C5FZJ2 · LIPA_ARTOC
- ProteinLipoyl synthase, mitochondrial
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids410 (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 | 129 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 134 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 140 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 160 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 164 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 167 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 375 | [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 > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Arthrodermataceae > Microsporum
Accessions
- Primary accessionC5FZJ2
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-29 | Mitochondrion | ||||
Sequence: MASTTVCSAARIRVASSQVLRSIANTRTY | ||||||
Chain | PRO_0000398272 | 30-410 | Lipoyl synthase, mitochondrial | |||
Sequence: ATTSPESSIPETKPTAKRTPTTFKDKLNKGPSFSDFIGGATEPPLSPDEAYALKTALVGPAGKKKEITRLPSWLKTPIPDSSSYKKIKNDLRGLNLHTVCEEARCPNISECWGGGSKAAATATIMLMGDTCTRGCRFCSVKTSRTPPPLDPHEPENTAEALSRWGLGYVVLTAVDRDDLVDGGARHFAETVRRIKGKAPNILVECLTGDFSGDMEMVSLMAESGMDVFAHNVETVEALTPFVRDRRASFQQSLSVLRGAKAANPELITKTSLMLGLGETKEQVLDALKQLRASQVDVVTFGQYMRPTKRHMAVHEYVRPDVFDMWKEKAMEMGFLYCASGPLVRSSYKAGEAFIENVLKKRAKERIGGAVEDSVKGKDVLL |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 29-46 | Polar residues | ||||
Sequence: YATTSPESSIPETKPTAK | ||||||
Region | 29-49 | Disordered | ||||
Sequence: YATTSPESSIPETKPTAKRTP | ||||||
Domain | 143-364 | Radical SAM core | ||||
Sequence: GGSKAAATATIMLMGDTCTRGCRFCSVKTSRTPPPLDPHEPENTAEALSRWGLGYVVLTAVDRDDLVDGGARHFAETVRRIKGKAPNILVECLTGDFSGDMEMVSLMAESGMDVFAHNVETVEALTPFVRDRRASFQQSLSVLRGAKAANPELITKTSLMLGLGETKEQVLDALKQLRASQVDVVTFGQYMRPTKRHMAVHEYVRPDVFDMWKEKAMEMGFL |
Sequence similarities
Belongs to the radical SAM superfamily. Lipoyl synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length410
- Mass (Da)44,727
- Last updated2009-07-28 v1
- ChecksumB3FAF375C58B00DE
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 29-46 | Polar residues | ||||
Sequence: YATTSPESSIPETKPTAK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS995708 EMBL· GenBank· DDBJ | EEQ35295.1 EMBL· GenBank· DDBJ | Genomic DNA |