D1PTB8 · D1PTB8_9BACT
- ProteinLipoyl synthase
- GenelipA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids608 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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
- L-lysyl-[lipoyl-carrier protein] + (R)-lipoate + ATP = N6-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H+
- [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S]2+ cluster] + N6-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine + 4 H+ = [[Fe-S] cluster scaffold protein] + N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 4 Fe3+ + 2 hydrogen sulfide + 2 5'-deoxyadenosine + 2 L-methionine + 2 reduced [2Fe-2S]-[ferredoxin]
Cofactor
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 363 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 368 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 374 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | |||
Binding site | 389 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 393 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 396 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | |||
Binding site | 600 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | ATP binding | |
Molecular Function | lipoate synthase activity | |
Molecular Function | lipoate-protein ligase activity | |
Molecular Function | metal ion binding | |
Biological Process | protein lipoylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipoyl synthase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Bacteroidia > Bacteroidales > Prevotellaceae > Hallella
Accessions
- Primary accessionD1PTB8
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 29-202 | BPL/LPL catalytic | |||
Domain | 375-589 | Radical SAM core | |||
Sequence similarities
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length608
- Mass (Da)68,770
- Last updated2010-02-09 v1
- MD5 ChecksumD423A16B4712436C14E844DF2F27F3C6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ACKS01000014 EMBL· GenBank· DDBJ | EFA45342.1 EMBL· GenBank· DDBJ | Genomic DNA |