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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
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