Q8IDQ0 · LIPA_PLAF7
- ProteinLipoyl synthase, apicoplast
- GenelipA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids415 (go to sequence)
- Protein existenceEvidence at transcript level
- 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.
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 | 153 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 158 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 164 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 179 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 183 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 186 | [4Fe-4S] cluster 2 (UniProtKB | ChEBI); 4Fe-4S-S-AdoMet | ||||
Sequence: C | ||||||
Binding site | 394 | [4Fe-4S] cluster 1 (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | apicoplast | |
Cellular Component | mitochondrion | |
Molecular Function | 4 iron, 4 sulfur cluster binding | |
Molecular Function | lipoate synthase activity | |
Molecular Function | metal ion binding | |
Biological Process | lipoate biosynthetic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipoyl synthase, apicoplast
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8IDQ0
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MHFGIPSLFYLYILFSIIMRIKC | ||||||
Chain | PRO_0000398230 | 24-415 | Lipoyl synthase, apicoplast | |||
Sequence: VITKNLKKTKKRTCSYIPHGNMEKGIILNYIEKPNPAYLKRGKNKNKNKNKKGDIYKLRNVEILLYANRYVHEGNENFSSTTKKLLLTPKVGNKMPEGKKPDWFHVAAPTVAKYNKLKDDIKKLNLHTVCEEAQCPNIGECWNIGTATIMLLGDTCTRGCKFCSIKTSSNPLPPDINEPFNTAKAICEWNIDYVVLTSVDRDDLPDGGASHFAKTVELVKFSRPDILIECLVSDFQGNIDSVRKLAFSGLDVYAHNIETVKRLQKYVRDKRANYDQSLFVLKTAKEINPQLYTKTSIMLGLGETKEEVIQTMYDARKNNIDVITFGQYLRPTKNHLSIVQYISPQMFEYYKEEGLKMGFKYIASGPLVRSSYKAGEYFIKNLVNQRNKDKKN |
Proteomic databases
Expression
Developmental stage
Expressed maximally in the early stages and late stages of the parasite erythrocytic development.
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 165-383 | Radical SAM core | ||||
Sequence: WNIGTATIMLLGDTCTRGCKFCSIKTSSNPLPPDINEPFNTAKAICEWNIDYVVLTSVDRDDLPDGGASHFAKTVELVKFSRPDILIECLVSDFQGNIDSVRKLAFSGLDVYAHNIETVKRLQKYVRDKRANYDQSLFVLKTAKEINPQLYTKTSIMLGLGETKEEVIQTMYDARKNNIDVITFGQYLRPTKNHLSIVQYISPQMFEYYKEEGLKMGFK |
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.
- Length415
- Mass (Da)47,593
- Last updated2003-03-01 v1
- ChecksumFB6D7CE36D52E2C1
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL844509 EMBL· GenBank· DDBJ | CAD52569.1 EMBL· GenBank· DDBJ | Genomic DNA |