Reviewed,
UniProtKB/Swiss-Prot P42113 (ASNH_BACSU)
Last modified
November 3, 2009.
Version 72.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Asparagine synthetase [glutamine-hydrolyzing] 2 EC=6.3.5.4 | ||||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 747 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | ATP + L-aspartate + L-glutamine + H2O = AMP + diphosphate + L-asparagine + L-glutamate. |
| Pathway | |
| Sequence similarities | Belongs to the asparagine synthetase family. 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 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | asparagine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| 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 – 747 | 747 | Asparagine synthetase [glutamine-hydrolyzing] 2 | PRO_0000056933 | |||||
Regions | |||||||||
| Domain | 2 – 218 | 217 | Glutamine amidotransferase type-2 | ||||||
Sites | |||||||||
| Active site | 2 | 1 | For GATase activity By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 185 | 1 | W → C in BAA21593. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning and sequencing of a 36-kb region of the Bacillus subtilis genome between the gnt and iol operons." Yoshida K., Seki S., Fujimura M., Miwa Y., Fujita Y. DNA Res. 2:61-69(1995) [PubMed: 7584049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / BGSC1A1. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed: 19383706] [Abstract] Cited for: SEQUENCE REVISION TO 185. |
| [4] | "Three asparagine synthetase genes of Bacillus subtilis." Yoshida K., Fujita Y., Ehrlich S.D. J. Bacteriol. 181:6081-6091(1999) [PubMed: 10498721] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| AB005554 Genomic DNA. Translation: BAA21593.1. AL009126 Genomic DNA. Translation: CAB16028.2. | |
| PIR | A69591. |
| RefSeq | NP_391871.2. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1CT9 based on UniProtKB P22106. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 937677. |
| GenomeReviews | Gene locus BSU39920 in contig AL009126_GR. |
| KEGG | bsu:BSU39920. |
| NMPDR | fig|224308.1.peg.3997. |
Organism-specific databases | |
| SubtiList | BG11116. asnH. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| OMA | NISANKC. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU3988-MON. |
| BRENDA | 6.3.5.4. 150. |
Family and domain databases | |
| InterPro | IPR006426. Asn_synth_AEB. IPR001962. Asn_synthase. IPR000583. GATase_2. IPR017932. GATase_II. IPR014729. Rossmann-like_a/b/a_fold. [Graphical view] |
| Gene3D | G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit. |
| Pfam | PF00733. Asn_synthase. 1 hit. PF00310. GATase_2. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01536. asn_synth_AEB. 1 hit. |
| PROSITE | PS51278. GATASE_TYPE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASNH_BACSU | ||||||||
| Accession | Primary (citable) accession number: P42113 | ||||||||
| 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
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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