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grxA reduced glutaredoxin 1 [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 945479, updated on 19-Sep-2024

Summary

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Official Symbol
grxA
Official Full Name
reduced glutaredoxin 1
Primary source
ECOCYC:EG10417
Locus tag
b0849
See related
ASAP:ABE-0002893
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
ECK0840; grx
Summary
Glutaredoxins are ubiquitous proteins that catalyze the reduction of disulfides via reduced glutathione (GSH). [More information is available at EcoCyc: EG10417].
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Genomic context

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Sequence:
NC_000913.3 (890496..890753, complement)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative transport protein YbjL Neighboring gene putative inner membrane protein Neighboring gene DUF1418 domain-containing protein YbjC Neighboring gene NADPH-dependent nitro/quinone reductase NfsA Neighboring gene ribosomal protein S6 modification protein

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. NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. Xia TH, et al. Protein Sci, 1992 Mar. PMID 1304339, Free PMC Article
  2. Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803. Hosoya-Matsuda N, et al. J Biol Chem, 2005 Jan 7. PMID 15509585
  3. oxyR-dependent induction of Escherichia coli grx gene expression by peroxide stress. Tao K. J Bacteriol, 1997 Sep. PMID 9294462, Free PMC Article
  4. Comparison of backbone dynamics of reduced and oxidized Escherichia coli glutaredoxin-1 using 15N NMR relaxation measurements. Kelley JJ 3rd, et al. Biochemistry, 1997 Apr 22. PMID 9125525
  5. Insights into deglutathionylation reactions. Different intermediates in the glutaredoxin and protein disulfide isomerase catalyzed reactions are defined by the gamma-linkage present in glutathione. Peltoniemi MJ, et al. J Biol Chem, 2006 Nov 3. PMID 16956877

See all (44) citations in PubMed

GeneRIFs: Gene References Into Functions

What's a GeneRIF?
  1. grxA 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].
  2. N-terminus verified by Edman degradation on complete protein
    Title: The primary structure of Escherichia coli glutaredoxin. Distant homology with thioredoxins in a superfamily of small proteins with a redox-active cystine disulfide/cysteine dithiol.
  3. in contrast to the glutaredoxin-glutathione mixed disulfide intermediate, the only intermediate in the protein disulfide isomerases (PDI)-catalyzed reaction was PDI peptide mixed disulfide
    Title: Insights into deglutathionylation reactions. Different intermediates in the glutaredoxin and protein disulfide isomerase catalyzed reactions are defined by the gamma-linkage present in glutathione.
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 disulfide oxidoreductase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables electron transfer activity IEA
Inferred from Electronic Annotation
more info
  
enables glutathione disulfide oxidoreductase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables nucleotide binding IEA
Inferred from Electronic Annotation
more info
  
enables protein-disulfide reductase (glutathione) activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein-disulfide reductase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables protein-disulfide reductase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in cell redox homeostasis IEA
Inferred from Electronic Annotation
more info
  
involved_in cellular response to oxidative stress IBA
Inferred from Biological aspect of Ancestor
more info
  
acts_upstream_of_or_within cellular response to oxidative stress IEP
Inferred from Expression Pattern
more info
 PubMed 
acts_upstream_of_or_within cysteine biosynthetic process via S-sulfo-L-cysteine IGI
Inferred from Genetic Interaction
more info
 PubMed 
acts_upstream_of_or_within cysteine biosynthetic process via S-sulfo-L-cysteine IMP
Inferred from Mutant Phenotype
more info
 PubMed 
involved_in deoxyribonucleotide biosynthetic process IEA
Inferred from Electronic Annotation
more info
  
acts_upstream_of_or_within deoxyribonucleotide biosynthetic process IMP
Inferred from Mutant Phenotype
more info
 PubMed 
acts_upstream_of_or_within sulfate assimilation via adenylyl sulfate reduction IDA
Inferred from Direct Assay
more info
 PubMed 
acts_upstream_of_or_within sulfate assimilation via adenylyl sulfate reduction IMP
Inferred from Mutant Phenotype
more info
 PubMed 
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  

General protein information

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Preferred Names
reduced glutaredoxin 1
NP_415370.1

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
    890496..890753 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_415370.1 reduced glutaredoxin 1 [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_415370.1

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A6N8QUD5, A0A8T6BIS5
    Conserved Domains (1) summary
    PRK11200
    Location:1 → 84
    grxA; glutaredoxin 1; Provisional
Nucleotide Protein
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