U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    purF amidophosphoribosyltransferase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946794, updated on 17-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    purF
    Official Full Name
    amidophosphoribosyltransferase
    Primary source
    ECOCYC:EG10794
    Locus tag
    b2312
    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
    ade; ECK2306; purC
    Summary
    The glutamine amide transfer domain has been identified near the N-terminal end . purF is a component of a polycistronic mRNA . [More information is available at EcoCyc: EG10794].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (2428721..2430238, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene lysine/arginine/ornithine ABC transporter periplasmic binding protein Neighboring gene flavin prenyltransferase Neighboring gene colicin V production protein Neighboring gene cell division protein DedD Neighboring gene bifunctional folylpolyglutamate synthetase/dihydrofolate synthetase

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Coupled formation of an amidotransferase interdomain ammonia channel and a phosphoribosyltransferase active site. Krahn JM, et al. Biochemistry, 1997 Sep 16. PMID 9333323
    2. Glutamine phosphoribosylpyrophosphate amidotransferase from Escherichia coli. Purification and properties. Messenger LJ, et al. J Biol Chem, 1979 May 10. PMID 372191
    3. Amino-terminal deletions define a glutamine amide transfer domain in glutamine phosphoribosylpyrophosphate amidotransferase and other PurF-type amidotransferases. Mei BG, et al. J Bacteriol, 1990 Jun. PMID 2188964, Free PMC Article
    4. Nucleotide sequence of the Escherichia coli purF gene encoding amidophosphoribosyltransferase for de novo purine nucleotide synthesis. Sampei G, et al. Nucleic Acids Res, 1988 Sep 12. PMID 3047685, Free PMC Article
    5. Nucleotide sequence of Escherichia coli purF and deduced amino acid sequence of glutamine phosphoribosylpyrophosphate amidotransferase. Tso JY, et al. J Biol Chem, 1982 Apr 10. PMID 6277938

    See all (28) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The ammonia channel in 5'-phosphoribosylpyrophosphate amidotransferase is regarded as a "pipe" through which ammonia travels in the absence of an external "driving" potential.
      Title: Computational studies of ammonia channel function in glutamine 5'-phosphoribosylpyrophosphate amidotransferase.
    2. phosphoribosylanthranilate isomerase
      Title: A study in molecular contingency: glutamine phosphoribosylpyrophosphate amidotransferase is a promiscuous and evolvable phosphoribosylanthranilate isomerase.
    3. N-terminus verified by Edman degradation on mature peptide
      Title: Glutamine phosphoribosylpyrophosphate amidotransferase from cloned Escherichia coli purF. NH2-terminal amino acid sequence, identification of the glutamine site, and trace metal analysis.
    Submit: New GeneRIF Correction

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables amidophosphoribosyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables amidophosphoribosyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables amidophosphoribosyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glycosyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glycosyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables guanosine tetraphosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion 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
    		  
    Process Evidence Code Pubs
    involved_in 'de novo' IMP biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within glutamine metabolic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    acts_upstream_of_or_within glutamine metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in purine nucleobase biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within purine nucleotide biosynthetic process EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in purine nucleotide biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within purine nucleotide biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in purine nucleotide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within purine nucleotide biosynthetic process 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 IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytosol HDA PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    amidophosphoribosyltransferase
    NP_416815.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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
      2428721..2430238 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_416815.1 amidophosphoribosyltransferase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_416815.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9AH83
      Conserved Domains (1) summary
      PRK09246
      Location:1 → 505
      PRK09246; amidophosphoribosyltransferase; Provisional
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.