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Information on EC 1.18.1.2 - ferredoxin-NADP+ reductase and Organism(s) Nostoc sp. and UniProt Accession P21890

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EC Tree
IUBMB Comments
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.
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This record set is specific for:
Nostoc sp.
UNIPROT: P21890
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The taxonomic range for the selected organisms is: Nostoc sp.
The enzyme appears in selected viruses and cellular organisms
Synonyms
nitrite reductase, adrenodoxin reductase, ferric reductase, ferredoxin-nadp+ reductase, ferredoxin-nadp reductase, ferredoxin-nadp(+) reductase, ferredoxin-nadp+ oxidoreductase, flavodoxin reductase, ferredoxin:nadp+ oxidoreductase, ferredoxin:nadp+ reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
adrenodoxin reductase
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DA1
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ferredoxin-NADP oxidoreductase
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ferredoxin-NADP reductase
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-
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Ferredoxin-NADP(+) reductase
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ferredoxin-NADP-oxidoreductase
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ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase
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ferredoxin-TPN reductase
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ferredoxin:NADP+ oxidoreductase
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Flavodoxin reductase
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FLDR
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-
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FLXR
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-
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FNR
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-
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NADP:ferredoxin oxidoreductase
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NADPH:ferredoxin oxidoreductase
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-
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NFR
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reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase
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reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate
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TPNH-ferredoxin reductase
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
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-, -
SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NADP+ oxidoreductase
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.
CAS REGISTRY NUMBER
COMMENTARY hide
56367-57-8
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9029-33-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
additional information
?
-
no changes are found in the kinetics of reduction of the FMN cofactor of flavodoxin modified by glycine ethyl ester as compared with the native protein (reaction of EC 1.19.1.1). The observed rate constants for reoxidation of ferredoxin by FNR are about 100fold decreased when phenylglyoxal-modified FNR is used
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
reduction of the FAD moiety of phenylglyoxal-modified FNR by laser-generated 5-deazariboflavin semiquinone occurrs with a second-order rate constant 2.5fold smaller than that obtained for reduction of native FNR
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31500
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strain MAC, sedimentation equilibrium
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a multiscale modelling approach for analysis of the electron transfer process in complexes of the enzyme with both ferredoxin and flavodoxin, reactions of EC 1.19.1.1 and EC1.18.1.2, respectively. The electron transfer in FNR/ferredoxin proceedes through a bridge-mediated mechanism in a dominant protein-protein complex, where transfer of the electron is facilitated by ferredoxin loop-residues 40-49. In FNR/flavodoxin, a direct transfer between redox cofactors is observed and less complex specificity than in ferredoxin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Nicotiana tabacum
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
design of an in vivo system to optimize flavodoxin reduction and NADP+ regeneration under stress using a version of cyanobacterial ferredoxin–NADP+ reductase without the thylakoid-binding domain. Co-expression of the two soluble flavoproteins in the chloroplast stroma of Nicotiana tabacum results in lines displaying maximal tolerance to redox-cycling oxidants, lower damage and decreased reactive oxygen species accumulation
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hutber, G.N.; Smith, A.J.; Rogers, L.J.
Isolation of ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase from a prokaryote
Biochem. Soc. Trans.
6
1214-1216
1978
Nostoc sp., Nostoc sp. MAC
Manually annotated by BRENDA team
Giro, M.; Ceccoli, R.D.; Poli, H.O.; Carrillo, N.; Lodeyro, A.F.
An in vivo system involving co-expression of cyanobacterial flavodoxin and ferredoxin-NADP(+) reductase confers increased tolerance to oxidative stress in plants
FEBS open bio
1
7-13
2011
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
Manually annotated by BRENDA team
Saen-Oon, S.; Cabeza De Vaca, I.; Masone, D.; Medina, M.; Guallar, V.
A theoretical multiscale treatment of protein-protein electron transfer: The ferredoxin/ferredoxin-NADP+ reductase and flavodoxin/ferredoxin-NADP+ reductase systems
Biochim. Biophys. Acta
1847
1530-1538
2015
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
Manually annotated by BRENDA team
Medina, M.; Gomez-Moreno, C.; Tollin, G.
Effects of chemical modification of Anabaena flavodoxin and ferredoxin-NADP+ reductase on the kinetics of interprotein electron transfer reactions
Eur. J. Biochem.
210
577-583
1992
Nostoc sp. (P21890), Nostoc sp. ATCC 29151 (P21890)
Manually annotated by BRENDA team