Q492U9 (LPLA_BLOPB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 43.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Lipoate-protein ligase A EC=2.7.7.63 Alternative name(s): Lipoate--protein ligase | ||||
| Gene names |
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| Organism | Blochmannia pennsylvanicus (strain BPEN) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 291272 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia |
Protein attributes
| Sequence length | 339 AA. |
| Sequence status | Complete. |
| 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. HAMAP MF_01602 |
| Catalytic activity | ATP + lipoate = diphosphate + lipoyl-AMP. HAMAP MF_01602 Lipoyl-AMP + protein = protein N(6)-(lipoyl)lysine + AMP. HAMAP MF_01602 |
| Pathway | Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2. HAMAP MF_01602 |
| Subunit structure | Monomer By similarity. HAMAP MF_01602 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01602. |
| 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. HAMAP MF_01602 |
| 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 | peptidyl-lysine lipoylation 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 lipoate-protein ligase activityInferred from electronic annotation. Source: InterPro 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 – 339 | 339 | Lipoate-protein ligase A HAMAP MF_01602 | PRO_0000311125 | |||||
Regions | |||||||||
| Nucleotide binding | 76 – 79 | 4 | ATP By similarity | ||||||
Sites | |||||||||
| Binding site | 71 | 1 | ATP By similarity | ||||||
| Binding site | 135 | 1 | ATP By similarity | ||||||
| Binding site | 135 | 1 | Lipoate By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Blochmannia pennsylvanicus indicates parallel evolutionary trends among bacterial mutualists of insects." Degnan P.H., Lazarus A.B., Wernegreen J.J. Genome Res. 15:1023-1033(2005) [PubMed: 16077009] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: BPEN. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000016 Genomic DNA. Translation: AAZ40993.1. |
| RefSeq | YP_277868.1. NC_007292.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1X2G based on UniProtKB P32099. |
| ProteinModelPortal | Q492U9. |
| SMR | Q492U9. Positions 3-338. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q492U9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 3563042. |
| GenomeReviews | Gene locus BPEN_368 in contig CP000016_GR. |
| KEGG | bpn:BPEN_368. |
| PATRIC | 31965637. VBICanBlo110049_0356. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0095. |
| HOGENOM | HBG715377. |
| OMA | YDRMENL. |
| PhylomeDB | Q492U9. |
| ProtClustDB | CLSK280831. |
Enzyme and pathway databases | |
| BioCyc | CBLO291272:BPEN_368-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01602. LplA. [Tree] |
| InterPro | IPR004143. BPL_LipA_LipB. IPR005107. CO_DH_flav_C. IPR023741. Lipoate_ligase_A. IPR019491. Lipoate_protein_ligase_C. IPR004562. LipoylTrfase_LipoateP_Ligase. [Graphical view] |
| Gene3D | G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. |
| KO | K03800. |
| Pfam | PF03099. BPL_LplA_LipB. 1 hit. PF10437. Lip_prot_lig_C. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00545. Lipoyltrans. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | LPLA_BLOPB | ||||||||
| Accession | Primary (citable) accession number: Q492U9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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