D4P095 · CNPD3_PSEAI

  • Protein
    3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
  • Gene
    cpdA
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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

Cofactor

a divalent metal cation (UniProtKB | Rhea| CHEBI:60240 )

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 μMcAMP
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
3.4 nmol/min/ng

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site21Fe cation 1 (UniProtKB | ChEBI)
Binding site23AMP (UniProtKB | ChEBI)
Binding site23Fe cation 1 (UniProtKB | ChEBI)
Binding site63AMP (UniProtKB | ChEBI)
Binding site63Fe cation 1 (UniProtKB | ChEBI)
Binding site63Fe cation 2 (UniProtKB | ChEBI)
Binding site93Fe cation 2 (UniProtKB | ChEBI)
Binding site93-94AMP (UniProtKB | ChEBI)
Binding site161Fe cation 2 (UniProtKB | ChEBI)
Binding site200Fe cation 2 (UniProtKB | ChEBI)
Binding site202AMP (UniProtKB | ChEBI)
Binding site202Fe cation 1 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Molecular Function3',5'-cyclic-AMP phosphodiesterase activity
Molecular Functionmetal ion binding
Molecular Functionnucleotide binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
  • EC number
  • Short names
    3',5'-cyclic AMP phosphodiesterase
    ; cAMP phosphodiesterase

Gene names

    • Name
      cpdA

Organism names

  • Taxonomic identifier
  • Strain
    • PAK
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas

Accessions

  • Primary accession
    D4P095

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.

TypeIDPosition(s)Description
Mutagenesis23Loss of activity.
Mutagenesis63Loss of activity.
Mutagenesis93Loss of activity.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004133731-2723',5'-cyclic adenosine monophosphate phosphodiesterase CpdA

Expression

Induction

Positively regulated by Vfr in response to elevated intracellular cAMP.

Interaction

Subunit

Monomer.

Structure

Family & Domains

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    272
  • Mass (Da)
    30,472
  • Last updated
    2010-05-18 v1
  • Checksum
    1C22AEBA58FD867F
MSRHSNTPATDASVLLVQLSDSHLFAEDGARLLGMDTAHSLEKVVERVAREQPRIDLILATGDVSQDGSLDSYTRFRRLSAPLAAPLRWFAGNHDEREPMQRATEGSDLLEQIVDVGNWRVVLLDSSIPGAVPGYLEDDQLDLLRRAIDSAGERFLLVSFHHHPVPIGSDWMDPIGLRNPQALFDLLAPYPQLRCLLWGHIHQEFDRQRGPLRLLASPSTCVQFAPGSSDFTLDRLAPGYRWLRLHDDGRLETGISRVDDVVFEVDYDTAGY

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
GU551724
EMBL· GenBank· DDBJ
ADD69827.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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