A0A0B0N395 · A0A0B0N395_GOSAR
- ProteinLipoyl synthase, mitochondrial
- GeneLIP1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids377 (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] + 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]
RHEA-COMP:14568 CHEBI:33722 Position: ACHEBI:33722 Position: B+ RHEA-COMP:9928 + 2 RHEA-COMP:10000 + 2 CHEBI:59789 + 4 CHEBI:15378 = RHEA-COMP:14569 CHEBI:33722 Position: A+ RHEA-COMP:10475 + 4 CHEBI:29034 + 2 CHEBI:29919 + 2 CHEBI:17319 + 2 CHEBI:57844 + 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 | 109 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 114 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 120 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 140 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 144 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 147 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 356 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | lipoate synthase 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, mitochondrial
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Malvales > Malvaceae > Malvoideae > Gossypium
Accessions
- Primary accessionA0A0B0N395
Proteomes
Subcellular Location
Structure
Sequence
- Sequence statusComplete
- Length377
- Mass (Da)41,438
- Last updated2015-03-04 v1
- Checksum27255E8F12B2A4C5
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JRRC01468049 EMBL· GenBank· DDBJ | KHG07122.1 EMBL· GenBank· DDBJ | Genomic DNA |