P0A793 (PAND_SHIFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 63.
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 1-decarboxylase EC=4.1.1.11 Alternative name(s): Aspartate alpha-decarboxylase Cleaved into the following 2 chains: | ||||
| Gene names |
| ||||
| Organism | Shigella flexneri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 623 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella![]() |
Protein attributes
| Sequence length | 126 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. HAMAP-Rule MF_00446 |
| Catalytic activity | L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446 |
| Cofactor | Pyruvoyl group By similarity. HAMAP-Rule MF_00446 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP-Rule MF_00446 |
| Subunit structure | Heterooctamer of four alpha and four beta subunits By similarity. |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00446. |
| 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. HAMAP-Rule MF_00446 |
| 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 |
| 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_0000023155 | |||||
| Chain | 25 – 126 | 102 | Aspartate 1-decarboxylase alpha chain By similarity | PRO_0000023156 | |||||
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
| [1] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005674 Genomic DNA. Translation: AAN41791.2. AE014073 Genomic DNA. Translation: AAP15672.1. |
| RefSeq | NP_706084.2. NC_004337.2. NP_835867.1. NC_004741.1. |
3D structure databases | |
| ProteinModelPortal | P0A793. |
| SMR | P0A793. Positions 25-122. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 198214.SF0128. |
Proteomic databases | |
| PaxDb | P0A793. |
| PRIDE | P0A793. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAN41791; AAN41791; SF0128. AAP15672; AAP15672; S0130. |
| GeneID | 1024489. 1076562. |
| KEGG | sfl:SF0128. sfx:S0130. |
| PATRIC | 18701202. VBIShiFle31049_0143. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0853. |
| HOGENOM | HOG000221007. |
| KO | K01579. |
| ProtClustDB | PRK05449. |
Enzyme and pathway databases | |
| UniPathway | UPA00028; UER00002. |
Family and domain databases | |
| Gene3D | 2.40.40.20. 1 hit. |
| HAMAP | MF_00446. PanD. |
| InterPro | IPR009010. Asp_de-COase-like_dom. IPR003190. Asp_decarbox. [Graphical view] |
| PANTHER | PTHR21012. PTHR21012. 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] |
| SUPFAM | SSF50692. Asp_decarb_fold. 1 hit. |
| TIGRFAMs | TIGR00223. panD. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PAND_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P0A793 Secondary accession number(s): P31664, Q8KMY8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
