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pheS phenylalanine--tRNA ligase subunit alpha [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 946223, updated on 2-May-2024

Summary

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Gene symbol
pheS
Gene description
phenylalanine--tRNA ligase subunit alpha
Primary source
ASAP:ABE-0005722
Locus tag
b1714
See related
ECOCYC:EG10709
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
ECK1712; phe-act
Summary
HT_Cmplx7_Cyt: [More information is available at EcoGene: EG10709]. The subunit of PheRS contains the phenylalanine binding site within the conserved motif 2 and motif 3 of the protein . [More information is available at EcoCyc: EG10709].
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Genomic context

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Sequence:
NC_000913.3 (1797959..1798942, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene integration host factor subunit alpha Neighboring gene phenylalanine--tRNA ligase subunit beta Neighboring gene pheST-ihfA operon leader peptide Neighboring gene 50S ribosomal subunit protein L20

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. G673 could be a novel mutational hot spot for intragenic suppressors of pheS5 lesion in Escherichia coli. Ponmani T, et al. Microbiologyopen, 2014 Jun. PMID 24811065, Free PMC Article
  2. PROTEIN AND NUCLEIC ACID SYNTHESIS IN TWO MUTANTS OF ESCHERICHIA COLI WITH TEMPERATURE-SENSITIVE AMINOACYL RIBONUCLEIC ACID SYNTHETASES. EIDLIC L, et al. J Bacteriol, 1965 Mar. PMID 14273649, Free PMC Article
  3. Impaired affinity for phenylalanine in Escherichia coli phenylalanyl-tRNA synthetase mutant caused by Gly-to-Asp exchange in motif 2 of class II tRNA synthetases. Kast P, et al. FEBS Lett, 1991 Nov 18. PMID 1959653
  4. Amino acid substrate specificity of Escherichia coli phenylalanyl-tRNA synthetase altered by distinct mutations. Kast P, et al. J Mol Biol, 1991 Nov 5. PMID 1942071
  5. Identification of the pheS5 mutation, which causes thermosensitivity of Escherichia coli mutant NP37. Kast P, et al. J Bacteriol, 1992 Mar. PMID 1537809, Free PMC Article

See all (89) citations in PubMed

GeneRIFs: Gene References Into Functions

Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables aminoacyl-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables magnesium ion binding IEA
Inferred from Electronic Annotation
more info
  
enables metal ion binding IEA
Inferred from Electronic Annotation
more info
  
enables phenylalanine-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables phenylalanine-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein binding IPI
Inferred from Physical Interaction
more info
 PubMed 
enables tRNA binding IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in phenylalanyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in phenylalanyl-tRNA aminoacylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in phenylalanyl-tRNA aminoacylation IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within phenylalanyl-tRNA aminoacylation IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in translation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
located_in cytoplasm HDA PubMed 
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytosol IDA
Inferred from Direct Assay
more info
 PubMed 
part_of phenylalanine-tRNA ligase complex IDA
Inferred from Direct Assay
more info
 PubMed 
part_of phenylalanine-tRNA ligase complex IPI
Inferred from Physical Interaction
more info
 PubMed 

General protein information

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Preferred Names
phenylalanine--tRNA ligase subunit alpha
NP_416229.1

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
    1797959..1798942 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_416229.1 phenylalanine--tRNA ligase subunit alpha [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_416229.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A6L6ZY99
    Conserved Domains (1) summary
    PRK00488
    Location:1 → 326
    pheS; phenylalanyl-tRNA synthetase subunit alpha; Validated
Nucleotide Protein
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