C5PIN8 · LIPA_COCP7

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 site136[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site141[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site147[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site167[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site171[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site174[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site382[4Fe-4S] cluster 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentmitochondrion
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, mitochondrial
  • EC number
  • Alternative names
    • Lipoate synthase
      (LS
      ; Lip-syn
      )
    • Lipoic acid synthase

Gene names

    • ORF names
      CPC735_057610

Organism names

Accessions

  • Primary accession
    C5PIN8

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for transit peptide, chain.

TypeIDPosition(s)Description
Transit peptide1-26Mitochondrion
ChainPRO_000039826327-419Lipoyl synthase, mitochondrial

Structure

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias28-52Polar residues
Region28-61Disordered
Domain150-371Radical SAM core
Region399-419Disordered

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
    419
  • Mass (Da)
    45,766
  • Last updated
    2009-09-01 v1
  • Checksum
    E41CAE42605B6DEF
MAVCAGRLKCFGNPAVSLRTAASRAYATTTSPDPAIPSSSSASSSSALPKRPQTSFRDKLNAGPSFSDFLSGGNRDDARILDPNEAYALKTALVGPKGKKKEITRLPSWLKTSIPDSNNYKRIKNDLRGLGLHTVCEEARCPNISECWGGSSKSAATATIMLMGDTCTRACRFCSVKTSKTPPPLDPHEPENTAEALSRWGLGYVVLTTVDRDDLIDGGARHFAETVIRIKQKAPNILVECLTGDYAGDLEMVALMAKSGLDVYAHNVETVEALTPHVRDRRANFQTSLRVLKAAKAAVPSLITKTSMMLGLGETEEQMWDALRQLRAANVDVVTFGQYMRPTKRHMPVHEYVRPDVFELWKDRALEMGFLYCASGPLVRSSYKAGEAFIENVLKKRRAESTGPESTNVPNVTPDAIVR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias28-52Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACFW01000049
EMBL· GenBank· DDBJ
EER24391.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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