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

Gene ID: 946132, updated on 2-May-2024

Summary

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Gene symbol
poxB
Gene description
pyruvate oxidase
Primary source
ASAP:ABE-0002958
Locus tag
b0871
See related
ECOCYC:EG10754
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. Reaction mechanisms of thiamin diphosphate enzymes: redox reactions. Tittmann K. FEBS J, 2009 May. PMID 19476487
  2. Structural basis for membrane binding and catalytic activation of the peripheral membrane enzyme pyruvate oxidase from Escherichia coli. Neumann P, et al. Proc Natl Acad Sci U S A, 2008 Nov 11. PMID 18988747, Free PMC Article
  3. Crystallization and preliminary X-ray diffraction analysis of full-length and proteolytically activated pyruvate oxidase from Escherichia coli. Weidner A, et al. Acta Crystallogr Sect F Struct Biol Cryst Commun, 2008 Mar 1. PMID 18323602, Free PMC Article
  4. An Escherichia coli mutant deficient in pyruvate oxidase activity due to altered phospholipid activation of the enzyme. Chang YY, et al. Proc Natl Acad Sci U S A, 1984 Jul. PMID 16593486, Free PMC Article
  5. Role of pyruvate oxidase in Escherichia coli strains lacking the phosphoenolpyruvate:carbohydrate phosphotransferase system. Flores N, et al. J Mol Microbiol Biotechnol, 2004. PMID 16179798

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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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
    A0A377AVX4
    Conserved Domains (1) summary
    PRK09124
    Location:1 → 572
    PRK09124; ubiquinone-dependent pyruvate dehydrogenase
Nucleotide Protein
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