Q9HKT1 · LPLAN_THEAC

Function

function

Part of a lipoate-protein ligase complex that 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. Can also use octanoate as substrate.

Miscellaneous

In contrast to E.coli, where the lipoate-protein ligase is encoded by a single gene product (LplA) with a large N-terminal domain and a small C-terminal domain, the same activity in T.acidophilum is dependent on two separate proteins, corresponding to the two domains of E.coli LplA, respectively.

Catalytic activity

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 site72ATP (UniProtKB | ChEBI)
Binding site77ATP (UniProtKB | ChEBI)
Binding site80ATP (UniProtKB | ChEBI)
Binding site85ATP (UniProtKB | ChEBI)
Binding site132ATP (UniProtKB | ChEBI)
Binding site135ATP (UniProtKB | ChEBI)
Binding site137Mg2+ (UniProtKB | ChEBI)
Binding site138Mg2+ (UniProtKB | ChEBI)
Binding site145(R)-lipoate (UniProtKB | ChEBI)
Binding site145ATP (UniProtKB | ChEBI)
Binding site149ATP (UniProtKB | ChEBI)
Binding site149Mg2+ (UniProtKB | ChEBI)
Binding site163ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentprotein-containing complex
Molecular FunctionATP binding
Molecular Functionlipoate-protein ligase activity
Molecular Functionlipoic acid binding
Molecular Functionmetal ion binding
Biological Processprotein lipoylation

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipoate-protein ligase A subunit 1
  • EC number
  • Alternative names
    • Lipoate--protein ligase subunit 1

Gene names

    • Name
      lplA
    • Ordered locus names
      Ta0514

Organism names

Accessions

  • Primary accession
    Q9HKT1

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00002095711-262Lipoate-protein ligase A subunit 1

Proteomic databases

Interaction

Subunit

Heterodimer composed of LplA and LplB.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain30-226BPL/LPL catalytic

Sequence similarities

Belongs to the LplA family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    262
  • Mass (Da)
    29,872
  • Last updated
    2001-03-01 v1
  • Checksum
    CDF95B791BAD93A2
MEGRLLLLETPGNTRMSLAYDEAIYRSFQYGDKPILRFYRHDRSVIIGYFQVAEEEVDLDYMKKNGIMLARRYTGGGAVYHDLGDLNFSVVRSSDDMDITSMFRTMNEAVVNSLRILGLDARPGELNDVSIPVNKKTDIMAGEKKIMGAAGAMRKGAKLWHAAMLVHTDLDMLSAVLKVPDEKFRDKIAKSTRERVANVTDFVDVSIDEVRNALIRGFSETLHIDFREDTITEKEESLARELFDKKYSTEEWNMGLLRKEVV

Mass Spectrometry

Molecular mass is 29,872 Da. Determined by Electrospray.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL445064
EMBL· GenBank· DDBJ
CAC11654.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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