Cloned (Comment) | Organism |
---|---|
gene pxpA3, phylogenetic analysis | Pseudomonas aeruginosa |
Crystallization (Comment) | Organism |
---|---|
crystal structure analysis, PDB ID 2XU2, and structure comparisons, structure-function relationships of 5-oxoprolinase subunit A, overview | Pseudomonas aeruginosa |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Pseudomonas aeruginosa |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5-oxo-L-proline + 2 H2O | Pseudomonas aeruginosa | - |
ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | Pseudomonas aeruginosa ATCC 15692 | - |
ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | Pseudomonas aeruginosa 1C | - |
ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | Pseudomonas aeruginosa PRS 101 | - |
ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | Pseudomonas aeruginosa DSM 22644 | - |
ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | Pseudomonas aeruginosa CIP 104116 | - |
ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | Pseudomonas aeruginosa LMG 12228 | - |
ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | Pseudomonas aeruginosa JCM 14847 | - |
ADP + phosphate + L-glutamate | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas aeruginosa | Q9HVR0 | encoding subunit A | - |
Pseudomonas aeruginosa 1C | Q9HVR0 | encoding subunit A | - |
Pseudomonas aeruginosa ATCC 15692 | Q9HVR0 | encoding subunit A | - |
Pseudomonas aeruginosa CIP 104116 | Q9HVR0 | encoding subunit A | - |
Pseudomonas aeruginosa DSM 22644 | Q9HVR0 | encoding subunit A | - |
Pseudomonas aeruginosa JCM 14847 | Q9HVR0 | encoding subunit A | - |
Pseudomonas aeruginosa LMG 12228 | Q9HVR0 | encoding subunit A | - |
Pseudomonas aeruginosa PRS 101 | Q9HVR0 | encoding subunit A | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + 5-oxo-L-proline + 2 H2O | - |
Pseudomonas aeruginosa | ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | - |
Pseudomonas aeruginosa ATCC 15692 | ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | - |
Pseudomonas aeruginosa 1C | ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | - |
Pseudomonas aeruginosa PRS 101 | ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | - |
Pseudomonas aeruginosa DSM 22644 | ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | - |
Pseudomonas aeruginosa CIP 104116 | ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | - |
Pseudomonas aeruginosa LMG 12228 | ADP + phosphate + L-glutamate | - |
? | |
ATP + 5-oxo-L-proline + 2 H2O | - |
Pseudomonas aeruginosa JCM 14847 | ADP + phosphate + L-glutamate | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A. Four putative PxpA three-dimensional structures are determined by structural genomics initiatives | Pseudomonas aeruginosa |
Synonyms | Comment | Organism |
---|---|---|
5-oxoprolinase | - |
Pseudomonas aeruginosa |
PA4511 | - |
Pseudomonas aeruginosa |
PxpA | prokaryotic 5-oxoprolinase subunit A | Pseudomonas aeruginosa |
pxpA3 | - |
Pseudomonas aeruginosa |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Pseudomonas aeruginosa |
General Information | Comment | Organism |
---|---|---|
evolution | phylogenetic analysis suggests a relationship between taxonomic grouping and PxpA oligomerization | Pseudomonas aeruginosa |
additional information | subunit A, PxpA, associates with the subunit B and C complex, PxpBC, to form a functional 5-oxoprolinase enzyme for conversion of 5-oxoproline to L-glutamate. PxpBC catalyses the first step of the reaction, which is phosphorylation of 5-oxoproline. PxpA is involved in the last two steps of the reaction: decyclization of the labile phosphorylated 5-oxoproline to the equally labile gamma-glutamylphosphate, and subsequent dephosphorylation to L-glutamate. Structural bioinformatics analysis of four putative PxpA structures reveal that PxpA adopts a non-canonical TIM barrel fold with well-characterized TIM barrel enzyme features. Structure-function relationships of 5-oxoprolinase subunit A, overview. PxpA forms a tunnel upon ligand binding, thus suggesting that the PxpABC complex employs the mechanism of substrate channeling to protect labile intermediates. Active site structure of PxpA | Pseudomonas aeruginosa |