P26899 (ASPA_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 88.
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: Aspartate ammonia-lyase Short name=Aspartase EC=4.3.1.1 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 475 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | L-aspartate = fumarate + NH3. |
| Subunit structure | Homotetramer. |
| Sequence similarities | Belongs to the class-II fumarase/aspartase family. Aspartase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | aspartate metabolic process Inferred from electronic annotation. Source: InterPro fumarate metabolic processInferred from electronic annotation. Source: InterPro tricarboxylic acid cycleInferred from electronic annotation. Source: InterPro |
| Cellular component | tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | aspartate ammonia-lyase activity Inferred from electronic annotation. Source: EC fumarate hydratase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 475 | 475 | Aspartate ammonia-lyase | PRO_0000161336 | |||||
Regions | |||||||||
| Region | 143 – 145 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Binding site | 104 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 144 | 1 | T → Q in AAA22244. Ref.1 | ||||||
| Sequence conflict | 144 | 1 | T → Q in BAA12643. Ref.2 | ||||||
| Sequence conflict | 182 | 1 | D → H in AAA22244. Ref.1 | ||||||
| Sequence conflict | 182 | 1 | D → H in BAA12643. Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning, nucleotide sequence, and expression of the Bacillus subtilis ans operon, which codes for L-asparaginase and L-aspartase." Sun D., Setlow P. J. Bacteriol. 173:3831-3845(1991) [PubMed: 1711029] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes." Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y. Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642. |
| [3] | "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. |
| [4] | "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 144 AND 182. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M63264 Genomic DNA. Translation: AAA22244.1. D84432 Genomic DNA. Translation: BAA12643.1. AL009126 Genomic DNA. Translation: CAB14289.2. |
| PIR | UFBSD. B39440. |
| RefSeq | NP_390238.2. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P26899. |
| SMR | P26899. Positions 9-469. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P26899. 2 interactions. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000000486; EBBACP00000000486; EBBACG00000000484. |
| GeneID | 938721. |
| GenomeReviews | Gene locus BSU23570 in contig AL009126_GR. |
| KEGG | bsu:BSU23570. |
| NMPDR | fig|224308.1.peg.2362. |
| PATRIC | 18976535. VBIBacSub10457_2458. |
Organism-specific databases | |
| GenoList | BSU23570. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00070000031773. |
| HOGENOM | HBG284369. |
| PhylomeDB | P26899. |
| ProtClustDB | PRK12273. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU23570-MONOMER. |
Family and domain databases | |
| InterPro | IPR004708. ApsA. IPR003031. D_crystallin. IPR005677. Fum_hydII. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR008948. L-Aspartase-like. IPR024083. L-Aspartase-like_N. IPR022761. Lyase1_N. [Graphical view] |
| Gene3D | G3DSA:1.10.275.10. G3DSA:1.10.275.10. 1 hit. |
| KO | K01744. |
| Pfam | PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view] |
| PRINTS | PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE. |
| SUPFAM | SSF48557. L-Aspartase-like. 1 hit. |
| TIGRFAMs | TIGR00839. AspA. 1 hit. |
| PROSITE | PS00163. FUMARATE_LYASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASPA_BACSU | ||||||||
| Accession | Primary (citable) accession number: P26899 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

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