RegulonDB RegulonDB 10.9: Gene Form
   

fpr gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

glpX fpr uspD MarA SoxS anti-anti-terminator anti-terminator terminator TSS_4622 TSS_4622 fprp fprp TSS_4621 TSS_4621

Gene      
Name: fpr    Texpresso search in the literature
Synonym(s): ECK3916, EG10628, b3924, flxR, mvrA
Genome position(nucleotides): 4113726 <-- 4114472 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
53.55
External database links:  
ASAP:
ABE-0012818
ECHOBASE:
EB1480
ECOLIHUB:
fpr
OU-MICROARRAY:
b3924
STRING:
511145.b3924
COLOMBOS: fpr


Product      
Name: flavodoxin/ferredoxin-NADP+ reductase
Synonym(s): FlxR, Fpr, MvrA, dA1
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 27.751
Isoelectric point: 6.634
Motif(s):
 
Type Positions Sequence
174 -> 174 R
74 -> 76 KLS
19 -> 90 LFSLTVHAPVLPFTAGQFTKLGLEIDGERVQRAYSYVNSPDNPDLEFYLVTVPDGKLSPRLAALKPGDEVQV
143 -> 144 AR
184 -> 184 R

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.7 - central intermediary metabolism --> 1.7.1 - unassigned reversible reactions
  5 - cell processes --> 5.6 - protection --> 5.6.2 - detoxification
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0016491 - oxidoreductase activity
GO:0000166 - nucleotide binding
GO:0004324 - ferredoxin-NADP+ reductase activity
GO:0071949 - FAD binding
biological_process GO:0016226 - iron-sulfur cluster assembly
GO:0042493 - response to drug
GO:0055114 - oxidation-reduction process
GO:0000303 - response to superoxide
Note(s): Note(s): ...[more].
Reference(s): [1] Bakkes PJ., et al., 2015
[2] Crain AV., et al., 2013
[3] Dangi B., et al., 2001
[4] Djaman O., et al., 2004
[5] Giro M., et al., 2006
[6] Griffith KL., et al., 2001
[7] Hall DA., et al., 2001
[8] Jair KW., et al., 1996
[9] Jenkins CM., et al., 1994
[10] Jenkins CM., et al., 1998
[11] Krapp AR., et al., 1995
[12] Krapp AR., et al., 1997
[13] Lee JH., et al., 2007
[14] Nakayama T., et al., 2013
[15] Niazi JH., et al., 2007
[16] Rodriguez RE., et al., 1998
External database links:  
ECOCYC:
FLAVONADPREDUCT-MONOMER
ECOLIWIKI:
b3924
INTERPRO:
IPR033892
INTERPRO:
IPR039261
INTERPRO:
IPR017938
INTERPRO:
IPR001433
INTERPRO:
IPR008333
INTERPRO:
IPR017927
MODBASE:
P28861
PDB:
2XNJ
PDB:
1FDR
PFAM:
PF00175
PFAM:
PF00970
PRIDE:
P28861
PRODB:
PRO_000022684
PROSITE:
PS51384
REFSEQ:
NP_418359
SMR:
P28861
UNIPROT:
P28861


Operon      
Name: fpr         
Operon arrangement:
Transcription unit        Promoter
fpr


Transcriptional Regulation      
Display Regulation             
Activated by: MarA, SoxS


RNA cis-regulatory element    
Attenuation: Transcriptional


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_4621 4114497 reverse nd [RS-EPT-CBR] [17]
  promoter TSS_4622 4115212 forward nd [RS-EPT-CBR] [17]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Bakkes PJ., Biemann S., Bokel A., Eickholt M., Girhard M., Urlacher VB., 2015, Design and improvement of artificial redox modules by molecular fusion of flavodoxin and flavodoxin reductase from Escherichia coli., Sci Rep 5:12158

 [2] Crain AV., Broderick JB., 2013, Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme., Biochim Biophys Acta 1834(12):2512-9

 [3] Dangi B., Pelupessey P., Martin RG., Rosner JL., Louis JM., Gronenborn AM., 2001, Structure and dynamics of MarA-DNA complexes: an NMR investigation., J Mol Biol 314(1):113-27

 [4] Djaman O., Outten FW., Imlay JA., 2004, Repair of oxidized iron-sulfur clusters in Escherichia coli., J Biol Chem 279(43):44590-9

 [5] Giro M., Carrillo N., Krapp AR., 2006, Glucose-6-phosphate dehydrogenase and ferredoxin-NADP(H) reductase contribute to damage repair during the soxRS response of Escherichia coli., Microbiology 152(Pt 4):1119-28

 [6] Griffith KL., Wolf RE., 2001, Systematic mutagenesis of the DNA binding sites for SoxS in the Escherichia coli zwf and fpr promoters: identifying nucleotides required for DNA binding and transcription activation., Mol Microbiol 40(5):1141-54

 [7] Hall DA., Vander Kooi CW., Stasik CN., Stevens SY., Zuiderweg ER., Matthews RG., 2001, Mapping the interactions between flavodoxin and its physiological partners flavodoxin reductase and cobalamin-dependent methionine synthase., Proc Natl Acad Sci U S A 98(17):9521-6

 [8] Jair KW., Yu X., Skarstad K., Thony B., Fujita N., Ishihama A., Wolf RE., 1996, Transcriptional activation of promoters of the superoxide and multiple antibiotic resistance regulons by Rob, a binding protein of the Escherichia coli origin of chromosomal replication., J Bacteriol 178(9):2507-13

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

 [10] Jenkins CM., Waterman MR., 1998, NADPH-flavodoxin reductase and flavodoxin from Escherichia coli: characteristics as a soluble microsomal P450 reductase., Biochemistry 37(17):6106-13

 [11] Krapp AR., Carrillo N., 1995, Functional complementation of the mvrA mutation of Escherichia coli by plant ferredoxin-NADP+ oxidoreductase., Arch Biochem Biophys 317(1):215-21

 [12] Krapp AR., Tognetti VB., Carrillo N., Acevedo A., 1997, The role of ferredoxin-NADP+ reductase in the concerted cell defense against oxidative damage -- studies using Escherichia coli mutants and cloned plant genes., Eur J Biochem 249(2):556-63

 [13] Lee JH., Youn CH., Kim BC., Gu MB., 2007, An oxidative stress-specific bacterial cell array chip for toxicity analysis., Biosens Bioelectron 22(9-10):2223-9

 [14] Nakayama T., Yonekura S., Yonei S., Zhang-Akiyama QM., 2013, Escherichia coli pyruvate:flavodoxin oxidoreductase, YdbK - regulation of expression and biological roles in protection against oxidative stress., Genes Genet Syst 88(3):175-88

 [15] Niazi JH., Kim BC., Gu MB., 2007, Characterization of superoxide-stress sensing recombinant Escherichia coli constructed using promoters for genes zwf and fpr fused to lux operon., Appl Microbiol Biotechnol 74(6):1276-83

 [16] Rodriguez RE., Krapp AR., Carrillo N., 1998, The mvrA locus of Escherichia coli does not encode a ferredoxin-NADP+ reductase., Microbiology 144 ( Pt 9):2375-6

 [17] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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