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    gshA glutamate--cysteine ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944881, updated on 3-Dec-2024

    Summary

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    Official Symbol
    gshA
    Official Full Name
    glutamate--cysteine ligase
    Primary source
    ECOCYC:EG10418
    Locus tag
    b2688
    See related
    ASAP:ABE-0008845
    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
    ECK2683; gsh-I
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    Genomic context

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    Sequence:
    NC_000913.3 (2814883..2816439, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene S-ribosylhomocysteine lyase Neighboring gene ncRNA Neighboring gene DedA family protein YqaA Neighboring gene fructose-1-phosphate phosphatase YqaB Neighboring gene tRNA-Arg

    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. Sulphydryl-mediated DNA breakage by phlemomycin in Escherichia coli. Sleigh MJ, et al. Mutat Res, 1977 Feb. PMID 320461
    2. Design, synthesis and evaluation of transition-state analogue inhibitors of Escherichia coli gamma-glutamylcysteine synthetase. Tokutake N, et al. Bioorg Med Chem, 1998 Oct. PMID 9839023
    3. ATP-dependent inactivation of Escherichia coli gamma-glutamylcysteine synthetase by L-glutamic acid gamma-monohydroxamate. Katoh M, et al. Biosci Biotechnol Biochem, 1998 Jul. PMID 9720231
    4. Effects of intracellular glutathione on sensitivity of Escherichia coli to mercury and arsenite. Latinwo LM, et al. Biochem Biophys Res Commun, 1998 Jan 6. PMID 9439611
    5. Bacterial glutathione: a sacrificial defense against chlorine compounds. Chesney JA, et al. J Bacteriol, 1996 Apr. PMID 8606194, Free PMC Article

    See all (55) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Polyamines are involved in easing of oxidative stress through stimulation of synthesis of SoxR, EmrR and GshA together with RpoS.
      Title: Three members of polyamine modulon under oxidative stress conditions: two transcription factors (SoxR and EmrR) and a glutathione synthetic enzyme (GshA).
    2. In a cysteine-free gamma-GCS that was non-functional, suppressor analysis yielded combinations of cysteine and aromatic residues at the position of the disulfide bond, and one mutant that lacked any cysteine residues.
      Title: Redox-dependent stability of the γ-glutamylcysteine synthetase enzyme of Escherichia coli: a novel means of redox regulation.
    3. gshA plays a role in E. coli resistance to distant UV irradiation and in regulation of SOS response.
      Title: [The role of thiol redox systems in response of Escherichia coli to distant UV irradiation].
    4. N-terminus verified by Edman degradation on complete protein
      Title: The nucleotide sequence of the gene for gamma-glutamylcysteine synthetase of Escherichia coli.
    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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glutamate-cysteine ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables glutamate-cysteine ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables glutamate-cysteine ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity, forming carbon-nitrogen bonds IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables metal ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    acts_upstream_of_or_within cellular response to arsenic-containing substance IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within cellular response to mercury ion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in glutathione biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in glutathione biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within glutathione biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    acts_upstream_of_or_within hyperosmotic response IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    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
    glutamate--cysteine ligase
    NP_417173.1

    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
      2814883..2816439 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417173.1 glutamate--cysteine ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417173.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9APJ6
      Conserved Domains (1) summary
      PRK02107
      Location:2 → 518
      PRK02107; glutamate--cysteine ligase; Provisional
    Nucleotide Protein
    Heading Accession and Version

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