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Escherichia coli K-12 substr. MG1655 Enzyme: flavodoxin NADP+ reductase



Gene: fpr Accession Numbers: EG10628 (EcoCyc), b3924, ECK3916

Synonyms: flxR, mvrA, dA1

Regulation Summary Diagram: ?

Component of: anaerobic nucleoside-triphosphate reductase activating system (summary available)

Summary:
Fpr: ferredoxin NADP+ reductase [Bianchi93]

Citations: [Eliasson92]

Gene Citations: [Jair95]

Locations: cytosol

Map Position: [4,111,749 <- 4,112,495] (88.62 centisomes)
Length: 747 bp / 248 aa

Molecular Weight of Polypeptide: 27.751 kD (from nucleotide sequence), 28.0 kD (experimental) [Truniger92 ]

pI: 6.57

Unification Links: ASAP:ABE-0012818 , EchoBASE:EB1480 , EcoGene:EG11518 , EcoliWiki:b3924 , ModBase:P28861 , OU-Microarray:b3924 , PortEco:fpr , PR:PRO_000022684 , Pride:P28861 , Protein Model Portal:P28861 , RefSeq:NP_418359 , RegulonDB:EG10628 , SMR:P28861 , String:511145.b3924 , UniProt:P28861

Relationship Links: InterPro:IN-FAMILY:IPR001433 , InterPro:IN-FAMILY:IPR008333 , InterPro:IN-FAMILY:IPR017927 , InterPro:IN-FAMILY:IPR017938 , PDB:Structure:1FDR , PDB:Structure:2XNJ , Pfam:IN-FAMILY:PF00175 , Pfam:IN-FAMILY:PF00970 , Prosite:IN-FAMILY:PS51384

In Paralogous Gene Group: 219 (6 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006001 - fructose catabolic process Inferred from experiment [Kornberg86]
GO:0042493 - response to drug Inferred from experiment [Morimyo88]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0004324 - ferredoxin-NADP+ reductase activity Inferred from experiment Inferred by computational analysis [GOA01, Kornberg86, Bianchi93]
GO:0016491 - oxidoreductase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Kornberg86]
GO:0071949 - FAD binding Inferred from experiment [Ingelman97]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment [Kornberg86]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: cell processes protection detoxification
metabolism central intermediary metabolism unassigned reversible reactions

Essentiality data for fpr knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 24-Mar-2008 by Fulcher C , SRI International


Enzymatic reaction of: flavodoxin NADP+ reductase

Synonyms: FNR, adrenodoxin reductase, methyl viologen resistance protein A, flavodoxin:NADP+ oxidoreductase

EC Number: 1.18.1.2

an oxidized flavodoxin + NADPH + H+ <=> a reduced flavodoxin + NADP+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Reversibility of this reaction is unspecified.

Summary:
Flavodoxin NADP+ reductase is a part of chains of redox reactions and in E. coli is also required for the activation of anaerobic ribonucleoside reductase, pyruvate-formate lyase and methionine synthase. It forms a multi-enzyme complex with flavodoxin and the appropriate activating enzyme. Ferredoxin does not substitute for flavodoxin in E. coli. The FN reductase uses noncovalently bound FAD as a cofactor. Flavodoxin contains FMN. [Bianchi93, Jenkins94, Bianchi95]

Cofactors or Prosthetic Groups: FAD


Subunit of: anaerobic nucleoside-triphosphate reductase activating system

Subunit composition of anaerobic nucleoside-triphosphate reductase activating system = [(NrdD)2][(NrdG)2][Fpr]
         ribonucleoside-triphosphate reductase = (NrdD)2
                 ribonucleoside-triphosphate reductase = NrdD
         ribonucleoside triphosphate reductase activase = (NrdG)2
         flavodoxin NADP+ reductase = Fpr (summary available)

Summary:
The anaerobic nucleoside-triphosphate reductase activating system is composed of three enzymes and several compounds. Anaerobic nucleoside-triphosphate reductase is activated through the action of a specific activating enzyme, nucleoside-triphosphate reductase activase, flavodoxin NADP+ reductase, S-adenosylmethionine, flavodoxin and NADPH. All of these components form a multi-enzyme complex with the ribonucleoside reductase itself. [Bianchi93, Sun95]

Credits:
Last-Curated ? 24-Mar-2008 by Fulcher C , SRI International


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Bianchi93, Jenkins94, UniProt11a]
UniProt: Removed.
Conserved-Region 2 -> 101
[UniProt09]
UniProt: FAD-binding FR-type;
Chain 2 -> 248
[UniProt09]
UniProt: Ferredoxin--NADP reductase;
Nucleotide-Phosphate-Binding-Region 50 -> 53
[UniProt10]
UniProt: FAD;
Amino-Acid-Sites-That-Bind 53
[UniProt10a]
UniProt: NADP; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 66
[UniProt10]
UniProt: FAD; via carbonyl oxygen;
Nucleotide-Phosphate-Binding-Region 74 -> 76
[UniProt10]
UniProt: FAD;
Amino-Acid-Sites-That-Bind 116
[UniProt10]
UniProt: FAD;
Nucleotide-Phosphate-Binding-Region 143 -> 144
[UniProt10a]
UniProt: NADP; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 173 -> 174
[UniProt10a]
UniProt: NADP; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 213 -> 214
[UniProt10a]
UniProt: NADP; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 245
[UniProt10a]
UniProt: NADP; Non-Experimental Qualifier: by similarity;
Nucleotide-Phosphate-Binding-Region 247 -> 248
[UniProt10]
UniProt: FAD;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
4/27/1998 (ptoole) Merged genes EG10005/fruB and EG10628/fpr. The genes fruB and fpr are easily confused; fpr is a synonym for fruB, but fruB is not a synonym for fpr.
3/2/1998 (pkarp) Merged genes G7964/fpr and EG10628/EG11518
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Bianchi93: 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 1993;175(6);1590-5. PMID: 8449868

Bianchi95: Bianchi V, Haggard-Ljungquist E, Pontis E, Reichard P (1995). "Interruption of the ferredoxin (flavodoxin) NADP+ oxidoreductase gene of Escherichia coli does not affect anaerobic growth but increases sensitivity to paraquat." J Bacteriol 1995;177(15);4528-31. PMID: 7635836

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Eliasson92: Eliasson R, Pontis E, Fontecave M, Gerez C, Harder J, Jornvall H, Krook M, Reichard P (1992). "Characterization of components of the anaerobic ribonucleotide reductase system from Escherichia coli." J Biol Chem 267(35);25541-7. PMID: 1460049

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Ingelman97: 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(1);147-57. PMID: 9149148

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Jair95: Jair KW, Martin RG, Rosner JL, Fujita N, Ishihama A, Wolf RE (1995). "Purification and regulatory properties of MarA protein, a transcriptional activator of Escherichia coli multiple antibiotic and superoxide resistance promoters." J Bacteriol 1995;177(24);7100-4. PMID: 8522515

Jenkins94: Jenkins CM, Waterman MR (1994). "Flavodoxin and NADPH-flavodoxin reductase from Escherichia coli support bovine cytochrome P450c17 hydroxylase activities." J Biol Chem 1994;269(44);27401-8. PMID: 7961651

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Kornberg86: Kornberg H (1986). "The roles of HPr and FPr in the utilization of fructose by Escherichia coli." FEBS Lett 194(1);12-5. PMID: 3510127

Morimyo88: Morimyo M (1988). "Isolation and characterization of methyl viologen-sensitive mutants of Escherichia coli K-12." J Bacteriol 170(5);2136-42. PMID: 2834327

Sun95: Sun X, Eliasson R, Pontis E, Andersson J, Buist G, Sjoberg BM, Reichard P (1995). "Generation of the glycyl radical of the anaerobic Escherichia coli ribonucleotide reductase requires a specific activating enzyme." J Biol Chem 1995;270(6);2443-6. PMID: 7852304

Truniger92: Truniger V, Boos W, Sweet G (1992). "Molecular analysis of the glpFKX regions of Escherichia coli and Shigella flexneri." J Bacteriol 174(21);6981-91. PMID: 1400248

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Gillette00: Gillette WK, Martin RG, Rosner JL (2000). "Probing the Escherichia coli transcriptional activator MarA using alanine-scanning mutagenesis: residues important for DNA binding and activation." J Mol Biol 299(5);1245-55. PMID: 10873449

Martin11: Martin RG, Rosner JL (2011). "Promoter discrimination at class I MarA regulon promoters mediated by glutamic acid 89 of the MarA transcriptional activator of Escherichia coli." J Bacteriol 193(2);506-15. PMID: 21097628

Martin99: Martin RG, Gillette WK, Rhee S, Rosner JL (1999). "Structural requirements for marbox function in transcriptional activation of mar/sox/rob regulon promoters in Escherichia coli: sequence, orientation and spatial relationship to the core promoter." Mol Microbiol 1999;34(3);431-41. PMID: 10564485

Pomposiello01: Pomposiello PJ, Bennik MH, Demple B (2001). "Genome-wide transcriptional profiling of the Escherichia coli responses to superoxide stress and sodium salicylate." J Bacteriol 183(13);3890-902. PMID: 11395452

Rodionov01: Rodionov DA, Gelfand MS, Mironov AA, Rakhmaninova AB (2001). "Comparative approach to analysis of regulation in complete genomes: multidrug resistance systems in gamma-proteobacteria." J Mol Microbiol Biotechnol 3(2);319-24. PMID: 11321589


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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