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    prpE propionyl-CoA synthetase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946891, updated on 3-Dec-2024

    Summary

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    Official Symbol
    prpE
    Official Full Name
    propionyl-CoA synthetase
    Primary source
    ECOCYC:G6200
    Locus tag
    b0335
    See related
    ASAP:ABE-0001154
    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
    ECK0332; yahU
    Summary
    Crp regulon. [More information is available at EcoGene: EG13604]. Acs appears to be more likely than PrpE to catalyze the first step in the propionate metabolism pathway . [More information is available at EcoCyc: G6200].
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    Genomic context

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    Sequence:
    NC_000913.3 (352706..354592)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene 2-methylcitrate synthase Neighboring gene 2-methylcitrate dehydratase Neighboring gene cytosine transporter Neighboring gene cytosine/isoguanine deaminase Neighboring gene DNA-binding transcriptional dual regulator CynR

    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. E. coli propionyl-CoA synthetase is regulated in vitro by an intramolecular disulfide bond. Guo Y, et al. Prikl Biokhim Mikrobiol, 2012 May-Jun. PMID 22834299
    2. The prpE gene of Salmonella typhimurium LT2 encodes propionyl-CoA synthetase. Horswill AR, et al. Microbiology (Reading), 1999 Jun. PMID 10411265
    3. Salmonella typhimurium LT2 catabolizes propionate via the 2-methylcitric acid cycle. Horswill AR, et al. J Bacteriol, 1999 Sep. PMID 10482501, Free PMC Article
    4. Propionate oxidation in Escherichia coli: evidence for operation of a methylcitrate cycle in bacteria. Textor S, et al. Arch Microbiol, 1997 Nov. PMID 9325432
    5. Oxidation of propionate to pyruvate in Escherichia coli. Involvement of methylcitrate dehydratase and aconitase. Brock M, et al. Eur J Biochem, 2002 Dec. PMID 12473114

    See all (8) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Pathways from PubChem

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    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity, forming carbon-sulfur bonds IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables propionate-CoA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables propionate-CoA ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables propionate-CoA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in propionate catabolic process, 2-methylcitrate cycle IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    propionyl-CoA synthetase
    NP_414869.1

    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
      352706..354592
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414869.1 propionyl-CoA synthetase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414869.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A7H9SDU9
      Conserved Domains (1) summary
      PRK10524
      Location:1 → 628
      prpE; propionyl-CoA synthetase; Provisional
    Nucleotide Protein
    Heading Accession and Version

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