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    asnB asparagine synthetase B [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945281, updated on 3-Dec-2024

    Summary

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    Official Symbol
    asnB
    Official Full Name
    asparagine synthetase B
    Primary source
    ECOCYC:EG10092
    Locus tag
    b0674
    See related
    ASAP:ABE-0002292
    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
    ECK0662
    Summary
    AsnA and AsnB are redundant; an asparagine auxotrophy requires that both genes be mutated. [More information is available at EcoGene: EG10092]. Asparagine synthetase B (AsnB) is one of two asparagine synthetases in Escherichia coli, catalyzing the glutamine-dependent and ammonia-dependent conversion of aspartate to asparagine. [More information is available at EcoCyc: EG10092].
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    Genomic context

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    Sequence:
    NC_000913.3 (697513..699177, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene tRNA-Leu Neighboring gene tRNA-Met Neighboring gene UMP phosphatase Neighboring gene DNA-binding transcriptional dual regulator NagC

    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. Three-dimensional structure of Escherichia coli asparagine synthetase B: a short journey from substrate to product. Larsen TM, et al. Biochemistry, 1999 Dec 7. PMID 10587437
    2. An alternative mechanism for the nitrogen transfer reaction in asparagine synthetase. Richards NG, et al. FEBS Lett, 1992 Nov 23. PMID 1358677
    3. Nucleotide sequence of Escherichia coli asnB and deduced amino acid sequence of asparagine synthetase B. Scofield MA, et al. J Biol Chem, 1990 Aug 5. PMID 1973930
    4. Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad. Boehlein SK, et al. J Biol Chem, 1994 Mar 11. PMID 7907328
    5. Mapping the aspartic acid binding site of Escherichia coli asparagine synthetase B using substrate analogs. Parr IB, et al. J Med Chem, 1996 Jun 7. PMID 8691431

    See all (27) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. formation of the beta-aspartyl-AMP intermediate, and therefore the eventual production of asparagine, is dependent on the presence of a carboxylate side chain at this Glu-348 position in the synthetase active site.
      Title: A conserved glutamate controls the commitment to acyl-adenylate formation in asparagine synthetase.
    2. N-terminus verified by Edman degradation on mature peptide
      Title: Glutamine-dependent nitrogen transfer in Escherichia coli asparagine synthetase B. Searching for the catalytic triad.
    3. observations are consistent with a model in which exogenous ammonia can access the intramolecular tunnel in AS-B during glutamine-dependent asparagine synthesis, in contrast to expectations based on studies of class I amidotransferases.
      Title: A convenient gHMQC-based NMR assay for investigating ammonia channeling in glutamine-dependent amidotransferases: studies of Escherichia coli asparagine synthetase B.
    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 ATP binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables amino acid binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables asparagine synthase (glutamine-hydrolyzing) activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables asparagine synthase (glutamine-hydrolyzing) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables asparagine synthase (glutamine-hydrolyzing) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables asparagine synthase (glutamine-hydrolyzing) activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables aspartate-ammonia ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein homodimerization activity IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in L-asparagine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within amino acid biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within amino acid catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in asparagine biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in asparagine biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in asparagine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within asparagine biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within glutamine metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    asparagine synthetase B
    NP_415200.1

    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
      697513..699177 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415200.1 asparagine synthetase B [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415200.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2X1QH51
      Conserved Domains (1) summary
      PRK09431
      Location:1 → 553
      asnB; asparagine synthetase B; Provisional
    Nucleotide Protein
    Heading Accession and Version

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