Q1LZA3 (ASNS_BOVIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 56.
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: Asparagine synthetase [glutamine-hydrolyzing] EC=6.3.5.4 Alternative name(s): Glutamine-dependent asparagine synthetase | ||
| Gene names |
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| Organism | Bos taurus (Bovine) [Reference proteome] | ||
| Taxonomic identifier | 9913 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos![]() |
Protein attributes
| Sequence length | 561 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Catalytic activity | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate. |
| Pathway | |
| Sequence similarities | Contains 1 asparagine synthetase domain. Contains 1 glutamine amidotransferase type-2 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Asparagine biosynthesis |
| Domain | Glutamine amidotransferase |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| PTM | Acetylation |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | L-asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic processInferred from electronic annotation. Source: Compara positive regulation of mitotic cell cycleInferred from electronic annotation. Source: Compara |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW asparagine synthase (glutamine-hydrolyzing) 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 – 561 | 561 | Asparagine synthetase [glutamine-hydrolyzing] | PRO_0000269563 | |||||
Regions | |||||||||
| Domain | 2 – 191 | 190 | Glutamine amidotransferase type-2 | ||||||
| Domain | 213 – 536 | 324 | Asparagine synthetase | ||||||
| Nucleotide binding | 363 – 364 | 2 | ATP By similarity | ||||||
| Region | 49 – 53 | 5 | Glutamine binding By similarity | ||||||
| Region | 75 – 77 | 3 | Glutamine binding By similarity | ||||||
Sites | |||||||||
| Active site | 2 | 1 | For GATase activity By similarity | ||||||
| Binding site | 97 | 1 | Glutamine By similarity | ||||||
| Binding site | 256 | 1 | ATP; via carbonyl oxygen By similarity | ||||||
| Binding site | 288 | 1 | ATP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Site | 365 | 1 | Important for beta-aspartyl-AMP intermediate formation By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 385 | 1 | N6-acetyllysine By similarity | ||||||
Sequences
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References
| [1] | NIH - Mammalian Gene Collection (MGC) project Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Ascending colon. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC116123 mRNA. Translation: AAI16124.1. |
| IPI | IPI00716331. |
| RefSeq | NP_001069121.1. NM_001075653.1. |
| UniGene | Bt.61275. |
3D structure databases | |
| ProteinModelPortal | Q1LZA3. |
| ModBase | Search... |
Proteomic databases | |
| PaxDb | Q1LZA3. |
| PRIDE | Q1LZA3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSBTAT00000004181; ENSBTAP00000004181; ENSBTAG00000003222. |
| GeneID | 514209. |
| KEGG | bta:514209. |
Organism-specific databases | |
| CTD | 440. |
Phylogenomic databases | |
| eggNOG | COG0367. |
| GeneTree | ENSGT00390000001994. |
| HOGENOM | HOG000027493. |
| HOVERGEN | HBG003103. |
| InParanoid | Q1LZA3. |
| KO | K01953. |
| OMA | KEAYYFR. |
| OrthoDB | EOG4RV2R2. |
Enzyme and pathway databases | |
| UniPathway | UPA00134; UER00195. |
Family and domain databases | |
| Gene3D | 3.40.50.620. 1 hit. |
| InterPro | IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR017932. GATase_2_dom. IPR000583. GATase_dom. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Pfam | PF00733. Asn_synthase. 1 hit. PF13537. GATase_7. 1 hit. [Graphical view] |
| PIRSF | PIRSF001589. Asn_synthetase_glu-h. 1 hit. |
| TIGRFAMs | TIGR01536. asn_synth_AEB. 1 hit. |
| PROSITE | PS51278. GATASE_TYPE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 20871226. |
Entry information
| Entry name | ASNS_BOVIN | ||||||||
| Accession | Primary (citable) accession number: Q1LZA3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
