A0A1R4FSV3 · A0A1R4FSV3_9ACTO
- ProteinMultifunctional fusion protein
- GenelipB
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids687 (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 | 70-77 | substrate | ||||
Sequence: RGGRITWH | ||||||
Site | 139 | Lowers pKa of active site Cys | ||||
Sequence: K | ||||||
Binding site | 142-144 | substrate | ||||
Sequence: AIG | ||||||
Binding site | 155-157 | substrate | ||||
Sequence: GIA | ||||||
Active site | 173 | Acyl-thioester intermediate | ||||
Sequence: C | ||||||
Binding site | 408 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 413 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 419 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 434 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 438 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 441 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 645 | [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
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Actinomycetales
Accessions
- Primary accessionA0A1R4FSV3
Proteomes
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 32-212 | BPL/LPL catalytic | ||||
Sequence: GTARDTLLVLEHEPVYTAGKRTARSDRPIDGSAVIDVDRGGRITWHGPGQIVVYPIVRLGEPVDVVAYVRALEDAVIDTCARLGLATTRVPGRTGVWVPGDENGPDRKICAIGVRVAKSVSMHGIALNVDPDLTAYDRIVPCGISDAGVTSLVKELGRELTLTEVADVLEAALSRHLAPLT | ||||||
Region | 317-370 | Disordered | ||||
Sequence: DAAEKAPASTEAAPAAQGANPATSDGEASSAPRSAVGEKLAPNGRKLLRLEKRN | ||||||
Domain | 420-634 | Radical SAM core | ||||
Sequence: WEDREATFLIGGSQCTRRCDFCQIDTGKPDAFDRAEPLKVASSVRRMGLKYATITGVARDDLDDGGAWLYAETVRQIKKMNPGTGVELLIPDFDAKPDQLAEVFSSRPEVLAHNVETVPRIFRRIRPGFRYDRSLSVIKSASEDGFVTKSNFMLGMGETFEEVVEALGMVREAGCDLITINQYMRPSLRHHPVERWVKPQEFVDLSTIAEELGYL | ||||||
Region | 667-687 | Disordered | ||||
Sequence: LMHLTEERSSRQEASSLLSRL |
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
- Length687
- Mass (Da)73,486
- Last updated2017-04-12 v1
- ChecksumC911272672AA145D
Keywords
- Technical term