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BACCE:BLA2
Contents
Species (Taxon ID) | Bacillus cereus. (1396) | |
Gene Name(s) | blm | |
Protein Name(s) | Beta-lactamase 2
Beta-lactamase II Cephalosporinase Penicillinase | |
External Links | ||
UniProt | P04190 | |
EMBL | M11189 | |
PIR | A91806 | |
PDB | 1BC2 1BMC 1BVT 1DXK 1MQO 2BC2 2BFK 2BFL 2BFZ 2BG2 2BG6 2BG7 2BG8 2BGA 2M5C 2M5D 2NXA 2NYP 2NZE 2NZF 2UYX 3BC2 3FCZ 3I0V 3I11 3I13 3I14 3I15 3KNR 3KNS 4C09 4C1C 4C1H 4NQ4 4NQ5 4NQ6 4NQ7 4TYT | |
PDBsum | 1BC2 1BMC 1BVT 1DXK 1MQO 2BC2 2BFK 2BFL 2BFZ 2BG2 2BG6 2BG7 2BG8 2BGA 2M5C 2M5D 2NXA 2NYP 2NZE 2NZF 2UYX 3BC2 3FCZ 3I0V 3I11 3I13 3I14 3I15 3KNR 3KNS 4C09 4C1C 4C1H 4NQ4 4NQ5 4NQ6 4NQ7 4TYT | |
ProteinModelPortal | P04190 | |
SMR | P04190 | |
BRENDA | 3.5.2.6 | |
SABIO-RK | P04190 | |
EvolutionaryTrace | P04190 | |
GO | GO:0008800 GO:0008270 GO:0017001 GO:0046677 | |
Gene3D | 3.60.15.10 | |
InterPro | IPR001279 IPR001018 | |
Pfam | PF00753 | |
SMART | SM00849 | |
SUPFAM | SSF56281 | |
PROSITE | PS00743 PS00744 |
Annotations
Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
---|---|---|---|---|---|---|---|---|---|---|
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008270 |
zinc ion binding |
ECO:0000314 |
direct assay evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0017001 |
antibiotic catabolic process |
ECO:0000314 |
direct assay evidence used in manual assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008800 |
beta-lactamase activity |
ECO:0000250 |
sequence similarity evidence used in manual assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008270 |
zinc ion binding |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
enables |
GO:0008800 |
beta-lactamase activity |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0017001 |
antibiotic catabolic process |
ECO:0000256 |
match to sequence model evidence used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0008800 |
beta-lactamase activity |
ECO:0000501 |
evidence used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
involved_in |
GO:0046677 |
response to antibiotic |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
P |
Seeded From UniProt |
complete | |||
enables |
GO:0016787 |
hydrolase activity |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
part_of |
GO:0042597 |
periplasmic space |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
C |
Seeded From UniProt |
complete | |||
enables |
GO:0046872 |
metal ion binding |
ECO:0000322 |
imported manually asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Carfi, A et al. (1995) The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 14 4914-21 PubMed GONUTS page
- ↑ Brem, J et al. (2016) Structural Basis of Metallo-β-Lactamase Inhibition by Captopril Stereoisomers. Antimicrob. Agents Chemother. 60 142-50 PubMed GONUTS page
- ↑ Hussain, M et al. (1985) Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli. J. Bacteriol. 164 223-9 PubMed GONUTS page