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MetaCyc Reaction: 1.18.1.2

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions Protein-Modification Reactions
Reactions Classified By Substrate Macromolecule Reactions Protein-Reactions Protein-Modification Reactions

EC Number: 1.18.1.2

Enzymes and Genes:

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

Supersedes EC numbers: 1.6.99.4, 1.6.7.1

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

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. 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): -37.261536 Inferred by computational analysis [Latendresse13]

Summary:
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:1.18.1.2 , ENZYME:EC:1.18.1.2 , IUBMB-ExplorEnz:EC:1.18.1.2 , 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


References

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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