B3LQ66 · LPLA_YEAS1
- ProteinPutative lipoate-protein ligase A
- GeneAIM22
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids409 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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.
Miscellaneous
In the transfer reaction, the free carboxyl group of lipoic 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-[lipoyl-carrier protein] + (R)-lipoate + ATP = N6-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H+
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | mitochondrion | |
Molecular Function | ATP binding | |
Molecular Function | lipoate-protein ligase activity | |
Molecular Function | lipoyltransferase activity | |
Biological Process | protein lipoylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutative lipoate-protein ligase A
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionB3LQ66
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000377668 | 1-409 | Putative lipoate-protein ligase A | |||
Sequence: MSMMLSNWALSPRYVGQRNLIHCTTLFHTLTRWAKDADDKYHDINSMYENMFTPSNDNVSILQDEGKSDYDTTKTSSMQEDISAFNKDLYNFYNIGYAKQIMSASQLENIVKAKGRFVIQSLSTSPYYNLALENYVFKNTPRAKRGPDNCRLLFYINDRCAVIGKNQNLWQEVDLAKLKSKNFELLRRFSGGGTVLHDLGNVNYSYLTSREKFETKFFNKMIIKWLNSLNPELRLDLNERGDIIQDGFKISGSAYKIAGGKAYHHATMLLNADLEQFSGLLEPSLPNNMEWESSGVHSVKSKIKNVGIITPNQFIAVVSERFQKTFKVDGEIPIYYCDEFKSINDEIKDAMNTLQSEQWKYFSGPKFSVKIKDKGLTIKVEKGMIYDCDRNDLIGLEFKGFLENIDSYT |
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 146-330 | BPL/LPL catalytic | ||||
Sequence: GPDNCRLLFYINDRCAVIGKNQNLWQEVDLAKLKSKNFELLRRFSGGGTVLHDLGNVNYSYLTSREKFETKFFNKMIIKWLNSLNPELRLDLNERGDIIQDGFKISGSAYKIAGGKAYHHATMLLNADLEQFSGLLEPSLPNNMEWESSGVHSVKSKIKNVGIITPNQFIAVVSERFQKTFKVDG |
Sequence similarities
Belongs to the LplA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length409
- Mass (Da)47,032
- Last updated2008-09-02 v1
- ChecksumFEDFE85D4D17E0DC