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Literature summary extracted from

  • Mulo, P.
    Chloroplast-targeted ferredoxin-NADP+ oxidoreductase (FNR): Structure, function and location (2010), Biochim. Biophys. Acta, 1807, 927-934.
    View publication on PubMed

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.18.1.2 chloroplast isozyme FNRI is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview Arabidopsis thaliana 9507
-
1.18.1.2 chloroplast isozyme FNRII is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview Arabidopsis thaliana 9507
-
1.18.1.2 chloroplast the enzyme is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview Triticum aestivum 9507
-
1.18.1.2 chloroplast the enzyme is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview Zea mays 9507
-
1.18.1.2 soluble
-
 Zea mays
-
-
1.18.1.2 thylakoid membrane
-
 Zea mays 42651
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 2 reduced ferredoxin + NADP+ Triticum aestivum
-
 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 2 reduced ferredoxin + NADP+ Arabidopsis thaliana
-
 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 2 reduced ferredoxin + NADP+ Zea mays
-
 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 additional information Triticum aestivum FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes ?
-
 ?
1.18.1.2 additional information Arabidopsis thaliana FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes ?
-
 ?
1.18.1.2 additional information Zea mays FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Arabidopsis thaliana F4JZ46 isozyme FNRII; plastidic isozyme FNRII, gene FNR1
-
1.18.1.2 Arabidopsis thaliana Q8W493 isozyme FNRI; plastidic isozyme FNRI, gene FNR2
-
1.18.1.2 Triticum aestivum Q8RVZ8 isozyme FNRI; isozyme FNRI, gene FNRI or FNR-B
-
1.18.1.2 Triticum aestivum Q8RVZ9 isozyme FNRII; isozyme FNRII, gene FNRII
-
1.18.1.2 Zea mays Q9SLP6 isozyme FNRI; isozyme FNRI, gene L-FNRI or FNR1
-
1.18.1.2 Zea mays Q9SLP6 isozyme FNRII; isozyme FNRII, gene L-FNRII or FNR2
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.18.1.2 leaf
-
 Zea mays
-
1.18.1.2 leaf four distinct leaf FNR isoforms, two in each group, FNRI and FNRII Triticum aestivum
-
1.18.1.2 additional information only minor amount of chloroplast isozyme FNR mRNA are detected in the stems, flowers and siliques. Chloroplast FNR transcripts or FNR proteins are not detected in the root tissue Arabidopsis thaliana
-
1.18.1.2 additional information only minor amount of chloroplast isozyme FNR1 mRNA are detected in the stems, flowers and siliques. Chloroplast FNR transcripts or FNR proteins are not detected in the root tissue Arabidopsis thaliana
-
1.18.1.2 rosette leaf both FNR chloroplast isozyme genes are predominantly expressed in the rosette leaves Arabidopsis thaliana
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 2 reduced ferredoxin + NADP+
-
 Triticum aestivum 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 2 reduced ferredoxin + NADP+
-
 Arabidopsis thaliana 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 2 reduced ferredoxin + NADP+
-
 Zea mays 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 2 reduced ferredoxin + NADP+ FNR C-terminal domain harbors the NADP+ binding site Triticum aestivum 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 2 reduced ferredoxin + NADP+ FNR C-terminal domain harbors the NADP+ binding site Arabidopsis thaliana 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 2 reduced ferredoxin + NADP+ FNR C-terminal domain harbors the NADP+ binding site Zea mays 2 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 additional information FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes Triticum aestivum ?
-
 ?
1.18.1.2 additional information FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes Arabidopsis thaliana ?
-
 ?
1.18.1.2 additional information FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes Zea mays ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.18.1.2 More chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview Triticum aestivum
1.18.1.2 More chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview Arabidopsis thaliana
1.18.1.2 More chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview Zea mays

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin-NADP+ oxidoreductase
-
 Triticum aestivum
1.18.1.2 ferredoxin-NADP+ oxidoreductase
-
 Arabidopsis thaliana
1.18.1.2 ferredoxin-NADP+ oxidoreductase
-
 Zea mays
1.18.1.2 FNR
-
 Triticum aestivum
1.18.1.2 FNR
-
 Arabidopsis thaliana
1.18.1.2 FNR
-
 Zea mays

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding Triticum aestivum
1.18.1.2 FAD FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding Arabidopsis thaliana
1.18.1.2 FAD FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding Zea mays

pI Value

EC Number Organism Comment pI Value Maximum pI Value
1.18.1.2 Triticum aestivum isozyme FNRII 5.5 5.3
1.18.1.2 Zea mays isozyme FNRI
-
 5.5
1.18.1.2 Arabidopsis thaliana mature FNRII
-
 5.54
1.18.1.2 Triticum aestivum isozyme FNRI 6.2 5.9
1.18.1.2 Arabidopsis thaliana mature FNRI
-
 6.19
1.18.1.2 Zea mays isozyme FNRI
-
 6.76

General Information

EC Number General Information Comment Organism
1.18.1.2 metabolism FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways Triticum aestivum
1.18.1.2 metabolism FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways Arabidopsis thaliana
1.18.1.2 metabolism FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways Zea mays
1.18.1.2 additional information chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants Triticum aestivum
1.18.1.2 additional information chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants Zea mays
1.18.1.2 additional information chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants. Inactivation of one chloroplast FNR isoform does not result in upregulation of the expression of the other isozyme, neither at the level of transcription nor translation, but results in general downregulation of the photosynthetic machinery Arabidopsis thaliana