U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

yghU disulfide reductase/organic hydroperoxide reductase [ Escherichia coli str. K-12 substr. MG1655 ]

Gene ID: 947472, updated on 2-May-2024

Summary

Go to the top of the page Help
Gene symbol
yghU
Gene description
disulfide reductase/organic hydroperoxide reductase
Primary source
ASAP:ABE-0009812
Locus tag
b2989
See related
ECOCYC:G7553
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
ECK2983
Summary
YghU is one of eight glutathione transferase homologs in Escherichia coli . [More information is available at EcoCyc: G7553].
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 (3138727..3139593)

NC_000913.3Genomic Context describing neighboring genes Neighboring gene metal phosphate:H(+) symporter PitB Neighboring gene fused glutathionylspermidine amidase/glutathionylspermidine synthetase Neighboring gene hydrogenase maturation factor HybG Neighboring gene hydrogenase maturation protein HybF Neighboring gene hydrogenase 2-specific chaperone

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. Structure and function of YghU, a nu-class glutathione transferase related to YfcG from Escherichia coli. Stourman NV, et al. Biochemistry, 2011 Feb 22. PMID 21222452, Free PMC Article
  2. Three distinct-type glutathione S-transferases from Escherichia coli important for defense against oxidative stress. Kanai T, et al. J Biochem, 2006 Nov. PMID 17018556
  3. From the genome sequence to the proteome and back: evaluation of E. coli genome annotation with a 2-D gel-based proteomics approach. Maillet I, et al. Proteomics, 2007 Apr. PMID 17366475
  4. Conserved structural elements in glutathione transferase homologues encoded in the genome of Escherichia coli. Rife CL, et al. Proteins, 2003 Dec 1. PMID 14635120
  5. Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Hayashi K, et al. Mol Syst Biol, 2006. PMID 16738553, Free PMC Article

See all (7) citations in PubMed

GeneRIFs: Gene References Into Functions

General gene information

Go to the top of the page Help

Gene Ontology Provided by EcoCyc

Function Evidence Code Pubs
enables disulfide oxidoreductase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables peroxidase activity IEA
Inferred from Electronic Annotation
more info
  
enables protein homodimerization activity IDA
Inferred from Direct Assay
more info
 PubMed 
Process Evidence Code Pubs
involved_in cellular oxidant detoxification IEA
Inferred from Electronic Annotation
more info
  

General protein information

Go to the top of the page Help
Preferred Names
disulfide reductase/organic hydroperoxide reductase

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
    3138727..3139593
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NP_417463.4 disulfide reductase/organic hydroperoxide reductase [Escherichia coli str. K-12 substr. MG1655]

    See identical proteins and their annotated locations for NP_417463.4

    Status: PROVISIONAL

    UniProtKB/TrEMBL
    A0A8S7F9J5
    Conserved Domains (1) summary
    PRK11752
    Location:1 → 264
    PRK11752; putative S-transferase; Provisional
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.