B3A2J0 (B3A2J0_ECO57) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 29.
History...
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Aspartate--ammonia ligase HAMAP MF_00555 EC=6.3.1.1 HAMAP MF_00555 Alternative name(s): Asparagine synthetase A HAMAP MF_00555 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli O157:H7 str. EC4401 EMBL EDU77786.1 | ||||
| Taxonomic identifier | 478004 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
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 SAAS SAAS004618 |
| Pathway | Amino-acid biosynthesis; L-asparagine biosynthesis; L-asparagine from L-aspartate (ammonia route): step 1/1. HAMAP MF_00555 SAAS SAAS004618 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00555 SAAS SAAS004618. |
| Sequence similarities | Belongs to the class-II aminoacyl-tRNA synthetase family. AsnA subfamily. HAMAP MF_00555 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Asparagine biosynthesis HAMAP MF_00555 SAAS SAAS004618 |
| Cellular component | Cytoplasm HAMAP MF_00555 SAAS SAAS004618 |
| Ligand | ATP-binding HAMAP MF_00555 SAAS SAAS004618 Nucleotide-binding |
| Molecular function | Ligase HAMAP MF_00555 SAAS SAAS004618 EMBL EDU77786.1 |
| 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... | |
Sequences
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References
| [1] | "Annotation of Escherichia coli O157:H7 str. EC4401." Eppinger M., Ravel J., Mammel M.K., LeClerc J.E., Cebula T.A., Sebastian Y. Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: EC4401 EMBL EDU77786.1. |
| [2] | Rosovitz M.J., Ravel J. Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: EC4401 EMBL EDU77786.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ABHR01000001 Genomic DNA. Translation: EDU77786.1. |
3D structure databases | |
| ProteinModelPortal | B3A2J0. |
| SMR | B3A2J0. Positions 4-330. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 29327455. VBIEscCol43159_0542. |
Phylogenomic databases | |
| OMA | LNDNLNG. |
Family and domain databases | |
| HAMAP | MF_00555. AsnA. [Tree] |
| InterPro | IPR006195. aa-tRNA-synth_II. 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 | B3A2J0_ECO57 | ||||||||
| Accession | Primary (citable) accession number: B3A2J0 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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