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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
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