Q8IEG9 · LIPLA_PLAF7
- ProteinLipoate--protein ligase 1
- GeneLipL1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids408 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes (PubMed:17244193, PubMed:25116855, PubMed:28543853).
In the mitochondrion, functions as a redox switch between two lipoylation routes (PubMed:25116855).
Senses the oxidation state of lipoate and determines which downstream enzymes will be lipoylated (PubMed:25116855).
In low reducing conditions, uses lipoate in its oxidized ring form to lipoylate glycine cleavage system H-protein GCVH (PubMed:17244193, PubMed:25116855, PubMed:28543853).
In high reducing conditions and together with LipL2, uses reduced lipoate (dihydrolipoate) to lipoylate the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha-ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction (PubMed:17244193, PubMed:25116855).
In the mitochondrion, functions as a redox switch between two lipoylation routes (PubMed:25116855).
Senses the oxidation state of lipoate and determines which downstream enzymes will be lipoylated (PubMed:25116855).
In low reducing conditions, uses lipoate in its oxidized ring form to lipoylate glycine cleavage system H-protein GCVH (PubMed:17244193, PubMed:25116855, PubMed:28543853).
In high reducing conditions and together with LipL2, uses reduced lipoate (dihydrolipoate) to lipoylate the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha-ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction (PubMed:17244193, PubMed:25116855).
Catalytic activity
- L-lysyl-[lipoyl-carrier protein] + (R)-lipoate + ATP = N6-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H+
- (R)-dihydrolipoate + L-lysyl-[lipoyl-carrier protein] + ATP = N6-[(R)-dihydrolipoyl]-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H+
- (R)-dihydrolipoate + ATP + H+ = N6-[(R)-dihydrolipoyl]-5'-AMP + diphosphate
- N6-[(R)-dihydrolipoyl]-5'-AMP + L-lysyl-[lipoyl-carrier protein] = N6-[(R)-dihydrolipoyl]-L-lysyl-[lipoyl-carrier protein] + AMP + 2 H+
Activity regulation
Inhibited by the lipoate analog 8-bromo-octanoate (BrO) (PubMed:17244193).
Catalytic activity is increased in the presence of Mg2+ (PubMed:17244193).
Catalytic activity is increased in the presence of Mg2+ (PubMed:17244193).
Pathway
Protein modification; protein lipoylation via exogenous pathway; protein N6-(lipoyl)lysine from lipoate: step 1/2.
Protein modification; protein lipoylation via exogenous pathway; protein N6-(lipoyl)lysine from lipoate: step 2/2.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 102 | ATP (UniProtKB | ChEBI) | |||
Binding site | 107 | (R)-lipoate (UniProtKB | ChEBI) | |||
Binding site | 107 | ATP (UniProtKB | ChEBI) | |||
Binding site | 110 | ATP (UniProtKB | ChEBI) | |||
Binding site | 153 | Mg2+ (UniProtKB | ChEBI) | |||
Binding site | 160 | (R)-lipoate (UniProtKB | ChEBI) | |||
Binding site | 160 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | lipoate-protein ligase activity | |
Molecular Function | lipoyltransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | lipid metabolic process | |
Biological Process | protein lipoylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipoate--protein ligase 1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Laverania)
Accessions
- Primary accessionQ8IEG9
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 160 | Loses the ability to form the reaction intermediate lipoyl-AMP resulting in a loss of catalytic activity. Abolishes lipoylation of GCVH/H-protein. Abolishes lipoylation of BCKDH-E2/BCDH and KDH in the presence of LipL2. | |||
PTM/Processing
Features
Showing features for transit peptide, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transit peptide | 1-18 | Mitochondrion | |||
Chain | PRO_0000456651 | 19-408 | Lipoate--protein ligase 1 | ||
Proteomic databases
Expression
Developmental stage
Expressed during the asexual blood stage, predominantly at the ring and schizont stages (at protein level).
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length408
- Mass (Da)47,943
- Last updated2003-03-01 v1
- MD5 Checksum60240A052ECCCB83802CA6314AA5C4BC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL844509 EMBL· GenBank· DDBJ | CAD52290.1 EMBL· GenBank· DDBJ | Genomic DNA |