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Q8IEG9 · LIPLA_PLAF7

Function

function

Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes (PubMed:17244193, PubMed:25116855, PubMed:28543853).
In the mitochondrion, functions as a redox switch between two lipoylation routes (PubMed:25116855).
Senses the oxidation state of lipoate and determines which downstream enzymes will be lipoylated (PubMed:25116855).
In low reducing conditions, uses lipoate in its oxidized ring form to lipoylate glycine cleavage system H-protein GCVH (PubMed:17244193, PubMed:25116855, PubMed:28543853).
In high reducing conditions and together with LipL2, uses reduced lipoate (dihydrolipoate) to lipoylate the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha-ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction (PubMed:17244193, PubMed:25116855).

Catalytic activity

Activity regulation

Inhibited by the lipoate analog 8-bromo-octanoate (BrO) (PubMed:17244193).
Catalytic activity is increased in the presence of Mg2+ (PubMed:17244193).

Pathway

Protein modification; protein lipoylation via exogenous pathway; protein N6-(lipoyl)lysine from lipoate: step 1/2.
Protein modification; protein lipoylation via exogenous pathway; protein N6-(lipoyl)lysine from lipoate: step 2/2.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site102ATP (UniProtKB | ChEBI)
Binding site107(R)-lipoate (UniProtKB | ChEBI)
Binding site107ATP (UniProtKB | ChEBI)
Binding site110ATP (UniProtKB | ChEBI)
Binding site153Mg2+ (UniProtKB | ChEBI)
Binding site160(R)-lipoate (UniProtKB | ChEBI)
Binding site160ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentmitochondrion
Molecular FunctionATP binding
Molecular Functionlipoate-protein ligase activity
Molecular Functionlipoyltransferase activity
Molecular Functionmetal ion binding
Biological Processlipid metabolic process
Biological Processprotein lipoylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipoate--protein ligase 1
  • EC number

Gene names

    • Name
      LipL1
    • Synonyms
      LplA
      , LplA1
    • ORF names
      PF3D7_1314600

Organism names

  • Taxonomic identifier
  • Strain
    • 3D7
  • Taxonomic lineage
    Eukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)

Accessions

  • Primary accession
    Q8IEG9

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis160Loses the ability to form the reaction intermediate lipoyl-AMP resulting in a loss of catalytic activity. Abolishes lipoylation of GCVH/H-protein. Abolishes lipoylation of BCKDH-E2/BCDH and KDH in the presence of LipL2.

PTM/Processing

Features

Showing features for transit peptide, chain.

Type
IDPosition(s)Description
Transit peptide1-18Mitochondrion
ChainPRO_000045665119-408Lipoate--protein ligase 1

Proteomic databases

Expression

Developmental stage

Expressed during the asexual blood stage, predominantly at the ring and schizont stages (at protein level).

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain60-242BPL/LPL catalytic

Sequence similarities

Belongs to the LplA family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    408
  • Mass (Da)
    47,943
  • Last updated
    2003-03-01 v1
  • MD5 Checksum
    60240A052ECCCB83802CA6314AA5C4BC
MKRIFRLVRRCHYSTEKRTNGPLVLVSNNQNIHFNLSLENFLLNNYNDLLKYLNINTIEKFNEPILFLWRNNRSIIIGKNQNIWSECNLKNIKEDGVLVARRFTGGGAVYHDLGNVCFTFLNNNINTSSNFLIILNTLKNHFNIEAKTQGRNDITVNDQKCSGSAFKKIKDVFLHHGTILINLEKNILNKYLTPDKIKYIKHGVSSVNARTINLSEINNNITCENLCIALIKEFTKFYEQNYKENINNIKNLENNINNSNFQNKEQININNTNENNLINNTNIIPNDITVHYIDQNNNITKNPEFLKYYNLLKDWDWCYGKTPKFQNHIWKQFTFGKLELFFNVSNGFIKDGNIFSDCLDINLIDHLKSIFNNDIKYSKEDISIFFKKLNVENKNYLDEVRSWILQEL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL844509
EMBL· GenBank· DDBJ
CAD52290.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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