D4P095 · CNPD3_PSEAI
- Protein3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
- GenecpdA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids272 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Specifically required for regulation of virulence factors. Can also hydrolyze cGMP, but cGMP is unlikely to be synthesized by P.aeruginosa and cAMP is probably the biologically relevant substrate for CpdA in vivo.
Catalytic activity
- 3',5'-cyclic AMP + H2O = AMP + H+
Cofactor
Note: Binds 2 metal cations per subunit. Site 1 may preferentially bind Fe3+ ions, while site 2 may have a preference for Fe2+ ions.
Activity regulation
Activated by iron. Other divalent metal ions have no effect.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
7.2 μM | cAMP |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
3.4 nmol/min/ng |
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 21 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 23 | AMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 23 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 63 | AMP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 63 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 63 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 93 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 93-94 | AMP (UniProtKB | ChEBI) | ||||
Sequence: NH | ||||||
Binding site | 161 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 200 | Fe cation 2 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 202 | AMP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 202 | Fe cation 1 (UniProtKB | ChEBI) | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3',5'-cyclic-AMP phosphodiesterase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
- EC number
- Short names3',5'-cyclic AMP phosphodiesterase ; cAMP phosphodiesterase
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionD4P095
Phenotypes & Variants
Disruption phenotype
Mutants show increased levels of cellular cAMP. In rich medium, mutants exhibit a significantly reduced growth rate compared to wild-type strain.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 23 | Loss of activity. | ||||
Sequence: H → A | ||||||
Mutagenesis | 63 | Loss of activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 93 | Loss of activity. | ||||
Sequence: N → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000413373 | 1-272 | 3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA | |||
Sequence: MSRHSNTPATDASVLLVQLSDSHLFAEDGARLLGMDTAHSLEKVVERVAREQPRIDLILATGDVSQDGSLDSYTRFRRLSAPLAAPLRWFAGNHDEREPMQRATEGSDLLEQIVDVGNWRVVLLDSSIPGAVPGYLEDDQLDLLRRAIDSAGERFLLVSFHHHPVPIGSDWMDPIGLRNPQALFDLLAPYPQLRCLLWGHIHQEFDRQRGPLRLLASPSTCVQFAPGSSDFTLDRLAPGYRWLRLHDDGRLETGISRVDDVVFEVDYDTAGY |
Expression
Induction
Positively regulated by Vfr in response to elevated intracellular cAMP.
Interaction
Subunit
Monomer.
Structure
Sequence
- Sequence statusComplete
- Length272
- Mass (Da)30,472
- Last updated2010-05-18 v1
- Checksum1C22AEBA58FD867F