A0A1B1B099 · A0A1B1B099_9ACTN
- ProteinAspartate 1-decarboxylase
- GenepanD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids140 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine.
Catalytic activity
- H+ + L-aspartate = beta-alanine + CO2
Cofactor
Note: Binds 1 pyruvoyl group covalently per subunit.
Pathway
Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 26 | Schiff-base intermediate with substrate; via pyruvic acid | ||||
Sequence: S | ||||||
Binding site | 58 | substrate | ||||
Sequence: T | ||||||
Active site | 59 | Proton donor | ||||
Sequence: Y | ||||||
Binding site | 74-76 | substrate | ||||
Sequence: GAA |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | aspartate 1-decarboxylase activity | |
Biological Process | alanine biosynthetic process | |
Biological Process | pantothenate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAspartate 1-decarboxylase
- EC number
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Actinomycetota > Actinomycetes > Kitasatosporales > Streptomycetaceae > Streptomyces
Accessions
- Primary accessionA0A1B1B099
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5013992942 | 1-25 | Aspartate 1-decarboxylase beta chain | |||
Sequence: MYYRTMFKSKVHRATVTQADLHYVG | ||||||
Modified residue | 26 | Pyruvic acid (Ser) | ||||
Sequence: S | ||||||
Chain | PRO_5013992940 | 26-140 | Aspartate 1-decarboxylase alpha chain | |||
Sequence: SLTLDADLMEAADLLPGEKVDIVDIDNGNRLSTYLIEGPRGSGVVGINGAAARLISPGDLVIIISYADIWNSDAARLVPRVVHVDRDNKIISLGSDPAEATPDGTTTRGDHIFVD |
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.
Keywords
- PTM
Interaction
Subunit
Heterooctamer of four alpha and four beta subunits.
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length140
- Mass (Da)15,121
- Last updated2016-11-02 v1
- ChecksumC0F2767E6A6A3B0C
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP016279 EMBL· GenBank· DDBJ | ANP52248.1 EMBL· GenBank· DDBJ | Genomic DNA |