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9PSED:Q7WSJ4
Contents
| Species (Taxon ID) | Pseudomonas chlororaphis. (587753) | |
| Gene Name(s) | oxdA (ECO:0000313 with EMBL:BAC81537.1) | |
| Protein Name(s) | Aldoxime dehydratase (ECO:0000313 with EMBL:BAC81537.1) | |
| External Links | ||
| UniProt | Q7WSJ4 | |
| EMBL | AB093544 | |
| PDB | 3W08 | |
| PDBsum | 3W08 | |
| BioCyc | MetaCyc:MONOMER-15569 | |
| BRENDA | 4.99.1.5 | |
| SABIO-RK | Q7WSJ4 | |
| GO | GO:0046872 | |
| InterPro | IPR025702 | |
| Pfam | PF13816 | |
| ProDom | PD320837 | |
Annotations
| Qualifier | GO ID | GO term name | Reference | ECO ID | ECO term name | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|---|---|
|
Contributes to |
GO:0034013 |
aliphatic aldoxime dehydratase activity |
ECO:0000314 |
F |
OxdA encodes for aldoxime dehydratase activity. Figure 3As shows the activity between the purified enzyme, the enzyme with Na2S2O4-reduced, and the enzyme with Na2S2O4-reduced plus CO. As a result, oxdA was shown to have much higher activity in the presence of Na2S2O4. This shows the Na2S2O4 reagent assists in the already present reducing activity. |
complete | ||||
|
enables |
GO:0046872 |
metal ion binding |
ECO:0000323 |
imported automatically asserted information used in automatic assertion |
F |
Seeded From UniProt |
complete | |||
Notes
References
See Help:References for how to manage references in GONUTS.
- ↑ Oinuma, K et al. (2003) Novel aldoxime dehydratase involved in carbon-nitrogen triple bond synthesis of Pseudomonas chlororaphis B23. Sequencing, gene expression, purification, and characterization. J. Biol. Chem. 278 29600-8 PubMed GONUTS page
