Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.18.1.2 - ferredoxin-NADP+ reductase and Organism(s) Synechocystis sp. and UniProt Accession Q55318

for references in articles please use BRENDA:EC1.18.1.2
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Synechocystis sp.
UNIPROT: Q55318
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Synechocystis 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
-
-
-
-
DA1
-
-
-
-
ferredoxin-NADP oxidoreductase
-
-
-
-
ferredoxin-NADP reductase
-
-
-
-
Ferredoxin-NADP(+) reductase
-
-
-
-
ferredoxin-NADP+ oxidoreductase
-
-
ferredoxin-NADP-oxidoreductase
-
-
-
-
ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase
-
-
-
-
ferredoxin-TPN reductase
-
-
-
-
ferredoxin:NADP+ oxidoreductase
Flavodoxin reductase
-
-
-
-
FLDR
-
-
-
-
FLXR
-
-
-
-
NADP:ferredoxin oxidoreductase
-
-
-
-
NADPH:ferredoxin oxidoreductase
-
-
-
-
NFR
-
-
-
-
reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase
-
-
-
-
reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate
-
-
-
-
TPNH-ferredoxin reductase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
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
-
9029-33-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 ferricyanide + NADPH
2 ferrocyanide + NADP+ + H+
show the reaction diagram
-
-
-
?
2 ferricytochrome c2 + NADPH
2 ferrocytochrome c2 + NADP+ + H+
show the reaction diagram
-
-
-
?
FAD + NADPH + H+
reduced FAD + NADP+
show the reaction diagram
-
-
-
?
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
show the reaction diagram
-
-
-
?
FMN + NADPH + H+
reduced FMN + NADP+
show the reaction diagram
-
-
-
?
oxidized 2,6-dichlorophenolindophenol + NADPH + H+
reduced 2,6-dichlorophenolindophenol + NADP+
show the reaction diagram
-
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
-
-
-
-
r
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone + NADP+ + H+
oxidized 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferricyanide + NADP+ + H+
ferrocyanide + NADPH
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH + H+
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme is involved in the electron transfer cascade from photosystem I to NADP+, formation of a ternary complex between photosystem I, ferredoxin, and enzyme
-
-
r
reduced ferredoxin + NADP+ + H+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
and FMN, ratio of FAD to FMN is 7.5 to 1
FMN
and FAD, ratio of FAD to FMN is 7.5 to 1
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
low CO2 enhances the expression and activity of FNR and the cyclic photosystem I mediated by FNR
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.46
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
at pH 7.5 and 22°C
-
0.0074
reduced ferricyanide
-
at pH 8.7 and 22°C
additional information
additional information
-
detailed binding kinetics, detailed reaction kinetics, enzyme-substrate complex formation
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.43
reduced 2,5-dibromo-3-methyl-6-isopropyl-p-benzoquinone
-
at pH 7.5 and 22°C
-
0.43
reduced ferricyanide
-
at pH 8.7 and 22°C
additional information
additional information
-
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.31
substrate Fe(III)-EDTA, pH 7.0, 25°C
0.39
substrate ferricytochrome c, pH 7.0, 25°C
35.27
substrate 2,6-dichlorophenolindophenol, pH 7.0, 25°C
35.28
substrate ferricyanide, pH 7.0, 25°C
5.92
substrate FMN, pH 7.0, 25°C
6
substrate FAD, pH 7.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
high- or low-CO2-grown (H or L)-cells
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
the petH gene encoding ferredoxin:NADP+ oxidoreductase has two translation products depending on growth conditions and leading to two isoforms. Under standard conditions where FNRL accumulates, two transcriptional start points are found at -52 and -34 relative to the first translation start site. Under nitrogen-starvation conditions where FNRS accumulates a transcriptional start point is mapped at -126 relative to the first translation start site. Therefore, the transcript responsible for FNRS translation is longer than that producing FNRL
physiological function
-
FNR catalyzes the final step of the linear photosynthetic electron flow by mediating the electron transfer from reduced ferredoxin to NADP+ with formation of NADPH for CO2 assimilation or other biosynthetic pathways. This process is a rate-limiting step of photosynthesis under both limiting and saturating light conditions. FNR is also involved in the cyclic electron flow around photosystem I, cyclic PSI, by its photoproduct NADPH recycling to plastoquinone or the cytochrome b6f complex. Analysis of contribution of FNR and NDH-1 to cyclic PSI under low CO2 conditions, overview
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
34000
46000
x * 34000, isoform FNRS, x * 46000, isoform FNRL
60000
gel filtration
34000
-
x * 38000, recombinant N-terminally truncated enzyme, SDS-PAGE, 1 * 34000, chloroplast enzyme form, SDS-PAGE
38000
-
x * 38000, recombinant N-terminally truncated enzyme, SDS-PAGE, 1 * 34000, chloroplast enzyme form, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 34000, isoform FNRS, x * 46000, isoform FNRL
dimer
2 * 34000, SDS-PAGE
?
-
x * 38000, recombinant N-terminally truncated enzyme, SDS-PAGE, 1 * 34000, chloroplast enzyme form, SDS-PAGE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression of N-terminally truncated gene petH
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the petH gene encoding ferredoxin:NADP+ oxidoreductase has two translation products depending on growth conditions and leading to two isoforms. Under standard conditions where FNRL accumulates, two transcriptional start points are found at -52 and -34 relative to the first translation start site. Under nitrogen-starvation conditions where FNRS accumulates a transcriptional start point is mapped at -126 relative to the first translation start site. Therefore, the transcript responsible for FNRS translation is longer than that producing FNRL
low CO2 enhances the expression and activity of FNR and the cyclic photosystem I mediated by FNR
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cassan, N.; Lagoutte, B.; Setif, P.
Ferredoxin-NADP+ reductase. Kinetics of electron transfer, transient intermediates, and catalytic activities studied by flash-absorption spectroscopy with isolated photosystem I and ferredoxin
J. Biol. Chem.
280
25960-25972
2005
Synechocystis sp.
Manually annotated by BRENDA team
Thomas, J.C.; Ughy, B.; Lagoutte, B.; Ajlani, G.
A second isoform of the ferredoxin:NADP oxidoreductase generated by an in-frame initiation of translation
Proc. Natl. Acad. Sci. USA
103
18368-18373
2006
Synechocystis sp. (Q55318), Synechocystis sp.
Manually annotated by BRENDA team
Liu, Y.; Ma, W.; Mi, H.
Increase of the expression and activity of ferredoxin-NADP+ oxidoreductase in the cells adapted to low CO2 in the cyanobacterium Synechocystis 6803
Photosynthetica
48
417-420
2010
Synechocystis sp.
-
Manually annotated by BRENDA team
Sato, J.; Takeda, K.; Nishiyama, R.; Watanabe, T.; Abo, M.; Yoshimura, E.; Nakagawa, J.; Abe, A.; Kawasaki, S.; Niimura, Y.
Synechocystis ferredoxin-NADP+ oxidoreductase is capable of functioning as ferric reductase and of driving the Fenton reaction in the absence or presence of free flavin
Biometals
24
311-321
2011
Synechocystis sp. (Q55318), Synechocystis sp.
Manually annotated by BRENDA team
Omairi-Nasser, A.; de Gracia, A.G.; Ajlani, G.
A larger transcript is required for the synthesis of the smaller isoform of ferredoxin:NADP oxidoreductase
Mol. Microbiol.
81
1178-1189
2011
Synechocystis sp. (Q55318), Synechocystis sp.
Manually annotated by BRENDA team
Szczepaniak, K.; Worch, R.; Grzyb, J.
Ferredoxin NADP+ oxidoreductase in junction with CdSe/ZnS quantum dots Characteristics of an enzymatically active nanohybrid
J. Phys. Condens. Matter
25
194162
2013
Synechocystis sp.
Manually annotated by BRENDA team