C1FMJ4 (C1FMJ4_CLOBJ) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 24.
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 Kyoto / Type A2) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 536232 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 340 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 ACO85673.1 |
| 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] | "Genome sequence of Clostridium botulinum A2 Kyoto." Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C., Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S. Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001581 Genomic DNA. Translation: ACO85673.1. |
| RefSeq | YP_002803929.1. NC_012563.1. |
3D structure databases | |
| ProteinModelPortal | C1FMJ4. |
| SMR | C1FMJ4. Positions 21-335. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | C1FMJ4. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 7765269. |
| GenomeReviews | Gene locus CLM_1740 in contig CP001581_GR. |
| KEGG | cby:CLM_1740. |
| PATRIC | 19379995. VBICloBot91161_1623. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| 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 | C1FMJ4_CLOBJ | ||||||||
| Accession | Primary (citable) accession number: C1FMJ4 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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