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D4P095 (CPDA_PSEAI) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA

Short name=3',5'-cyclic AMP phosphodiesterase
Short name=cAMP phosphodiesterase
EC=3.1.4.17
Gene names
Name:cpdA
OrganismPseudomonas aeruginosa
Taxonomic identifier287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length272 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.1

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. Ref.1

Cofactor

Binds 2 metal cations per subunit. Site 1 may preferentially bind Fe3+ ions, while site 2 may have a preference for Fe2+ ions. Ref.1

Enzyme regulation

Activated by iron. Other divalent metal ions have no effect. Ref.1

Subunit structure

Monomer. Ref.1

Induction

Positively regulated by Vfr in response to elevated intracellular cAMP. Ref.1

Disruption phenotype

Mutants show increased levels of cellular cAMP. In rich medium, mutants exhibit a significantly reduced growth rate compared to wild-type strain. Ref.1

Sequence similarities

Belongs to the cAMP phosphodiesterase class-III family.

Biophysicochemical properties

Kinetic parameters:

KM=7.2 µM for cAMP Ref.1

Vmax=3.4 nmol/min/ng enzyme

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2722723',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000413373

Regions

Nucleotide binding93 – 942cAMP By similarity

Sites

Metal binding211Iron 1 By similarity
Metal binding231Iron 1 Probable
Metal binding631Iron 1 Probable
Metal binding631Iron 2 By similarity
Metal binding931Iron 2 Probable
Metal binding1611Iron 2 By similarity
Metal binding2001Iron 2 By similarity
Metal binding2021Iron 1 By similarity
Binding site231cAMP By similarity
Binding site631cAMP By similarity
Binding site2021cAMP By similarity

Experimental info

Mutagenesis231H → A: Loss of activity. Ref.1
Mutagenesis631D → A: Loss of activity. Ref.1
Mutagenesis931N → A: Loss of activity. Ref.1

Sequences

Sequence LengthMass (Da)Tools
D4P095 [UniParc].

Last modified May 18, 2010. Version 1.
Checksum: 1C22AEBA58FD867F

FASTA27230,472
        10         20         30         40         50         60 
MSRHSNTPAT DASVLLVQLS DSHLFAEDGA RLLGMDTAHS LEKVVERVAR EQPRIDLILA 

        70         80         90        100        110        120 
TGDVSQDGSL DSYTRFRRLS APLAAPLRWF AGNHDEREPM QRATEGSDLL EQIVDVGNWR 

       130        140        150        160        170        180 
VVLLDSSIPG AVPGYLEDDQ LDLLRRAIDS AGERFLLVSF HHHPVPIGSD WMDPIGLRNP 

       190        200        210        220        230        240 
QALFDLLAPY PQLRCLLWGH IHQEFDRQRG PLRLLASPST CVQFAPGSSD FTLDRLAPGY 

       250        260        270 
RWLRLHDDGR LETGISRVDD VVFEVDYDTA GY 

« Hide

References

[1]"In vitro and in vivo characterization of the Pseudomonas aeruginosa cyclic AMP (cAMP) phosphodiesterase CpdA, required for cAMP homeostasis and virulence factor regulation."
Fuchs E.L., Brutinel E.D., Klem E.R., Fehr A.R., Yahr T.L., Wolfgang M.C.
J. Bacteriol. 192:2779-2790(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF HIS-23; ASP-63 AND ASN-93.
Strain: PAK.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
GU551724 Genomic DNA. Translation: ADD69827.1.

3D structure databases

ProteinModelPortalD4P095.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR026575. cAMP_Pdiest_CpdA.
IPR004843. PEstase_dom.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPDA_PSEAI
AccessionPrimary (citable) accession number: D4P095
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: May 18, 2010
Last modified: February 19, 2014
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families