A0A2M6VP28 · A0A2M6VP28_9BURK
- ProteinLipoyl synthase
- GenelipA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids335 (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
- [[Fe-S] cluster scaffold protein carrying a second [4Fe-4S]2+ cluster] + 4 H+ + N6-octanoyl-L-lysyl-[protein] + 2 oxidized [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [[Fe-S] cluster scaffold protein] + 4 Fe3+ + 2 hydrogen sulfide + 2 L-methionine + N6-[(R)-dihydrolipoyl]-L-lysyl-[protein] + 2 reduced [2Fe-2S]-[ferredoxin]
RHEA-COMP:14568 CHEBI:33722 Position: ACHEBI:33722 Position: B+ 4 CHEBI:15378 + RHEA-COMP:9928 + 2 RHEA-COMP:10000 + 2 CHEBI:59789 = 2 CHEBI:17319 + RHEA-COMP:14569 CHEBI:33722 Position: A+ 4 CHEBI:29034 + 2 CHEBI:29919 + 2 CHEBI:57844 + RHEA-COMP:10475 + 2 RHEA-COMP:10001
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.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 78 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 83 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 89 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 104 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 108 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 111 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 318 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | lipoate synthase activity | |
Molecular Function | metal ion binding |
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 > Pseudomonadota > Betaproteobacteria > Burkholderiales > Comamonadaceae > Limnohabitans
Accessions
- Primary accessionA0A2M6VP28
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 89-307 | Radical SAM core | ||||
Sequence: CFGKGTATFMIMGDKCTRRCPFCDVGHGRPDPLDVNEPDNLAKTIAQLKLQYVVITSVDRDDLRDGGAGHFVECIRKTRELSPTTQIEVLVPDFRGRDDRALEILKAAPPDVMNHNMETVPRLYKEARPGSDYQFSLNLLKKFKALFPNVPTKSGLMVGLGETDEEIIEVMRDMRAHNIEMLTIGQYLAPSNSHLPVRRYVHPDTFKMFEAKAYEMGFS |
Sequence similarities
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length335
- Mass (Da)37,522
- Last updated2018-04-25 v1
- Checksum09E93BBE37717ACC