A0A1I6D4J7 · A0A1I6D4J7_9FIRM
- ProteinMultifunctional fusion protein
- GenelipA
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids525 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
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
- L-lysyl-[protein] + octanoyl-[ACP] = H+ + holo-[ACP] + N6-octanoyl-L-lysyl-[protein]
- [[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]
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 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 88-95 | substrate | ||||
Sequence: RGGGVTYH | ||||||
Site | 152 | Lowers pKa of active site Cys | ||||
Sequence: K | ||||||
Binding site | 155-157 | substrate | ||||
Sequence: SIG | ||||||
Binding site | 168-170 | substrate | ||||
Sequence: GFA | ||||||
Active site | 186 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 279 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 284 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 290 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 305 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 309 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 312 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 518 | [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 | lipoyl(octanoyl) transferase activity | |
Molecular Function | metal ion binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMultifunctional fusion protein
Including 2 domains:
- Recommended nameLipoyl synthase
- EC number
- Alternative names
- Recommended nameOctanoyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Eubacteriales > Desulfallaceae > Desulfoscipio
Accessions
- Primary accessionA0A1I6D4J7
Proteomes
Subcellular Location
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 43-225 | BPL/LPL catalytic | ||||
Sequence: GEMPDCMLCLEHPPTLTLGRAGGDTDILVSGERLAREGVEVYRVERGGGVTYHGPGQLVGYPIVDLNNYQRDVHLLVQNLEEVIIRALGAFGIKGRRKEGYPGVWVDEAKIASIGVAVSKWVTMHGFALNVDPQMSHFKLINPCGMQGVRMTSMRELLGRPVGVWEVKDRVIEEMAAVFRWAE | ||||||
Domain | 291-507 | Radical SAM core | ||||
Sequence: FGMGTATFMVLGDACTRNCRFCSVNSGPPREPDLAEPQSLAETVRELGLRHAVVTSVTRDDLPDGGAGHFARVISAVRRLCPGVTVEVLVPDFGGSEESLATVVAARPDILGHNLETVPRLYEKVRPGADYRRSLQLLASAKRLAPGMVTKSGIMVGLGEEPEEMLGVMDDLKKAGCDYVTIGQYLQPTPGHLPVQGFVTPAMFDWYREQCLLKGFR |
Sequence similarities
Belongs to the LipB family.
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length525
- Mass (Da)57,338
- Last updated2017-11-22 v1
- ChecksumA6DBE0BCD4FD382F
Keywords
- Technical term