A8FK85 (PAND_CAMJ8) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 29.
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 | Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 407148 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
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 MF_00446 |
| Catalytic activity | L-aspartate = beta-alanine + CO2. HAMAP MF_00446 |
| Cofactor | Pyruvoyl group By similarity. HAMAP MF_00446 |
| 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 HAMAP 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 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: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: EC 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_1000072349 | |||||
| Chain | 25 – 126 | 102 | Aspartate 1-decarboxylase alpha chain By similarity | PRO_1000072350 | |||||
Regions | |||||||||
| Region | 72 – 74 | 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] | "The complete genome sequence of Campylobacter jejuni strain 81116 (NCTC11828)." Pearson B.M., Gaskin D.J.H., Segers R.P.A.M., Wells J.M., Nuijten P.J.M., van Vliet A.H.M. J. Bacteriol. 189:8402-8403(2007) [PubMed: 17873037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 81116 / NCTC 11828. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000814 Genomic DNA. Translation: ABV51872.1. |
| RefSeq | YP_001481849.1. NC_009839.1. |
3D structure databases | |
| ProteinModelPortal | A8FK85. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A8FK85. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5617068. |
| GenomeReviews | Gene locus C8J_0273 in contig CP000814_GR. |
| KEGG | cju:C8J_0273. |
| PATRIC | 20054116. VBICamJej119085_0281. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0853. |
| HOGENOM | HBG302821. |
| OMA | LYSKIHR. |
| ProtClustDB | PRK05449. |
Enzyme and pathway databases | |
| BioCyc | CJEJ407148:C8J_0273-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00446. PanD. [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. |
| KO | K01579. |
| 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] |
| SUPFAM | SSF50692. Asp_decarb_fold. 1 hit. |
| TIGRFAMs | TIGR00223. PanD. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PAND_CAMJ8 | ||||||||
| Accession | Primary (citable) accession number: A8FK85 | ||||||||
| 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 |

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