Reviewed,
UniProtKB/Swiss-Prot Q9Y9E6 (LPLA_AERPE)
Last modified
June 16, 2009.
Version 50.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Putative lipoate-protein ligase A Short name=Lipoate--protein ligase EC=2.7.7.63 | ||||||
| Gene names |
| ||||||
| Organism | Aeropyrum pernix [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 56636 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Desulfurococcales › Desulfurococcaceae › Aeropyrum |
Protein attributes
| Sequence length | 264 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| 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 By similarity. |
| Catalytic activity | ATP + lipoate = diphosphate + lipoyl-AMP. Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. |
| Pathway | |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| 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 By similarity. |
| Sequence similarities | Belongs to the lplA family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | protein modification process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 264 | 264 | Putative lipoate-protein ligase A | PRO_0000062902 | |||||
Regions | |||||||||
| Nucleotide binding | 73 – 76 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 68 | 1 | ATP By similarity | ||||||
| Binding site | 130 | 1 | ATP By similarity | ||||||
| Binding site | 130 | 1 | Lipoate By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon, Aeropyrum pernix K1." Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K., Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S. Kikuchi H.DNA Res. 6:83-101(1999) [PubMed: 10382966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K1. |
Cross-references
Sequence databases | |
|---|---|
| BA000002 Genomic DNA. Translation: BAA81354.1. | |
| PIR | B72462. |
| RefSeq | NP_148553.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1445362. |
| GenomeReviews | Gene locus APE_2341 in contig BA000002_GR. |
| KEGG | ape:APE_2341. |
| NMPDR | fig|272557.1.peg.1661. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q9Y9E6. |
| OMA | Q9Y9E6. NSLERIT. |
Enzyme and pathway databases | |
| BRENDA | 2.7.7.63. 256344. |
Family and domain databases | |
| InterPro | IPR004143. BPL_LipA_LipB. [Graphical view] |
| Pfam | PF03099. BPL_LipA_LipB. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LPLA_AERPE | ||||||||
| Accession | Primary (citable) accession number: Q9Y9E6 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


