I3INL5 · I3INL5_9BACT
- 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.
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
- Taxonomic lineageBacteria > Planctomycetota > Candidatus Brocadiia > Candidatus Brocadiales > Candidatus Brocadiaceae > Candidatus Jettenia
Accessions
- Primary accessionI3INL5
Proteomes
Structure
Sequence
- Sequence statusComplete
- Length501
- Mass (Da)57,600
- Last updated2012-07-11 v1
- ChecksumBD60D4E12101AC80
Keywords
- Technical term