A0A1I6D4J7 · A0A1I6D4J7_9FIRM

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.
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.

Miscellaneous

In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.

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 1/2.
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, site, active site.

TypeIDPosition(s)Description
Binding site88-95substrate
Site152Lowers pKa of active site Cys
Binding site155-157substrate
Binding site168-170substrate
Active site186Acyl-thioester intermediate
Binding site279[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site284[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site290[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site305[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site309[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site312[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site518[4Fe-4S] cluster 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular Functionlipoate synthase activity
Molecular Functionlipoyl(octanoyl) transferase activity
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Multifunctional fusion protein

Including 2 domains:

  • Recommended name
    Lipoyl synthase
  • EC number
  • Alternative names
    • Lip-syn
    • Lipoate synthase
    • Lipoic acid synthase
    • Sulfur insertion protein LipA
      (LS
      )
  • Recommended name
    Octanoyltransferase
  • EC number
  • Alternative names
    • Lipoate-protein ligase B
    • Lipoyl/octanoyl transferase
    • Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase

Gene names

    • Name
      lipA
    • Synonyms
      lipB
    • ORF names
      SAMN05660706_10587

Organism names

Accessions

  • Primary accession
    A0A1I6D4J7

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain43-225BPL/LPL catalytic
Domain291-507Radical SAM core

Sequence similarities

Belongs to the LipB family.
Belongs to the radical SAM superfamily. Lipoyl synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    525
  • Mass (Da)
    57,338
  • Last updated
    2017-11-22 v1
  • Checksum
    A6DBE0BCD4FD382F
MVQTLCDTVITKYQRALVIGLDTLAYPRALELQRRLQRLRIAGEMPDCMLCLEHPPTLTLGRAGGDTDILVSGERLAREGVEVYRVERGGGVTYHGPGQLVGYPIVDLNNYQRDVHLLVQNLEEVIIRALGAFGIKGRRKEGYPGVWVDEAKIASIGVAVSKWVTMHGFALNVDPQMSHFKLINPCGMQGVRMTSMRELLGRPVGVWEVKDRVIEEMAAVFRWAEVLPGTPAPVCKLLDELGVETPSSRPGWLGVQVPAPGVLGKMVGLLERGRLNTVCREARCPNVAECFGMGTATFMVLGDACTRNCRFCSVNSGPPREPDLAEPQSLAETVRELGLRHAVVTSVTRDDLPDGGAGHFARVISAVRRLCPGVTVEVLVPDFGGSEESLATVVAARPDILGHNLETVPRLYEKVRPGADYRRSLQLLASAKRLAPGMVTKSGIMVGLGEEPEEMLGVMDDLKKAGCDYVTIGQYLQPTPGHLPVQGFVTPAMFDWYREQCLLKGFRQADCGPLVRSSYHARPLA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FOYM01000005
EMBL· GenBank· DDBJ
SFR00365.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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