Reviewed,
UniProtKB/Swiss-Prot B5YY02 (ASNA_ECO5E)
Last modified
November 3, 2009.
Version 11.
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 | Escherichia coli O157:H7 (strain EC4115 / EHEC) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 444450 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 330 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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_1000129112 | |||
Sequences
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References
| [1] | "Complete genome sequence of Escherichia coli O157:H7 str. EC4115." Eppinger M., Sebastian Y., Ravel J. Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP001164 Genomic DNA. Translation: ACI38317.1. | |
| RefSeq | YP_002273272.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 6970332. |
| GenomeReviews | Gene locus ECH74115_5180 in contig CP001164_GR. |
| KEGG | ecf:ECH74115_5180. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | LNDNLNG. |
Family and domain databases | |
| HAMAP | MF_00555. [Tree] |
| InterPro | IPR006195. aa-tRNA-synth_II_cons-reg. 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_ECO5E | ||||||||
| Accession | Primary (citable) accession number: B5YY02 | ||||||||
| 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 |

Clusters with


