A0A9P2TX92 · A0A9P2TX92_BRUML
- ProteinD-aminopeptidase
- Genedap
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids518 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Hydrolyzes N-terminal residues in D-amino acid-containing peptides.
Catalytic activity
Activity regulation
Inhibited by beta-lactam compounds such as 6-aminopenicillic acid, 7-aminocephalosporanic acid, benzylpenicillin and ampicillin. Inhibited by p-chloromercuribenzoate.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 62 | Nucleophile | |||
Active site | 65 | Proton donor/acceptor | |||
Binding site | 481 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | aminopeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameD-aminopeptidase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Brucellaceae > Brucella/Ochrobactrum group > Brucella
Accessions
- Primary accessionA0A9P2TX92
Proteomes
Interaction
Subunit
Homodimer.
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 10-324 | Beta-lactamase-related | |||
Domain | 340-516 | D-aminopeptidase | |||
Region | 373-392 | Disordered | |||
Region | 477-487 | Important for specificity | |||
Sequence similarities
Belongs to the peptidase S12 family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length518
- Mass (Da)56,887
- Last updated2023-09-13 v1
- ChecksumEBC9EA71E2CB3C57
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AXMZ01000009 EMBL· GenBank· DDBJ | ERU21955.1 EMBL· GenBank· DDBJ | Genomic DNA |