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    tpx lipid hydroperoxide peroxidase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945880, updated on 17-Dec-2024

    Summary

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    Official Symbol
    tpx
    Official Full Name
    lipid hydroperoxide peroxidase
    Primary source
    ECOCYC:G6660
    Locus tag
    b1324
    See related
    ASAP:ABE-0004442
    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
    ECK1320; yzzJ
    Summary
    Binds TrxA (Kumar, 2004). although initially reported to be a periplasmic enzyme, the formation of a mixed-disulfide complex with TrxA indicates a cytoplasmic localization (Tao, 2008). [More information is available at EcoGene: EG12672]. Tpx is a |FRAME: [More information is available at EcoCyc: G6660].
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    Genomic context

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    Sequence:
    NC_000913.3 (1388305..1388811, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene DUF463 domain-containing protein YcjX Neighboring gene DUF697 domain-containing inner membrane protein YcjF Neighboring gene DNA-binding transcriptional dual regulator TyrR Neighboring gene L-Ala-D/L-Glu epimerase Neighboring gene murein tripeptide amidase A Neighboring gene putative uncharacterized protein YmjC

    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. The structure of an orthorhombic crystal form of a 'forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag. Beckham KS, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2012 May 1. PMID 22691780, Free PMC Article
    2. Identification of promoter in the 5'-flanking region of the E. coli thioredoxin-linked thiol peroxidase gene: evidence for the existence of oxygen-related transcriptional regulatory protein. Kim HK, et al. Biochem Biophys Res Commun, 1996 Apr 25. PMID 8630014
    3. Structural changes common to catalysis in the Tpx peroxiredoxin subfamily. Hall A, et al. J Mol Biol, 2009 Nov 6. PMID 19699750, Free PMC Article
    4. The dual functions of thiol-based peroxidases in H2O2 scavenging and signaling. Fourquet S, et al. Antioxid Redox Signal, 2008 Sep. PMID 18498222
    5. Bacterial scavengase p20 is structurally and functionally related to peroxiredoxins. Zhou Y, et al. Biochem Biophys Res Commun, 1997 Apr 28. PMID 9168946

    See all (34) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Structural alignments revealed that Tpx is conserved
      Title: The structure of an orthorhombic crystal form of a 'forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag.
    2. Results describe in detail the structural changes associated with catalysis in the thiol peroxidase subfamily.
      Title: Structural changes common to catalysis in the Tpx peroxiredoxin subfamily.
    3. N-terminus verified by Edman degradation on mature peptide
      Title: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.
    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 hydroperoxide reductase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peroxidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables thioredoxin peroxidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables thioredoxin peroxidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables thioredoxin-dependent peroxiredoxin activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cellular oxidant detoxification IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within cellular response to oxidative stress IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in periplasmic space IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    lipid hydroperoxide peroxidase
    NP_415840.1

    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
      1388305..1388811 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415840.1 lipid hydroperoxide peroxidase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415840.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9AMQ6, A0A8S7BD52
      Conserved Domains (1) summary
      PRK00522
      Location:2 → 168
      tpx; thiol peroxidase
    Nucleotide Protein
    Heading Accession and Version

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