A0A8D5UJ53 · A0A8D5UJ53_9BACL
- ProteinMetal-dependent carboxypeptidase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids501 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
Catalytic activity
Cofactor
Note: Binds 1 zinc ion per subunit.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 264 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 265 | Proton donor/acceptor | |||
Binding site | 268 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 294 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | metallocarboxypeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMetal-dependent carboxypeptidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Bacillales > Thermoactinomycetaceae > Polycladomyces
Accessions
- Primary accessionA0A8D5UJ53
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length501
- Mass (Da)57,577
- Last updated2022-01-19 v1
- Checksum57F3BA7D2D582012
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP024601 EMBL· GenBank· DDBJ | BCU82792.1 EMBL· GenBank· DDBJ | Genomic DNA |