A5K883 · LIPA_PLAVS

Function

function

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.

Catalytic activity

Cofactor

[4Fe-4S] cluster (UniProtKB | Rhea| CHEBI:49883 )

Note: Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.

Pathway

Protein modification; protein lipoylation via endogenous pathway; protein N6-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 2/2.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site177[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site182[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site188[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site203[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site207[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site210[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site418[4Fe-4S] cluster 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentapicoplast
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionlipoate synthase activity
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Lipoyl synthase, apicoplast
  • EC number
  • Alternative names
    • Lipoate synthase
      (LS
      ; Lip-syn
      )
    • Lipoic acid synthase

Gene names

    • Name
      lipA
    • ORF names
      PVX_083125

Organism names

Accessions

  • Primary accession
    A5K883

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-25
ChainPRO_000039823226-442Lipoyl synthase, apicoplast

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region92-154Disordered
Compositional bias115-131Basic and acidic residues
Compositional bias139-153Basic and acidic residues
Domain189-407Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase 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
    442
  • Mass (Da)
    50,317
  • Last updated
    2007-07-10 v1
  • Checksum
    0EFA968BB12F4E3F
MHVLTPSLYIYAFFIVCVRLKCGRSKRVANAKHATYDMPPKGLRVRDMLEKTAQQNCNQRKRGKCRKFFFLWKMDKMGDTHLGGQANGRKNLLRSESATDEASLGGNPLKEKLKESPANWGKDKQEEQQSTDRLPLPKVGNKMPEKKPDWFHVPAPTGKKYNELKADLKKLKLHTVCEEAQCPNIGECWNIGTATIMLLGDTCTRGCKFCSIKTSSKPLPPDANEPFNTAKAICEWDINYVVLTSVDRDDLPDGGASHFAKTIELIKFSRPEILIECLVSDFQGNVDSIRKLANSGMEVYAHNIETVRRLQKFVRDRRANYEQSLWVLKTAKEINPLLYTKTSIMLGLGETKQEVLQAMADVRQNNIDVITFGQYLRPTKNHLNVVEYVSPQMFDYYKEEGMKMGFKYIASGPLVRSSYKAGEYFMKNLVEQRRGVKLHAEG

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias115-131Basic and acidic residues
Compositional bias139-153Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AAKM01000009
EMBL· GenBank· DDBJ
EDL44497.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp