Q9HKT1 · LPLAN_THEAC
- ProteinLipoate-protein ligase A subunit 1
- GenelplA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids262 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Part of a lipoate-protein ligase complex that 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. Can also use octanoate as substrate.
Miscellaneous
In contrast to E.coli, where the lipoate-protein ligase is encoded by a single gene product (LplA) with a large N-terminal domain and a small C-terminal domain, the same activity in T.acidophilum is dependent on two separate proteins, corresponding to the two domains of E.coli LplA, respectively.
Catalytic activity
- (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = AMP + diphosphate + H+ + N6-[(R)-lipoyl]-L-lysyl-[lipoyl-carrier protein]
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 | 72 | ATP (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 77 | ATP (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 80 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 85 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 132 | ATP (UniProtKB | ChEBI) | ||||
Sequence: P | ||||||
Binding site | 135 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 137 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 138 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 145 | (R)-lipoate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 145 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 149 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 149 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: A | ||||||
Binding site | 163 | ATP (UniProtKB | ChEBI) | ||||
Sequence: A |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | protein-containing complex | |
Molecular Function | ATP binding | |
Molecular Function | lipoate-protein ligase activity | |
Molecular Function | lipoic acid binding | |
Molecular Function | metal ion binding | |
Biological Process | protein lipoylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameLipoate-protein ligase A subunit 1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageArchaea > Candidatus Thermoplasmatota > Thermoplasmata > Thermoplasmatales > Thermoplasmataceae > Thermoplasma
Accessions
- Primary accessionQ9HKT1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000209571 | 1-262 | Lipoate-protein ligase A subunit 1 | |||
Sequence: MEGRLLLLETPGNTRMSLAYDEAIYRSFQYGDKPILRFYRHDRSVIIGYFQVAEEEVDLDYMKKNGIMLARRYTGGGAVYHDLGDLNFSVVRSSDDMDITSMFRTMNEAVVNSLRILGLDARPGELNDVSIPVNKKTDIMAGEKKIMGAAGAMRKGAKLWHAAMLVHTDLDMLSAVLKVPDEKFRDKIAKSTRERVANVTDFVDVSIDEVRNALIRGFSETLHIDFREDTITEKEESLARELFDKKYSTEEWNMGLLRKEVV |
Proteomic databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 30-226 | BPL/LPL catalytic | ||||
Sequence: YGDKPILRFYRHDRSVIIGYFQVAEEEVDLDYMKKNGIMLARRYTGGGAVYHDLGDLNFSVVRSSDDMDITSMFRTMNEAVVNSLRILGLDARPGELNDVSIPVNKKTDIMAGEKKIMGAAGAMRKGAKLWHAAMLVHTDLDMLSAVLKVPDEKFRDKIAKSTRERVANVTDFVDVSIDEVRNALIRGFSETLHIDF |
Sequence similarities
Belongs to the LplA family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length262
- Mass (Da)29,872
- Last updated2001-03-01 v1
- ChecksumCDF95B791BAD93A2
Mass Spectrometry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL445064 EMBL· GenBank· DDBJ | CAC11654.1 EMBL· GenBank· DDBJ | Genomic DNA |