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fbp fructose-1,6-bisphosphatase 1 [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948753, updated on 19-Sep-2024

Summary

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Official Symbol
fbp
Official Full Name
fructose-1,6-bisphosphatase 1
Primary source
ECOCYC:EG10283
Locus tag
b4232
See related
ASAP:ABE-0013842
Gene type
protein coding
RefSeq status
PROVISIONAL
Organism
Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
Lineage
Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
Also known as
ECK4227; fdp
Summary
Fructose-1,6-bisphosphatase catalyzes the conversion of fructose-1,6-bisphosphate to fructose-6-phosphate in the gluconeogenesis pathway. [More information is available at EcoCyc: EG10283].
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Genomic context

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Sequence:
NC_000913.3 (4454611..4455609, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene galactofuranose ABC transporter putative ATP binding subunit Neighboring gene galactofuranose ABC transporter putative membrane subunit YtfT Neighboring gene galactofuranose ABC transporter putative membrane subunit YjtF Neighboring gene UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate ligase Neighboring gene putative ribosome biogenesis factor YjgA

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition. Hines JK, et al. J Biol Chem, 2007 Dec 7. PMID 17933867
  2. Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch. Hines JK, et al. J Biol Chem, 2007 Aug 24. PMID 17567577
  3. Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state. Hines JK, et al. J Biol Chem, 2007 Apr 20. PMID 17314096
  4. Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase. Hines JK, et al. J Biol Chem, 2006 Jul 7. PMID 16670087
  5. R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase. Iancu CV, et al. J Biol Chem, 2005 May 20. PMID 15767255

See all (25) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. analysis of inhibited fructose-1,6-bisphosphatase from Escherichia coli
    Title: Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch.
  2. suggest a new mechanism of regulation in the FBPase enzyme family: anionic ligands, most likely phosphoenolpyruvate, bind to allosteric activator sites, which in turn stabilize a tetramer and a polypeptide fold that obstructs AMP binding
    Title: Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase.
  3. conformational changes in two helices due to the binding of AMP
    Title: R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase.
  4. analysis of activated fructose-1,6-bisphosphatase from Escherichia coli shows a mechanism of feed-forward activation in bacterial central metabolism
    Title: Structures of activated fructose-1,6-bisphosphatase from Escherichia coli. Coordinate regulation of bacterial metabolism and the conservation of the R-state.
Submit: New GeneRIF Correction

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables fructose 1,6-bisphosphate 1-phosphatase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables fructose 1,6-bisphosphate 1-phosphatase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables fructose 1,6-bisphosphate 1-phosphatase activity IEA
Inferred from Electronic Annotation
more info
  
enables hydrolase activity IEA
Inferred from Electronic Annotation
more info
  
enables identical protein binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables magnesium ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in carbohydrate metabolic process IEA
Inferred from Electronic Annotation
more info
  
involved_in fructose 1,6-bisphosphate metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in fructose 6-phosphate metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in fructose metabolic process IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in gluconeogenesis IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in gluconeogenesis IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within gluconeogenesis IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
part_of protein-containing complex IPI
Inferred from Physical Interaction
more info
 PubMed 

General protein information

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Preferred Names
fructose-1,6-bisphosphatase 1
NP_418653.1

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_000913.3 Reference assembly

    Range
    4454611..4455609 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418653.1 fructose-1,6-bisphosphatase 1 [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418653.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A828NX89
    Conserved Domains (1) summary
    PRK09293
    Location:1 → 330
    PRK09293; class 1 fructose-bisphosphatase
Nucleotide Protein
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