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    lplA lipoate--protein ligase A [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944865, updated on 3-Dec-2024

    Summary

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    Official Symbol
    lplA
    Official Full Name
    lipoate--protein ligase A
    Primary source
    ECOCYC:EG11796
    Locus tag
    b4386
    See related
    ASAP:ABE-0014385
    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
    ECK4378; slr; yjjF
    Summary
    LplA first activates lipoic acid with ATP to form lipoyl-AMP. [More information is available at EcoGene: EG11796]. LplA is a lipoyl-protein ligase that preferentially utilizes lipoate imported from outside the cell, in contrast to the other lipoyl-protein ligase, LipB, which utilizes octanoyl-ACP . [More information is available at EcoCyc: EG11796].
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    Genomic context

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    Sequence:
    NC_000913.3 (4623101..4624117, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene purine nucleoside phosphorylase Neighboring gene toxin YjjJ Neighboring gene putative inner membrane protein Smp Neighboring gene phosphoserine phosphatase

    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. Purification and properties of the lipoate protein ligase of Escherichia coli. Green DE, et al. Biochem J, 1995 Aug 1. PMID 7639702, Free PMC Article
    2. Structure and selectivity in post-translational modification: attaching the biotinyl-lysine and lipoyl-lysine swinging arms in multifunctional enzymes. Reche P, et al. EMBO J, 1999 May 17. PMID 10329614, Free PMC Article
    3. Activation and competition of lipoylation of H protein and its hydrolysis in a reaction cascade catalyzed by the multifunctional enzyme lipoate-protein ligase A. Zhang X, et al. Biotechnol Bioeng, 2020 Dec. PMID 32749694
    4. Lipoic acid content of Escherichia coli and other microorganisms. Herbert AA, et al. Arch Microbiol, 1975 Dec 31. PMID 814874
    5. Use of trypsin and lipoamidase to study the role of lipoic acid moieties in the pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli. Stepp LR, et al. Biochemistry, 1981 Aug 4. PMID 6794598

    See all (26) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Activation and competition of lipoylation of H protein and its hydrolysis in a reaction cascade catalyzed by the multifunctional enzyme lipoate-protein ligase A.
      Title: Activation and competition of lipoylation of H protein and its hydrolysis in a reaction cascade catalyzed by the multifunctional enzyme lipoate-protein ligase A.
    2. analysis of the conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A
      Title: Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A.
    3. N-terminus verified by Edman degradation on mature peptide
      Title: Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product.
    Submit: New GeneRIF Correction

    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 lipoate-protein ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables lipoate-protein ligase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables lipoate-protein ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lipoate-protein ligase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables lipoyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables lipoyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in protein lipoylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    is_active_in cytoplasm IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    lipoate--protein ligase A
    NP_418803.1

    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
      4623101..4624117 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_418803.1 lipoate--protein ligase A [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_418803.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A3L5GXP8
      Conserved Domains (1) summary
      PRK03822
      Location:1 → 338
      lplA; lipoate-protein ligase A; Provisional
    Nucleotide Protein
    Heading Accession and Version

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