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    pyrB aspartate carbamoyltransferase catalytic subunit [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948767, updated on 17-Dec-2024

    Summary

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    Official Symbol
    pyrB
    Official Full Name
    aspartate carbamoyltransferase catalytic subunit
    Primary source
    ECOCYC:EG10805
    Locus tag
    b4245
    See related
    ASAP:ABE-0013892
    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
    ECK4240
    Summary
    HT_Cmplx5_Cyt: [More information is available at EcoGene: EG10805]. The catalytic subunit is enzymatically active but lacks the homotropic response to the substates, and is insensitive to inhibition by CTP . [More information is available at EcoCyc: EG10805].
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    Genomic context

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    Sequence:
    NC_000913.3 (4471460..4472395, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene enamine/imine deaminase, redox-regulated chaperone Neighboring gene aspartate carbamoyltransferase, PyrI subunit Neighboring gene pyrBI operon leader peptide Neighboring gene RutC family protein YjgH

    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. Weakening of the interface between adjacent catalytic chains promotes domain closure in Escherichia coli aspartate transcarbamoylase. Baker DP, et al. Protein Sci, 1995 Feb. PMID 7757014, Free PMC Article
    2. Random circular permutation leading to chain disruption within and near alpha helices in the catalytic chains of aspartate transcarbamoylase: effects on assembly, stability, and function. Beernink PT, et al. Protein Sci, 2001 Mar. PMID 11344321, Free PMC Article
    3. The conserved residues glutamate-37, aspartate-100, and arginine-269 are important for the structural stabilization of Escherichia coli aspartate transcarbamoylase. Baker DP, et al. Biochemistry, 1993 Sep 28. PMID 8104480
    4. Direct observation in solution of a preexisting structural equilibrium for a mutant of the allosteric aspartate transcarbamoylase. Fetler L, et al. Proc Natl Acad Sci U S A, 2007 Jan 9. PMID 17202260, Free PMC Article
    5. Design, synthesis, and bioactivity of novel inhibitors of E. coli aspartate transcarbamoylase. Eldo J, et al. Bioorg Med Chem Lett, 2007 Apr 1. PMID 17336518, Free PMC Article

    See all (126) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. N-terminus verified by Edman degradation on mature peptide
      Title: Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis.
    2. studies of the transition between the R and T states involving the quaternary structure of the protein; results emphasize a significant role of the protein-solvent interactions
      Title: Cooperativity and high pressure: stabilization of the R conformation of the allosteric aspartate transcarbamylase under the influence of pressure.
    3. mutant Q137A enzyme was studied by time-resolved, small-angle X-ray scattering and its structure was determined in the presence of N-phosphonacetyl-L-aspartate to 2.7 angstroms resolution
      Title: A single amino acid substitution in the active site of Escherichia coli aspartate transcarbamoylase prevents the allosteric transition.
    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 amino acid binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables aspartate carbamoyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in 'de novo' UMP biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in 'de novo' pyrimidine nucleobase biosynthetic process IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in 'de novo' pyrimidine nucleobase biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in amino acid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glutamine metabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within protein homotrimerization IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in pyrimidine nucleotide biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    part_of aspartate carbamoyltransferase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in cytoplasm HDA PubMed 
    is_active_in cytoplasm 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
    aspartate carbamoyltransferase catalytic subunit
    NP_418666.1

    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
      4471460..4472395 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418666.1 aspartate carbamoyltransferase catalytic subunit [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418666.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A775TFP9
      Conserved Domains (1) summary
      TIGR00670
      Location:8 → 306
      asp_carb_tr; aspartate carbamoyltransferase
    Nucleotide Protein
    Heading Accession and Version

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