E3ZRV6 · E3ZRV6_LISSE
- ProteinAspartate 1-decarboxylase
- GenepanD
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids127 (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
- L-aspartate + H+ = 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 | 25 | Schiff-base intermediate with substrate; via pyruvic acid | ||||
Sequence: S | ||||||
Binding site | 57 | substrate | ||||
Sequence: T | ||||||
Active site | 58 | Proton donor | ||||
Sequence: Y | ||||||
Binding site | 73-75 | 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 > Bacillota > Bacilli > Bacillales > Listeriaceae > Listeria
Accessions
- Primary accessionE3ZRV6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5014006698 | 1-24 | Aspartate 1-decarboxylase beta chain | |||
Sequence: MIRTMMNGKIHRATVTEANLNYVG | ||||||
Modified residue | 25 | Pyruvic acid (Ser) | ||||
Sequence: S | ||||||
Chain | PRO_5014006694 | 25-127 | Aspartate 1-decarboxylase alpha chain | |||
Sequence: SITIDSAILEAVDMLPNEKVQIVNNNNGARIETYIIPGEPGSGVICLNGAAARHVQVGDVVIIISYGMFTSEEANGHEPKIVVLDETNQIEMVLPEEKAHTTL |
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.
Structure
Sequence
- Sequence statusComplete
- Length127
- Mass (Da)13,771
- Last updated2011-02-08 v1
- Checksum3BF9E59B64D05C41
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ADXJ01000770 EMBL· GenBank· DDBJ | EFR99648.1 EMBL· GenBank· DDBJ | Genomic DNA |