A0A0S6TZ18 · A0A0S6TZ18_CLOBO
- ProteinAspartate 1-decarboxylase
- GenepanD
- StatusUniProtKB unreviewed (TrEMBL)
- 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
- 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 | cytoplasm | |
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 > Bacillota > Clostridia > Eubacteriales > Clostridiaceae > Clostridium
Accessions
- Primary accessionA0A0S6TZ18
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5014001077 | 1-24 | Aspartate 1-decarboxylase beta chain | |||
Sequence: MTITMLKSKIHRATITEANLNYVG | ||||||
Modified residue | 25 | Pyruvic acid (Ser) | ||||
Sequence: S | ||||||
Chain | PRO_5014001079 | 25-127 | Aspartate 1-decarboxylase alpha chain | |||
Sequence: SITIDKNLMDKANILEYEKVQIVDIDNGSRFETYVIAGEKNSGVICLNGAAARMVQKGDKIIIMSYCDLTIDEAKKFNPTVLFVDNTNIIEKLTNYERHGEII |
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)14,288
- Last updated2016-02-17 v1
- Checksum3446E0CC32845847