxin-NADP oxidoreductaseInferred by computational analysis: petH

Supersedes EC numbers:,

Note that this reaction equation differs from the official Enzyme Commission reaction equation for this EC number, which can be found here .

The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name: ferredoxin—NADP+ reductase

Enzyme Commission Synonyms: ferredoxin-nicotinamide adenine dinucleotide phosphate reductase, ferredoxin-NADP+ reductase, TPNH-ferredoxin reductase, ferredoxin-NADP+ oxidoreductase, NADP+:ferredoxin oxidoreductase, ferredoxin-TPN reductase, ferredoxin-NADP+-oxidoreductase, NADPH:ferredoxin oxidoreductase, ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase

Taxonomic Range: Archaea, Viridiplantae, Bacteria

Standard Gibbs Free Energy (ΔrG in kcal/mol): -37.261536Inferred by computational analysis [Latendresse13]

A flavoprotein. Can also reduce flavodoxin.

Enzyme Commission Summary:
A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] ferredoxins and flavodoxin.

Citations: [Shin63, Knaff91, Karplus91, Morales00]

Gene-Reaction Schematic

Gene-Reaction Schematic

Relationship Links: BRENDA:EC:, ENZYME:EC:, IUBMB-ExplorEnz:EC:, UniProt:RELATED-TO:O04397, UniProt:RELATED-TO:O04977, UniProt:RELATED-TO:O23877, UniProt:RELATED-TO:O59710, UniProt:RELATED-TO:O65206, UniProt:RELATED-TO:O65208, UniProt:RELATED-TO:P00454, UniProt:RELATED-TO:P00455, UniProt:RELATED-TO:P08165, UniProt:RELATED-TO:P10933, UniProt:RELATED-TO:P22570, UniProt:RELATED-TO:P24134, UniProt:RELATED-TO:P28861, UniProt:RELATED-TO:P41343, UniProt:RELATED-TO:P41344, UniProt:RELATED-TO:P41345, UniProt:RELATED-TO:P48360, UniProt:RELATED-TO:P53991, UniProt:RELATED-TO:Q7M1R4, UniProt:RELATED-TO:Q7M1S9, UniProt:RELATED-TO:Q7M1T0, UniProt:RELATED-TO:Q9JRE3, UniProt:RELATED-TO:Q00598, UniProt:RELATED-TO:Q41641, UniProt:RELATED-TO:Q41736, UniProt:RELATED-TO:Q44532, UniProt:RELATED-TO:Q55318, UniProt:RELATED-TO:Q61578


Karplus91: Karplus PA, Daniels MJ, Herriott JR (1991). "Atomic structure of ferredoxin-NADP+ reductase: prototype for a structurally novel flavoenzyme family." Science 251(4989);60-6. PMID: 1986412

Knaff91: Knaff DB, Hirasawa M (1991). "Ferredoxin-dependent chloroplast enzymes." Biochim Biophys Acta 1056(2);93-125. PMID: 1671559

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Morales00: Morales R, Charon MH, Kachalova G, Serre L, Medina M, Gomez-Moreno C, Frey M (2000). "A redox-dependent interaction between two electron-transfer partners involved in photosynthesis." EMBO Rep 1(3);271-6. PMID: 11256611

Shin63: Shin M, Tagawa K, Arnon DI (1963). "Crystallization of ferredoxin-TPN reductase and its role in the photosynthetic apparatus of chloroplasts." Biochem Z 338;84-96. PMID: 14087348

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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