Reviewed,
UniProtKB/Swiss-Prot P52999 (PAND_BACSU)
Last modified
November 3, 2009.
Version 73.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Aspartate 1-decarboxylase EC=4.1.1.11 Alternative name(s): Aspartate alpha-decarboxylase Cleaved into the following 2 chains: 1- Recommended name: Aspartate 1-decarboxylase beta chain 2- Recommended name: Aspartate 1-decarboxylase alpha chain | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1423 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 127 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. |
| Catalytic activity | L-aspartate = beta-alanine + CO2. HAMAP MF_00446 |
| Cofactor | Pyruvoyl group By similarity. |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP MF_00446 |
| Subunit structure | Heterooctamer of four alpha and four beta subunits By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Post-translational modification | Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus By similarity. |
| Sequence similarities | Belongs to the panD family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Pyruvate Schiff base |
| Molecular function | Decarboxylase Lyase |
| PTM | Autocatalytic cleavage Zymogen |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | alanine biosynthetic process Inferred from electronic annotation. Source: InterPro pantothenate biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: HAMAP bindingInferred 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 – 24 | 24 | Aspartate 1-decarboxylase beta chain By similarity | PRO_0000023035 | |||||
| Chain | 25 – 127 | 103 | Aspartate 1-decarboxylase alpha chain By similarity | PRO_0000023036 | |||||
Regions | |||||||||
| Region | 73 – 75 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 25 | 1 | Schiff-base intermediate with substrate; via pyruvic acid By similarity | ||||||
| Active site | 58 | 1 | Proton donor By similarity | ||||||
| Binding site | 57 | 1 | Substrate By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 25 | 1 | Pyruvic acid (Ser) By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence analysis of the Bacillus subtilis chromosome region between the serA and kdg loci cloned in a yeast artificial chromosome." Sorokin A.V., Azevedo V., Zumstein E., Galleron N., Ehrlich S.D., Serror P. Microbiology 142:2005-2016(1996) [PubMed: 8760912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / Marburg. |
| [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. |
Cross-references
Sequence databases | |
|---|---|
| L47709 Genomic DNA. Translation: AAB38450.1. AL009126 Genomic DNA. Translation: CAB14157.1. | |
| PIR | A69672. |
| RefSeq | NP_390122.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AW8 based on UniProtKB P31664. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 939033. |
| GenomeReviews | Gene locus BSU22410 in contig AL009126_GR. |
| KEGG | bsu:BSU22410. |
| NMPDR | fig|224308.1.peg.2245. |
Organism-specific databases | |
| SubtiList | BG11493. panD. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P52999. |
| OMA | TTYAIRA. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU2240-MON. |
| BRENDA | 4.1.1.11. 150. |
Family and domain databases | |
| HAMAP | MF_00446. [Tree] |
| InterPro | IPR009010. Asp_de-COase-like_fold. IPR003190. Asp_decarbox. [Graphical view] |
| Gene3D | G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit. |
| PANTHER | PTHR21012. Asp_decarbox. 1 hit. |
| Pfam | PF02261. Asp_decarbox. 1 hit. [Graphical view] |
| PIRSF | PIRSF006246. Asp_decarbox. 1 hit. |
| ProDom | PD009294. Asp_decarbox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00223. panD. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PAND_BACSU | ||||||||
| Accession | Primary (citable) accession number: P52999 | ||||||||
| 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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