RegulonDB RegulonDB 11.0: Gene Form
   

fldA gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

fldA ybfE uof fur SoxS OxyR SoxS OxyR CRP Fur Fur fldAp fldAp TSS_821 TSS_821 uofp uofp TSS_820 TSS_820 furpb furpb furpa furpa TSS_817 TSS_817 TSS_816 TSS_816 TSS_815 TSS_815

Gene      
Name: fldA    Texpresso search in the literature
Synonym(s): ECK0672, EG10318, b0684
Genome position(nucleotides): 710935 <-- 711465
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
 48.96
External database links:  
ASAP:
 ABE-0002332
CGSC:
 31496
ECHOBASE:
 EB0314
ECOLIHUB:
 fldA
OU-MICROARRAY:
 b0684
STRING:
 511145.b0684
COLOMBOS: fldA


Product      
Name: flavodoxin 1
Synonym(s): FldA
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 19.737
Isoelectric point: 3.986
Motif(s):
 
Type Positions Sequence Comment
2 -> 176 AITGIFFGSDTGNTENIAKMIQKQLGKDVADVHDIAKSSKEDLEAYDILLLGIPTWYYGEAQCDWDDFFPTLEEIDFNGKLVALFGCGDQEDYAEYFCDALGTIRDIIEPRGATIVGHWPTAGYHFEASKGLADDDHFVGLAIDEDRQPELTAERVEKWVKQISEELHLDEILNA UniProt: Flavodoxin 1.
4 -> 165 TGIFFGSDTGNTENIAKMIQKQLGKDVADVHDIAKSSKEDLEAYDILLLGIPTWYYGEAQCDWDDFFPTLEEIDFNGKLVALFGCGDQEDYAEYFCDALGTIRDIIEPRGATIVGHWPTAGYHFEASKGLADDDHFVGLAIDEDRQPELTAERVEKWVKQIS UniProt: Flavodoxin-like.
6 -> 160 IFFGSDTGNTENIAKMIQKQLGKDVADVHDIAKSSKEDLEAYDILLLGIPTWYYGEAQCDWDDFFPTLEEIDFNGKLVALFGCGDQEDYAEYFCDALGTIRDIIEPRGATIVGHWPTAGYHFEASKGLADDDHFVGLAIDEDRQPELTAERVEKW
10 -> 15 SDTGNT UniProt: FMN.
56 -> 60 TWYYG UniProt: FMN.

 
Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.4 - energy production/transport --> 1.4.1 - electron donors
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0005515 - protein binding
GO:0009055 - electron transfer activity
GO:0000166 - nucleotide binding
GO:0010181 - FMN binding
biological_process GO:0022900 - electron transport chain
Note(s): Note(s): ...[more].
Evidence: [IE] Inferred from experiment
Reference(s): [1] Crain AV., et al., 2013
[2] Hall DA., et al., 2001
[3] McIver L., et al., 1998
[4] Vetter H., et al., 1971
External database links:  
ALPHAFOLD:
 P61949
DIP:
 DIP-48242N
ECOCYC:
 FLAVODOXIN1-MONOMER
ECOLIWIKI:
 b0684
INTERPRO:
 IPR010086
INTERPRO:
 IPR029039
INTERPRO:
 IPR008254
INTERPRO:
 IPR001226
MODBASE:
 P61949
PDB:
 1AG9
PDB:
 2MOK
PDB:
 1AHN
PFAM:
 PF00258
PRIDE:
 P61949
PRODB:
 PRO_000022635
PROSITE:
 PS00201
PROSITE:
 PS50902
REFSEQ:
 NP_415210
SMR:
 P61949
UNIPROT:
 P61949


Operon      
Name: fldA-uof-fur         
Operon arrangement:
Transcription unit        Promoter
fur
fur
uof-fur
fldA-uof-fur


Transcriptional Regulation      
Display Regulation             
Activated by: SoxS


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_815 710700 reverse nd [RS-EPT-CBR] [5]
  promoter TSS_816 710711 reverse nd [RS-EPT-CBR] [5]
  promoter TSS_817 710713 reverse nd [RS-EPT-CBR] [5]
  promoter TSS_820 710828 reverse nd [RS-EPT-CBR] [5]
  promoter TSS_821 711001 reverse nd [RS-EPT-CBR] [5]


Evidence    

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


Reference(s)    

 [1] 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

 [2] 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

 [3] McIver L., Leadbeater C., Campopiano DJ., Baxter RL., Daff SN., Chapman SK., Munro AW., 1998, Characterisation of flavodoxin NADP+ oxidoreductase and flavodoxin; key components of electron transfer in Escherichia coli., Eur J Biochem 257(3):577-85

 [4] Vetter H., Knappe J., 1971, Flavodoxin and ferredoxin of Escherichia coli., Hoppe Seylers Z Physiol Chem 352(3):433-46

 [5] 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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