B5FN47 (ASNA_SALDC) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 23.
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: Aspartate--ammonia ligase EC=6.3.1.1 Alternative name(s): Asparagine synthetase A | ||||
| Gene names |
| ||||
| Organism | Salmonella dublin (strain CT_02021853) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 439851 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › Salmonella dublin |
Protein attributes
| Sequence length | 330 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | ATP + L-aspartate + NH3 = AMP + diphosphate + L-asparagine. HAMAP MF_00555 |
| Pathway | Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1. HAMAP MF_00555 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00555. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Asparagine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW tRNA aminoacylation for protein translationInferred 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 aminoacyl-tRNA ligase activityInferred from electronic annotation. Source: InterPro aspartate-ammonia ligase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 330 | 330 | Aspartate--ammonia ligase HAMAP MF_00555 | PRO_1000129124 | |||
Sequences
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References
| [1] | "Complete genome of Salmonella dublin strain CT_02021853." Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT_02021853. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001144 Genomic DNA. Translation: ACH75436.1. |
| RefSeq | YP_002217825.1. NC_011205.1. |
3D structure databases | |
| ProteinModelPortal | B5FN47. |
| SMR | B5FN47. Positions 4-330. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B5FN47. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6872232. |
| GenomeReviews | Gene locus SeD_A4269 in contig CP001144_GR. |
| KEGG | sed:SeD_A4269. |
| PATRIC | 18496602. VBISalEnt111443_4203. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG288146. |
| OMA | LNDNLNG. |
| ProtClustDB | PRK05425. |
Family and domain databases | |
| HAMAP | MF_00555. AsnA. [Tree] |
| InterPro | IPR006195. aa-tRNA-synth_II. IPR004618. AsnA. [Graphical view] |
| KO | K01914. |
| Pfam | PF03590. AsnA. 1 hit. [Graphical view] |
| PIRSF | PIRSF001555. Asp_ammon_ligase. 1 hit. |
| TIGRFAMs | TIGR00669. AsnA. 1 hit. |
| PROSITE | PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASNA_SALDC | ||||||||
| Accession | Primary (citable) accession number: B5FN47 | ||||||||
| 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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