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

Gene ID: 945281, updated on 25-Jun-2025
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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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 Sequence:
NC_000913.3

Go to nucleotide: Graphics FASTA GenBank

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
Products Interactant Other Gene Complex Source Pubs Description

Homology

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IDA
Inferred from Direct Assay
more info
 PubMed 
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 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 protein homodimerization activity IPI
Inferred from Physical Interaction
more info
 PubMed 
Process Evidence Code Pubs
acts_upstream_of_or_within L-asparagine biosynthetic process IGI
Inferred from Genetic Interaction
more info
 PubMed 
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 
acts_upstream_of_or_within asparagine biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within glutamine metabolic process IGI
Inferred from Genetic Interaction
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 
Preferred Names
asparagine synthetase B
NP_415200.1

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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
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