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Literature summary for 1.18.1.2 extracted from

  • Moolna, A.; Bowsher, C.G.
    The physiological importance of photosynthetic ferredoxin NADP+ oxidoreductase (FNR) isoforms in wheat (2010), J. Exp. Bot., 61, 2669-2681.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast subchloroplast localization of pFNR isoforms, overview. Isozyme FNRI with subforms pFNRISKKQ and pFNRIKKVS shows a differential distribution between stroma and thylakoid with 76% of pFNRISKKQ and only 33% of pFNRIKKVS located in the thylakoid pool Triticum aestivum 9507
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chloroplast subchloroplast localization of pFNR isoforms, overview. Isozyme FNRII with subforms pFNRIIISKK and pFNRIIKKQD shows an eual distribution between stroma and thylakoid Triticum aestivum 9507
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 reduced ferredoxin + NADP+ Triticum aestivum
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2 oxidized ferredoxin + NADPH + H+
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r
2 reduced ferredoxin + NADP+ Triticum aestivum Paragon
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2 oxidized ferredoxin + NADPH + H+
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r

Organism

Organism UniProt Comment Textmining
Triticum aestivum Q8RVZ8 isozyme FNRI with subforms pFNRISKKQ and pFNRIKKVS; four photosynthetic pFNR protein isoforms
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Triticum aestivum Q8RVZ9 isozyme FNRII with subforms pFNRIIISKK and pFNRIIKKQD; four photosynthetic pFNR protein isoforms
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Triticum aestivum Paragon Q8RVZ8 isozyme FNRI with subforms pFNRISKKQ and pFNRIKKVS; four photosynthetic pFNR protein isoforms
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Triticum aestivum Paragon Q8RVZ9 isozyme FNRII with subforms pFNRIIISKK and pFNRIIKKQD; four photosynthetic pFNR protein isoforms
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the four pFNR protein isoforms are each present in the chloroplast in phosphorylated and nonphosphorylated states. The pFNR isoforms vary in putative phosphorylation responses to physiological parameters, prediction of phosphorylation sites, e.g. S75, and differences between isoforms in putative phosphorylation patterns, overview Triticum aestivum
phosphoprotein the four pFNR protein isoforms are each present in the chloroplast in phosphorylated and nonphosphorylated states. The pFNR isoforms vary in putative phosphorylation responses to physiological parameters, prediction of phosphorylation sites, e.g. T104 and T293, and differences between isoforms in putative phosphorylation patterns, overview Triticum aestivum

Source Tissue

Source Tissue Comment Organism Textmining
leaf primary wheat leaf Triticum aestivum
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 reduced ferredoxin + NADP+
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Triticum aestivum 2 oxidized ferredoxin + NADPH + H+
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r
2 reduced ferredoxin + NADP+
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Triticum aestivum Paragon 2 oxidized ferredoxin + NADPH + H+
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r

Subunits

Subunits Comment Organism
More three-dimensional modelling of pFNR protein structure, overview Triticum aestivum

Synonyms

Synonyms Comment Organism
ferredoxin NADP+ oxidoreductase
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Triticum aestivum
FNR
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Triticum aestivum
pFNR
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Triticum aestivum
photosynthetic ferredoxin NADP+ oxidoreductase
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Triticum aestivum
photosynthetic FNR
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Triticum aestivum

pI Value

Organism Comment pI Value Maximum pI Value
Triticum aestivum isoelectric focusing of isozymes, overview
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additional information

General Information

General Information Comment Organism
physiological function the photosynthetic FNRs may be crucial to the regulation of reductant partition between carbon fixation and other metabolic pathways. The alternative N-terminal pFNRI and pFNRII protein isoforms have statistically significant differences in response to the physiological parameters of chloroplast maturity, nitrogen regime, and oxidative stress, overview Triticum aestivum