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D1PTB8 · D1PTB8_9BACT

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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.
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 site363[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site368[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site374[4Fe-4S] cluster 1 (UniProtKB | ChEBI)
Binding site389[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site393[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site396[4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet
Binding site600[4Fe-4S] cluster 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular Function4 iron, 4 sulfur cluster binding
Molecular FunctionATP binding
Molecular Functionlipoate synthase activity
Molecular Functionlipoate-protein ligase activity
Molecular Functionmetal ion binding
Biological Processprotein lipoylation

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
    • ORF names
      HMPREF0645_0203

Organism names

  • Taxonomic identifier
  • Strain
    • DSM 17361
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Prevotellaceae > Hallella

Accessions

  • Primary accession
    D1PTB8

Proteomes

Subcellular Location

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain29-202BPL/LPL catalytic
Domain375-589Radical SAM core

Sequence similarities

Belongs to the radical SAM superfamily. Lipoyl synthase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    608
  • Mass (Da)
    68,770
  • Last updated
    2010-02-09 v1
  • MD5 Checksum
    D423A16B4712436C14E844DF2F27F3C6
MKYIHIPHPETIRTLPFYFAVEEYVARHYTDDDYFMVWRVEPTVMLGRNQLIENEVNTAYCQENDVHIFRRKSGGGCIYSDLGCIQFSYISSADNVNQAFARYMQRVADMLQSLGVDARLSGRNDILVNGGKVAGSAFYGLPNRCVLHNSMLFNTRLEHLSQSLTPSHEKLQSKGVASVSQRVNNIAPHTRLTIEDFMAYARRYMCGEASRMLSETDMEGIAKIERELASDSFVYGKNPKYSEVRKHRFEGVGTLEAHIELKNGVIVNISLSGDYFQLGDIDRHLLAPLRGVEFSREAVERRLRGTDLSTMIRALTLQQFLRLLFGRKPHVMKPDWLKIDLTAKKQTGETAEILAKHHLNTICTSGLCPNRAECWMARTATLMIGGNICTRRCRFCNTPSGRPELLDPDEPRRVAESIRSLGLRYAVITSVDRDDLSDYGAAHWIRTVEEVRALNPNTKIELLIPDFMGDANLIRRVMDTRPHVTGHNIETVRRLTPSVRSVARYERSLEVLREITRCGITAKTGFMLGLGETHEEVLETMDDILATGCRRLTIGQYLQPTAAHLPVVAYIPPQQFADYKKIALTKGFEHVESGPLVRSSYHAADAEA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACKS01000014
EMBL· GenBank· DDBJ
EFA45342.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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