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Literature summary extracted from

  • Ceccarelli, E.A.; Arakaki, A.K.; Cortez, N.; Carrillo, N.
    Functional plasticity and catalytic efficiency in plant and bacterial ferredoxin-NADP(H) reductases (2004), Biochim. Biophys. Acta, 1698, 155-165.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information forward and reverse reactions follow different kinetic mechanism, overview Cyanophora paradoxa
1.18.1.2 additional information
-
 additional information forward and reverse reactions follow different kinetic mechanism, overview Chlamydomonas reinhardtii
1.18.1.2 additional information
-
 additional information forward and reverse reactions follow different kinetic mechanism, overview Escherichia coli
1.18.1.2 additional information
-
 additional information forward and reverse reactions follow different kinetic mechanism, overview Spinacia oleracea
1.18.1.2 additional information
-
 additional information forward and reverse reactions follow different kinetic mechanism, overview Rhodobacter capsulatus
1.18.1.2 additional information
-
 additional information forward and reverse reactions follow different kinetic mechanism, overview Azotobacter vinelandii
1.18.1.2 additional information
-
 additional information forward and reverse reactions follow different kinetic mechanism, overview Anabaena sp.
1.18.1.2 additional information
-
 additional information forward and reverse reactions follow different kinetic mechanism, overview Leptospira interrogans

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.18.1.2 chloroplast
-
 Spinacia oleracea 9507
-
1.18.1.2 additional information nucleus-encoded enzyme Cyanophora paradoxa
-
-
1.18.1.2 plastid
-
 Spinacia oleracea 9536
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.18.1.2 additional information Escherichia coli enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview ?
-
 ?
1.18.1.2 additional information Azotobacter vinelandii enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview ?
-
 ?
1.18.1.2 additional information Spinacia oleracea enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview ?
-
 ?
1.18.1.2 additional information Chlamydomonas reinhardtii phylogenetic evolution, relatiionships, and classification, overview ?
-
 ?
1.18.1.2 additional information Rhodobacter capsulatus phylogenetic evolution, relatiionships, and classification, overview ?
-
 ?
1.18.1.2 additional information Leptospira interrogans phylogenetic evolution, relatiionships, and classification, overview ?
-
 ?
1.18.1.2 additional information Cyanophora paradoxa phylogenetic evolution, relationships, and classification, overview ?
-
 ?
1.18.1.2 additional information Anabaena sp. phylogenetic evolution, relationships, and classification, overview ?
-
 ?
1.18.1.2 additional information Anabaena sp. PCC7119 phylogenetic evolution, relationships, and classification, overview ?
-
 ?
1.18.1.2 reduced ferredoxin + NADP+ Cyanophora paradoxa
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Chlamydomonas reinhardtii
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Escherichia coli
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Spinacia oleracea
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Rhodobacter capsulatus
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Azotobacter vinelandii
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Anabaena sp.
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Leptospira interrogans
-
 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ Anabaena sp. PCC7119
-
 oxidized ferredoxin + NADPH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Anabaena sp.
-
 PCC7119
-
1.18.1.2 Anabaena sp. PCC7119
-
 PCC7119
-
1.18.1.2 Azotobacter vinelandii
-
-
-
1.18.1.2 Chlamydomonas reinhardtii
-
-
-
1.18.1.2 Cyanophora paradoxa
-
-
-
1.18.1.2 Escherichia coli
-
-
-
1.18.1.2 Leptospira interrogans
-
 parasitic bacterium
-
1.18.1.2 Rhodobacter capsulatus
-
-
-
1.18.1.2 Spinacia oleracea
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Cyanophora paradoxa
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Chlamydomonas reinhardtii
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Escherichia coli
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Spinacia oleracea
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Rhodobacter capsulatus
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Azotobacter vinelandii
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Anabaena sp.
a
1.18.1.2 2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH catalytic mechanism of forward and reverse reactions Leptospira interrogans
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.18.1.2 leaf
-
 Spinacia oleracea
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.18.1.2 additional information enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview Escherichia coli ?
-
 ?
1.18.1.2 additional information enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview Azotobacter vinelandii ?
-
 ?
1.18.1.2 additional information enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview Spinacia oleracea ?
-
 ?
1.18.1.2 additional information phylogenetic evolution, relatiionships, and classification, overview Chlamydomonas reinhardtii ?
-
 ?
1.18.1.2 additional information phylogenetic evolution, relatiionships, and classification, overview Rhodobacter capsulatus ?
-
 ?
1.18.1.2 additional information phylogenetic evolution, relatiionships, and classification, overview Leptospira interrogans ?
-
 ?
1.18.1.2 additional information phylogenetic evolution, relationships, and classification, overview Cyanophora paradoxa ?
-
 ?
1.18.1.2 additional information phylogenetic evolution, relationships, and classification, overview Anabaena sp. ?
-
 ?
1.18.1.2 additional information phylogenetic evolution, relationships, and classification, overview Anabaena sp. PCC7119 ?
-
 ?
1.18.1.2 NADPH + acceptor diaphorase activity, acceptors can be complexed metals or aromatic molecules Anabaena sp. NADP+ + reduced acceptor
-
 ?
1.18.1.2 NADPH + acceptor diaphorase activity, acceptors can be complexed metals or aromatic molecules Anabaena sp. PCC7119 NADP+ + reduced acceptor
-
 ?
1.18.1.2 reduced ferredoxin + NADP+
-
 Cyanophora paradoxa oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Chlamydomonas reinhardtii oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Escherichia coli oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Spinacia oleracea oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Rhodobacter capsulatus oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Azotobacter vinelandii oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Anabaena sp. oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Leptospira interrogans oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Cyanophora paradoxa oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Chlamydomonas reinhardtii oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Escherichia coli oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Rhodobacter capsulatus oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Azotobacter vinelandii oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Anabaena sp. oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Leptospira interrogans oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ ferredoxin contains a [2Fe2S] cluster and binds to the concave surface of the FAD domain, association of ferredoxin with the enzyme is steered by electrostatic interactions Spinacia oleracea oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Anabaena sp. PCC7119 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+ association of ferredoxin with the enzyme is steered by electrostatic interactions Anabaena sp. PCC7119 oxidized ferredoxin + NADPH
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Chlamydomonas reinhardtii oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Escherichia coli oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Spinacia oleracea oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Azotobacter vinelandii oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Anabaena sp. oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 reduced ferredoxin + NADP+
-
 Anabaena sp. PCC7119 oxidized ferredoxin + NADPH + H+
-
 r
1.18.1.2 reduced flavodoxin + NADP+
-
 Escherichia coli oxidized flavodoxin + NADPH + H+
-
 r

Subunits

EC Number Subunits Comment Organism
1.18.1.2 More 2-domain structure Cyanophora paradoxa
1.18.1.2 More 2-domain structure Chlamydomonas reinhardtii
1.18.1.2 More 2-domain structure Rhodobacter capsulatus
1.18.1.2 More 2-domain structure Leptospira interrogans
1.18.1.2 More 2-domain structure, structure analysis Escherichia coli
1.18.1.2 More 2-domain structure, structure analysis Spinacia oleracea
1.18.1.2 More 2-domain structure, structure analysis Azotobacter vinelandii
1.18.1.2 More 2-domain structure, structure analysis Anabaena sp.

Synonyms

EC Number Synonyms Comment Organism
1.18.1.2 ferredoxin (flavodoxin)-NADP(H) reductase
-
 Cyanophora paradoxa
1.18.1.2 ferredoxin (flavodoxin)-NADP(H) reductase
-
 Chlamydomonas reinhardtii
1.18.1.2 ferredoxin (flavodoxin)-NADP(H) reductase
-
 Escherichia coli
1.18.1.2 ferredoxin (flavodoxin)-NADP(H) reductase
-
 Spinacia oleracea
1.18.1.2 ferredoxin (flavodoxin)-NADP(H) reductase
-
 Rhodobacter capsulatus
1.18.1.2 ferredoxin (flavodoxin)-NADP(H) reductase
-
 Azotobacter vinelandii
1.18.1.2 ferredoxin (flavodoxin)-NADP(H) reductase
-
 Anabaena sp.
1.18.1.2 ferredoxin (flavodoxin)-NADP(H) reductase
-
 Leptospira interrogans
1.18.1.2 ferredoxin-NADP(H) reductase
-
 Cyanophora paradoxa
1.18.1.2 ferredoxin-NADP(H) reductase
-
 Chlamydomonas reinhardtii
1.18.1.2 ferredoxin-NADP(H) reductase
-
 Escherichia coli
1.18.1.2 ferredoxin-NADP(H) reductase
-
 Spinacia oleracea
1.18.1.2 ferredoxin-NADP(H) reductase
-
 Rhodobacter capsulatus
1.18.1.2 ferredoxin-NADP(H) reductase
-
 Azotobacter vinelandii
1.18.1.2 ferredoxin-NADP(H) reductase
-
 Anabaena sp.
1.18.1.2 ferredoxin-NADP(H) reductase
-
 Leptospira interrogans
1.18.1.2 FNR
-
 Cyanophora paradoxa
1.18.1.2 FNR
-
 Chlamydomonas reinhardtii
1.18.1.2 FNR
-
 Escherichia coli
1.18.1.2 FNR
-
 Spinacia oleracea
1.18.1.2 FNR
-
 Rhodobacter capsulatus
1.18.1.2 FNR
-
 Azotobacter vinelandii
1.18.1.2 FNR
-
 Anabaena sp.
1.18.1.2 FNR
-
 Leptospira interrogans
1.18.1.2 More enzyme belongs more to the plant-type enzyme family than to the bacterial-type enzyme family Cyanophora paradoxa
1.18.1.2 More enzyme belongs to the bacterial-type enzyme family Escherichia coli
1.18.1.2 More enzyme belongs to the bacterial-type enzyme family Azotobacter vinelandii
1.18.1.2 More enzyme belongs to the plant-type enzyme family Chlamydomonas reinhardtii
1.18.1.2 More enzyme belongs to the plant-type enzyme family Spinacia oleracea
1.18.1.2 More enzyme belongs to the plant-type enzyme family Rhodobacter capsulatus
1.18.1.2 More enzyme belongs to the plant-type enzyme family Anabaena sp.
1.18.1.2 More enzyme belongs to the plant-type enzyme family, result of lateral gene transfer Leptospira interrogans

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.18.1.2 additional information
-
 additional information low efficiency Rhodobacter capsulatus
1.18.1.2 additional information
-
 additional information low efficiency Azotobacter vinelandii
1.18.1.2 additional information
-
 additional information the low efficiency is intrinsic to the reductase itself Escherichia coli
1.18.1.2 0.004
-
 reduced flavodoxin flavodoxin I or II Escherichia coli
1.18.1.2 0.15
-
 reduced ferredoxin
-
 Escherichia coli
1.18.1.2 1
-
 reduced ferredoxin
-
 Azotobacter vinelandii
1.18.1.2 90 174 reduced ferredoxin
-
 Chlamydomonas reinhardtii
1.18.1.2 200 600 reduced ferredoxin
-
 Spinacia oleracea
1.18.1.2 200 600 reduced ferredoxin
-
 Anabaena sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.18.1.2 FAD extended conformation Cyanophora paradoxa
1.18.1.2 FAD extended conformation Chlamydomonas reinhardtii
1.18.1.2 FAD extended conformation Rhodobacter capsulatus
1.18.1.2 FAD extended conformation Leptospira interrogans
1.18.1.2 FAD extended conformation, interaction via Tyr96, direct electron transfer between FAD and ferredoxin [2Fe2S] center, modeling of conformation of C4alpha polypeptide backbone and FAD Spinacia oleracea
1.18.1.2 FAD extended conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal Anabaena sp.
1.18.1.2 FAD folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal Escherichia coli
1.18.1.2 FAD folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal Azotobacter vinelandii
1.18.1.2 additional information poor activity with NAD(H) Anabaena sp.
1.18.1.2 NADP+
-
 Cyanophora paradoxa
1.18.1.2 NADP+
-
 Chlamydomonas reinhardtii
1.18.1.2 NADP+
-
 Rhodobacter capsulatus
1.18.1.2 NADP+
-
 Leptospira interrogans
1.18.1.2 NADP+ C-terminal binding domain Escherichia coli
1.18.1.2 NADP+ C-terminal binding domain Azotobacter vinelandii
1.18.1.2 NADP+ C-terminal binding domain Anabaena sp.
1.18.1.2 NADP+ interaction via Tyr314, binding site at the C-terminus Spinacia oleracea
1.18.1.2 NADPH
-
 Cyanophora paradoxa
1.18.1.2 NADPH
-
 Chlamydomonas reinhardtii
1.18.1.2 NADPH
-
 Rhodobacter capsulatus
1.18.1.2 NADPH
-
 Leptospira interrogans
1.18.1.2 NADPH C-terminal binding domain Escherichia coli
1.18.1.2 NADPH C-terminal binding domain Azotobacter vinelandii
1.18.1.2 NADPH C-terminal binding domain Anabaena sp.
1.18.1.2 NADPH interaction via Tyr314, binding site at the C-terminus Spinacia oleracea