O84562 · LIPA_CHLTR

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 site47[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site52[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site58[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site73[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site77[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site80[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site286[4Fe-4S] cluster 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
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
  • EC number
  • Alternative names
    • Lip-syn
      (LS
      )
    • Lipoate synthase
    • Lipoic acid synthase
    • Sulfur insertion protein LipA

Gene names

    • Name
      lipA
    • Ordered locus names
      CT_558

Organism names

Accessions

  • Primary accession
    O84562

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001023061-311Lipoyl synthase

Interaction

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain59-276Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    311
  • Mass (Da)
    34,661
  • Last updated
    1998-11-01 v1
  • Checksum
    0B613421B1F330DB
MTDSESPIPKKSIPARFPKWLRQKLPLGRVFAQTDNTIKNKGLPTVCEEASCPNRTHCWSRHTATYLALGDACTRRCGFCDIDFTRNPLPPDPEEGAKIAESAKALGLKHIVITMVSRDDLEDGGASALVHIIETLHTELPTATIEVLASDFEGNIAALHHLLDAHIAIYNHNVETVERLTPFVRHKATYRRSLMMLENAAKYLPNLMTKSGIMVGLGEQESEVKQTLKDLADHGVKIVTIGQYLRPSRRHIPVKSYVSPETFDYYRSVGESLGLFIYAGPFVRSSFNADSVFEAMRQRETSTSALLPNKD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE001273
EMBL· GenBank· DDBJ
AAC68160.1
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