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    poxB pyruvate oxidase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946132, updated on 3-Dec-2024

    Summary

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    Official Symbol
    poxB
    Official Full Name
    pyruvate oxidase
    Primary source
    ECOCYC:EG10754
    Locus tag
    b0871
    See related
    ASAP:ABE-0002958
    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
    ECK0862
    Summary
    Metabolism of pyruvate via pyruvate oxidase is less efficient than the route via the pyruvate dehydrogenase multienzyme complex; however, the pyruvate oxidase route is important for wild-type growth efficiency and responsible for a significant amount of pyruvate metabolism under aerobic conditions . [More information is available at EcoCyc: EG10754].
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    Genomic context

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    Sequence:
    NC_000913.3 (909331..911049, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative NAD(P)-binding protein YbjT Neighboring gene low-specificity L-threonine aldolase Neighboring gene NADH oxidoreductase Neighboring gene protein S-nitrosylase

    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. Molecular cloning of the gene (poxB) encoding the pyruvate oxidase of Escherichia coli, a lipid-activated enzyme. Grabau C, et al. J Bacteriol, 1984 Dec. PMID 6209262, Free PMC Article
    2. Identification of the high-affinity lipid binding site in Escherichia coli pyruvate oxidase. Hamilton SE, et al. Biochemistry, 1986 Dec 16. PMID 3545288
    3. Reconstitution of the Ubiquinone-dependent pyruvate oxidase system of Escherichia coli with the cytochrome o terminal oxidase complex. Carter K, et al. J Biol Chem, 1985 Sep 15. PMID 3897227
    4. Characterization of the alpha-peptide released upon protease activation of pyruvate oxidase. Recny MA, et al. J Biol Chem, 1985 Nov 15. PMID 3902830
    5. Kinetic studies of the lipid-activated pyruvate oxidase flavoprotein of Escherichia coli. Mather MW, et al. J Biol Chem, 1985 Dec 25. PMID 3905808

    See all (79) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Deletion of the E. coli poxB gene (together with deletions of other ferementation disruption genes) increased production of succinate
      Title: Eliminating side products and increasing succinate yields in engineered strains of Escherichia coli C.
    2. N-terminus verified by Edman degradation on complete protein
      Title: Characterization of the alpha-peptide released upon protease activation of pyruvate oxidase.
    3. The dissociation of pyruvate oxidase caused by pressure revealed information about roles FAD and pyruvic acid play in stabilizing the enzyme, and about the physical separation of alpha-peptide
      Title: Exploration of pressure-induced dissociation of pyruvate oxidase.
    4. The results presented here strongly suggest that acetyl coenzyme A is mainly synthesized from acetate produced by pyruvate oxidase in strains with inactive phosphoenolpyruvate:carbohydrate phosphotransferase system
      Title: Role of pyruvate oxidase in Escherichia coli strains lacking the phosphoenolpyruvate:carbohydrate phosphotransferase system.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    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 flavin adenine dinucleotide binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables flavin adenine dinucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables lipid binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lipid binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidoreductase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables pyruvate dehydrogenase (quinone) activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables pyruvate dehydrogenase (quinone) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables thiamine pyrophosphate binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables thiamine pyrophosphate binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ubiquinone binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in carboxylic acid metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in pyruvate catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within pyruvate catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in pyruvate metabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within pyruvate metabolic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytosol HDA PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of protein-containing complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    pyruvate oxidase
    NP_415392.1

    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
      909331..911049 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415392.1 pyruvate oxidase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415392.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A376FNI8, A0A377AVX4
      Conserved Domains (1) summary
      PRK09124
      Location:1 → 572
      PRK09124; ubiquinone-dependent pyruvate dehydrogenase
    Nucleotide Protein
    Heading Accession and Version

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