Ferredoxin--NADP reductase (P28861)

Identification
Name:Ferredoxin--NADP reductase
Synonyms:
  • FNR
  • DA1
  • Flavodoxin reductase
  • FLDR
  • FLXR
  • Methyl viologen resistance protein A
Gene Name:fpr
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity
Specific Function:Transports electrons between flavodoxin or ferredoxin and NADPH. Involved in the reductive activation of cobalamin- independent methionine synthase, pyruvate formate lyase and anaerobic ribonucleotide reductase. Also protects against superoxide radicals due to methyl viologen in the presence of oxygen
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Reduced ferredoxin+1.0Thumb+1.0Thumb ↔ 1.0Oxidized ferredoxin+1.0Thumb
1.0Reduced ferredoxin + 1.0NADP + 1.0Hydrogen ion ↔ 1.0Oxidized ferredoxin + 1.0NADPH
ReactionCard
Complex Reactions:
1.0Thumb+2.0Flavodoxin reduced+2.0Thumb → 1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb
1.0Cytidine triphosphate + 2.0Flavodoxin reduced + 2.0Hydrogen ion → 1.0dCTP + 2.0flavodoxin semi oxidized + 1.0Water
ReactionCard
1.0Thumb+2.0Flavodoxin reduced+2.0Thumb → 1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb
1.0Adenosine triphosphate + 2.0Flavodoxin reduced + 2.0Hydrogen ion → 1.0dATP + 2.0flavodoxin semi oxidized + 1.0Water
ReactionCard
2.0Flavodoxin reduced+1.0Thumb+2.0Thumb → 1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb
2.0Flavodoxin reduced + 1.0Guanosine triphosphate + 2.0Hydrogen ion → 1.0dGTP + 2.0flavodoxin semi oxidized + 1.0Water
ReactionCard
2.0Flavodoxin reduced+2.0Thumb+1.0Thumb → 1.0Thumb+2.0flavodoxin semi oxidized+1.0Thumb
2.0Flavodoxin reduced + 2.0Hydrogen ion + 1.0Uridine triphosphate → 1.0Deoxyuridine triphosphate + 2.0flavodoxin semi oxidized + 1.0Water
ReactionCard
2.0flavodoxin semi oxidized+1.0Thumb → 2.0Flavodoxin reduced+1.0Thumb+1.0Thumb
2.0flavodoxin semi oxidized + 1.0NADPH → 2.0Flavodoxin reduced + 1.0Hydrogen ion + 1.0NADP
ReactionCard
2.0reduced ferredoxin+1.0Thumb+1.0Thumb → 2.0oxidized ferredoxin+1.0Thumb
2.0reduced ferredoxin + 1.0NADP + 1.0Hydrogen ion → 2.0oxidized ferredoxin + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB00082Cytidine triphosphateMetaboCard
ECMDB01532dATPMetaboCard
ECMDB00998dCTPMetaboCard
ECMDB01191Deoxyuridine triphosphateMetaboCard
ECMDB01440dGTPMetaboCard
ECMDB01273Guanosine triphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
ECMDB00285Uridine triphosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
oxidoreductase activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b3924
Gene OrientationCounterclockwise
Centisome Percentage:88.62
Left Sequence End4111749
Right Sequence End4112495
Gene Sequence:
>747 bp
ATGGATTTCAGCGGTAAAAATGTCTGGGTAACCGGCGCAGGTAAAGGTATCGGCTACGCC
ACGGCGCTGGCGTTTGTTGAGGCGGGAGCGAAAGTTACAGGTTTTGATCAAGCGTTCACT
CAGGAGCAATATCCCTTTGCGACCGAAGTGATGGATGTTGCCGACGCTGCGCAGGTCGCG
CAAGTGTGTCAGCGACTGTTAGCTGAAACGGAGCGACTGGACGCGCTGGTCAATGCGGCG
GGAATTTTACGCATGGGCGCGACCGATCAGCTCAGTAAAGAGGACTGGCAGCAGACTTTT
GCGGTTAACGTCGGCGGTGCGTTTAACCTGTTCCAGCAAACCATGAACCAGTTTCGCCGT
CAGCGGGGCGGGGCGATTGTCACTGTGGCGTCCGACGCCGCGCACACGCCGCGTATTGGC
ATGAGTGCTTATGGCGCATCGAAAGCGGCGCTGAAAAGCCTGGCGTTGAGCGTCGGGCTG
GAACTGGCGGGTAGCGGCGTGCGCTGTAATGTGGTTTCGCCTGGCTCCACCGACACCGAT
ATGCAACGCACGCTGTGGGTGAGCGATGACGCCGAAGAACAGCGTATTCGCGGCTTTGGC
GAGCAGTTTAAACTCGGCATTCCGCTGGGGAAAATCGCCCGTCCACAAGAGATCGCCAAC
ACGATTTTGTTCCTCGCCTCTGACCTCGCCAGCCATATTACCCTACAGGATATTGTGGTC
GATGGCGGCTCAACGCTGGGGGCATAA
Protein Properties
Pfam Domain Function:
Protein Residues:248
Protein Molecular Weight:27751
Protein Theoretical pI:7
PDB File:1FDR
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Ferredoxin--NADP reductase
MADWVTGKVTKVQNWTDALFSLTVHAPVLPFTAGQFTKLGLEIDGERVQRAYSYVNSPDN
PDLEFYLVTVPDGKLSPRLAALKPGDEVQVVSEAAGFFVLDEVPHCETLWMLATGTAIGP
YLSILQLGKDLDRFKNLVLVHAARYAADLSYLPLMQELEKRYEGKLRIQTVVSRETAAGS
LTGRIPALIESGELESTIGLPMNKETSHVMLCGNPQMVRDTQQLLKETRQMTKHLRRRPG
HMTAEHYW
References
External Links:
ResourceLink
Uniprot ID:P28861
Uniprot Name:FENR_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674717
PDB ID:1FDR
Ecogene ID:EG11518
Ecocyc:EG11518
ColiBase:b3924
Kegg Gene:b3924
EchoBASE ID:EB1480
CCDB:FENR_ECOLI
BacMap:16131762
General Reference:
  • Bianchi, V., Reichard, P., Eliasson, R., Pontis, E., Krook, M., Jornvall, H., Haggard-Ljungquist, E. (1993). "Escherichia coli ferredoxin NADP+ reductase: activation of E. coli anaerobic ribonucleotide reduction, cloning of the gene (fpr), and overexpression of the protein." J Bacteriol 175:1590-1595. Pubmed: 8449868
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Ingelman, M., Bianchi, V., Eklund, H. (1997). "The three-dimensional structure of flavodoxin reductase from Escherichia coli at 1.7 A resolution." J Mol Biol 268:147-157. Pubmed: 9149148
  • Jenkins, C. M., Waterman, M. R. (1994). "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities." J Biol Chem 269:27401-27408. Pubmed: 7961651
  • Morimyo, M. (1988). "Isolation and characterization of methyl viologen-sensitive mutants of Escherichia coli K-12." J Bacteriol 170:2136-2142. Pubmed: 2834327
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Nucleic Acids Res 21:3391-3398. Pubmed: 8346018
  • Truniger, V., Boos, W., Sweet, G. (1992). "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri." J Bacteriol 174:6981-6991. Pubmed: 1400248