A4SGF2 · PAND_CHLPM
- ProteinAspartate 1-decarboxylase
- GenepanD
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids128 (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 | 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
- Strain
- Taxonomic lineageBacteria > Chlorobiota > Chlorobiia > Chlorobiales > Chlorobiaceae > Chlorobium/Pelodictyon group > Chlorobium
Accessions
- Primary accessionA4SGF2
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000080932 | 1-24 | Aspartate 1-decarboxylase beta chain | |||
Sequence: MKLHLLKSKIHNAIVTSGDLEYEG | ||||||
Modified residue | 25 | Pyruvic acid (Ser) | ||||
Sequence: S | ||||||
Chain | PRO_1000080933 | 25-128 | Aspartate 1-decarboxylase alpha chain | |||
Sequence: SITVDSELLKKADMIPNEKVLVVNNNNGERFETYIIKGDHGSRVIQLNGAAARCALPGDEIIIMTFCEIEAEEAPDFKPMVLIVDKNNNPKRRHRIGEEDEQLG |
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
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length128
- Mass (Da)14,326
- Last updated2007-05-15 v1
- Checksum273C01D6C21F5B5A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000607 EMBL· GenBank· DDBJ | ABP37561.1 EMBL· GenBank· DDBJ | Genomic DNA |