Reviewed,
UniProtKB/Swiss-Prot Q9CKN6 (ASNA_PASMU)
Last modified
February 9, 2010.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aspartate--ammonia ligase EC=6.3.1.1 Alternative name(s): Asparagine synthetase A | ||||
| Gene names |
| ||||
| Organism | Pasteurella multocida [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 747 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Pasteurella |
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: HAMAP 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: HAMAP aminoacyl-tRNA ligase activityInferred from electronic annotation. Source: InterPro aspartate-ammonia ligase activityInferred from electronic annotation. Source: HAMAP |
| 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_0000195884 | |||
Sequences
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References
| [1] | "Complete genomic sequence of Pasteurella multocida Pm70." May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V. Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed: 11248100] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Pm70. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE004439 Genomic DNA. Translation: AAK03658.1. |
| RefSeq | NP_246513.1. |
3D structure databases | |
| SMR | Q9CKN6. Positions 4-330. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1244921. |
| GenomeReviews | Gene locus PM1574 in contig AE004439_GR. |
| KEGG | pmu:PM1574. |
| NMPDR | fig|272843.1.peg.1575. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG288146. |
| OMA | LNDNLNG. |
Enzyme and pathway databases | |
| BRENDA | 6.3.1.1. 258935. |
Family and domain databases | |
| HAMAP | MF_00555. AsnA. [Tree] |
| InterPro | IPR006195. aa-tRNA-synth_II_cons-dom. IPR004618. AsnA. [Graphical view] |
| 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_PASMU | ||||||||
| Accession | Primary (citable) accession number: Q9CKN6 | ||||||||
| Entry history |
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| 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 |

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