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    ansB L-asparaginase 2 [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947454, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ansB
    Official Full Name
    L-asparaginase 2
    Primary source
    ECOCYC:EG10046
    Locus tag
    b2957
    See related
    ASAP:ABE-0009700
    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
    ECK2952
    Summary
    There are two asparaginase enzymes in Escherichia coli, I and II. [More information is available at EcoCyc: EG10046].
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    Genomic context

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    Sequence:
    NC_000913.3 (3099682..3100728, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene dITP/XTP pyrophosphatase Neighboring gene heme chaperone HemW Neighboring gene DUF1202 domain-containing protein YggM Neighboring gene DUF2884 domain-containing protein YggN Neighboring gene putative ribosome assembly factor YggL Neighboring gene tRNA m(7)G46 methyltransferase

    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. Interaction between L-aspartic acid and L-asparaginase from Escherichia coli: binding and inhibition studies. Jayaram HN, et al. J Enzyme Inhib, 1986. PMID 3334241
    2. Transcriptional co-activation at the ansB promoters: involvement of the activating regions of CRP and FNR when bound in tandem. Scott S, et al. Mol Microbiol, 1995 Nov. PMID 8748035
    3. Revealing Escherichia coli type II L-asparaginase active site flexible loop in its open, ligand-free conformation. Maggi M, et al. Sci Rep, 2021 Sep 23. PMID 34556749, Free PMC Article
    4. Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy. Swain AL, et al. Proc Natl Acad Sci U S A, 1993 Feb 15. PMID 8434007, Free PMC Article
    5. Co-dependent positive regulation of the ansB promoter of Escherichia coli by CRP and the FNR protein: a molecular analysis. Jennings MP, et al. Mol Microbiol, 1993 Jul. PMID 8412660

    See all (39) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Revealing Escherichia coli type II L-asparaginase active site flexible loop in its open, ligand-free conformation.
      Title: Revealing Escherichia coli type II L-asparaginase active site flexible loop in its open, ligand-free conformation.
    2. Biophysical characterization of two commercially available preparations of the drug containing Escherichia coli L-Asparaginase 2.
      Title: Biophysical characterization of two commercially available preparations of the drug containing Escherichia coli L-Asparaginase 2.
    3. deletion of the gspDE gene reduced extracellular production of asparaginase isozyme II, indicating that secretion of recombinant asparaginase isozyme II was partially ascribed to the recognition by the general secretion machinery
      Title: Application of repeated aspartate tags to improving extracellular production of Escherichia coli L-asparaginase isozyme II.
    4. The crystal structure of active site variants of E coli antileukemic L-asparaginase reveals a conserved zinc-binding site.
      Title: Crystal structure of active site mutant of antileukemic L-asparaginase reveals conserved zinc-binding site.
    5. N-terminus verified by Edman degradation on mature peptide
      Title: The primary structure of L-asparaginase from Escherichia coli.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    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 asparaginase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables asparaginase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables asparaginase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in asparagine catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in asparagine metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein homotetramerization IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in outer membrane-bounded periplasmic space IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in periplasmic space IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of protein-containing complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    L-asparaginase 2
    NP_417432.1

    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
      3099682..3100728 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417432.1 L-asparaginase 2 [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417432.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5C0PZP7
      Conserved Domains (1) summary
      PRK11096
      Location:2 → 348
      ansB; L-asparaginase II; Provisional
    Nucleotide Protein
    Heading Accession and Version

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