B2TNF0 (B2TNF0_CLOBB) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 33.
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 |
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| Organism | Clostridium botulinum (strain Eklund 17B / Type B) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 508765 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 337 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 ACD23993.1 |
| 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... | |
Sequences
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References
| [1] | "Complete sequence of Clostridium botulinum strain Eklund." Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S. Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001056 Genomic DNA. Translation: ACD23993.1. |
| RefSeq | YP_001886757.1. NC_010674.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B2TNF0. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 6293460. |
| GenomeReviews | Gene locus CLL_A2568 in contig CP001056_GR. |
| KEGG | cbk:CLL_A2568. |
| PATRIC | 19397954. VBICloBot123574_2482. |
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 | B2TNF0_CLOBB | ||||||||
| Accession | Primary (citable) accession number: B2TNF0 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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