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Protein

3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA

Gene

cpdA

Organism
Pseudomonas aeruginosa
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.UniRule annotation1 Publication

Catalytic activityi

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.UniRule annotation1 Publication

Cofactori

a divalent metal cationUniRule annotation1 PublicationNote: Binds 2 metal cations per subunit. Site 1 may preferentially bind Fe(3+) ions, while site 2 may have a preference for Fe2+ ions.UniRule annotation1 Publication

Enzyme regulationi

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

Kineticsi

  1. KM=7.2 µM for cAMP1 Publication
  1. Vmax=3.4 nmol/min/ng enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi21 – 211Iron 1By similarity
Metal bindingi23 – 231Iron 1Curated
Binding sitei23 – 231cAMPUniRule annotation
Metal bindingi63 – 631Iron 1Curated
Metal bindingi63 – 631Iron 2By similarity
Binding sitei63 – 631cAMPUniRule annotation
Metal bindingi93 – 931Iron 2Curated
Metal bindingi161 – 1611Iron 2By similarity
Metal bindingi200 – 2001Iron 2By similarity
Metal bindingi202 – 2021Iron 1By similarity
Binding sitei202 – 2021cAMPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi93 – 942cAMPUniRule annotation

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Iron, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi3.1.4.53. 5087.

Names & Taxonomyi

Protein namesi
Recommended name:
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdAUniRule annotation (EC:3.1.4.17UniRule annotation)
Short name:
3',5'-cyclic AMP phosphodiesteraseUniRule annotation
Short name:
cAMP phosphodiesteraseUniRule annotation
Gene namesi
Name:cpdAUniRule annotation
OrganismiPseudomonas aeruginosa
Taxonomic identifieri287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Pathology & Biotechi

Disruption phenotypei

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

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 231H → A: Loss of activity. 1 Publication
Mutagenesisi63 – 631D → A: Loss of activity. 1 Publication
Mutagenesisi93 – 931N → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2722723',5'-cyclic adenosine monophosphate phosphodiesterase CpdAPRO_0000413373Add
BLAST

Expressioni

Inductioni

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

Interactioni

Subunit structurei

Monomer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliD4P095.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cAMP phosphodiesterase class-III family.UniRule annotation

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
HAMAPiMF_00905. cAMP_phophodiest_CpdA.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.

Sequencei

Sequence statusi: Complete.

D4P095-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRHSNTPAT DASVLLVQLS DSHLFAEDGA RLLGMDTAHS LEKVVERVAR
60 70 80 90 100
EQPRIDLILA TGDVSQDGSL DSYTRFRRLS APLAAPLRWF AGNHDEREPM
110 120 130 140 150
QRATEGSDLL EQIVDVGNWR VVLLDSSIPG AVPGYLEDDQ LDLLRRAIDS
160 170 180 190 200
AGERFLLVSF HHHPVPIGSD WMDPIGLRNP QALFDLLAPY PQLRCLLWGH
210 220 230 240 250
IHQEFDRQRG PLRLLASPST CVQFAPGSSD FTLDRLAPGY RWLRLHDDGR
260 270
LETGISRVDD VVFEVDYDTA GY
Length:272
Mass (Da):30,472
Last modified:May 18, 2010 - v1
Checksum:i1C22AEBA58FD867F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU551724 Genomic DNA. Translation: ADD69827.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
GU551724 Genomic DNA. Translation: ADD69827.1.

3D structure databases

ProteinModelPortaliD4P095.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.4.53. 5087.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
HAMAPiMF_00905. cAMP_phophodiest_CpdA.
InterProiIPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMiSSF56300. SSF56300. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiCPDA_PSEAI
AccessioniPrimary (citable) accession number: D4P095
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: May 18, 2010
Last modified: April 1, 2015
This is version 20 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.