A4GRB2 · A4GRB2_CHRID
- ProteinMetallo-beta-lactamase type 2
- GeneblaIND-7
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids239 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring.
Catalytic activity
- a beta-lactam + H2O = a substituted beta-amino acid
Cofactor
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 96 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 98 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 100 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 159 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 178 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 220 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | periplasmic space | |
Molecular Function | beta-lactamase activity | |
Molecular Function | zinc ion binding | |
Biological Process | antibiotic catabolic process | |
Biological Process | response to antibiotic |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameMetallo-beta-lactamase type 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacteroidota > Flavobacteriia > Flavobacteriales > Weeksellaceae > Chryseobacterium group > Chryseobacterium
Accessions
- Primary accessionA4GRB2
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MKKSIRFFIVSILLSPFASA | ||||||
Chain | PRO_5010820328 | 21-239 | Metallo-beta-lactamase type 2 | |||
Sequence: QVKDFVIEPPIKNNLHIYKTFGVFGGKEYSANSMYLVTKKGVVLFDVPWEKVQYQSLMDTIKKRHNLPVVAVFATHSHDDRAGDLSFFNNKGIKTYATAKTNEFLKKDGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYNVLDGGCLVKSNSATDLGYIKEANVEQWPKTINKLKAKYSKATLIIPGHDEWKGGGHVEHTLELLNKK |
Interaction
Subunit
Monomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 50-220 | Metallo-beta-lactamase | ||||
Sequence: SANSMYLVTKKGVVLFDVPWEKVQYQSLMDTIKKRHNLPVVAVFATHSHDDRAGDLSFFNNKGIKTYATAKTNEFLKKDGKATSTEIIKTGKPYRIGGEEFVVDFLGEGHTADNVVVWFPKYNVLDGGCLVKSNSATDLGYIKEANVEQWPKTINKLKAKYSKATLIIPGH |
Sequence similarities
Belongs to the metallo-beta-lactamase superfamily. Class-B beta-lactamase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length239
- Mass (Da)26,829
- Last updated2007-04-17 v1
- Checksum85F1C7A71C3EA656
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
EF394437 EMBL· GenBank· DDBJ | ABO21412.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB529520 EMBL· GenBank· DDBJ | BAJ05825.1 EMBL· GenBank· DDBJ | Genomic DNA |