U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

pyrI aspartate carbamoyltransferase, PyrI subunit [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 948763, updated on 4-Feb-2024

Summary

Go to the top of the page Help
Gene symbol
pyrI
Gene description
aspartate carbamoyltransferase, PyrI subunit
Primary source
ASAP:ABE-0013889
Locus tag
b4244
See related
ECOCYC:EG10811
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
ECK4239
Summary
HT_Cmplx5_Cyt: [More information is available at EcoGene: EG10811]. The regulatory subunit is catalytically inactive but contains the common binding site for the allosteric effectors CTP and ATP . [More information is available at EcoCyc: EG10811].
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 (4470986..4471447, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene Mg(2(+)) importing P-type ATPase Neighboring gene enamine/imine deaminase, redox-regulated chaperone Neighboring gene aspartate carbamoyltransferase catalytic subunit Neighboring gene pyrBI operon leader peptide

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. Comparison of two T-state structures of regulatory-chain mutants of Escherichia coli aspartate transcarbamoylase suggests that His20 and Asp19 modulate the response to heterotropic effectors. Stec B, et al. Acta Crystallogr D Biol Crystallogr, 2007 Dec. PMID 18084072
  2. Threonine 82 in the regulatory chain is important for nucleotide affinity and for the allosteric stabilization of Escherichia coli aspartate transcarbamoylase. Williams MK, et al. Biochim Biophys Acta, 1998 Dec 8. PMID 9920401
  3. A single mutation in the regulatory chain of Escherichia coli aspartate transcarbamoylase results in an extreme T-state structure. Williams MK, et al. J Mol Biol, 1998 Aug 7. PMID 9680480
  4. Role of allosteric: zinc interdomain region of the regulatory subunit in the allosteric regulation of aspartate transcarbamoylase from Escherichia coli. Rastogi VK, et al. Arch Biochem Biophys, 1998 Jun 15. PMID 9637729
  5. The influence of the regulatory chain amino acids Glu-62 and IIe-12 on the heterotropic properties of Escherichia coli aspartate transcarbamoylase. Dutta M, et al. Biochemistry, 1998 Jun 16. PMID 9628727

See all (123) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. N-terminus verified by Edman degradation on mature peptide
    Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
  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

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

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables zinc ion binding IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
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 pyrimidine nucleotide biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
part_of aspartate carbamoyltransferase complex IEA
Inferred from Electronic Annotation
more info
  
part_of aspartate carbamoyltransferase complex IPI
Inferred from Physical Interaction
more info
 PubMed 
located_in cytoplasm HDA PubMed 

General protein information

Go to the top of the page Help
Preferred Names
aspartate carbamoyltransferase, PyrI subunit
NP_418665.1

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
    4470986..4471447 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_418665.1 aspartate carbamoyltransferase, PyrI subunit [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_418665.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A5B9AFB2, A0A7H9QU30
    Conserved Domains (1) summary
    TIGR00240
    Location:4 → 153
    ATCase_reg; aspartate carbamoyltransferase, regulatory subunit
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.