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D4P095

- CPDA_PSEAI

UniProt

D4P095 - CPDA_PSEAI

Protein

3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA

Gene

cpdA

Organism
Pseudomonas aeruginosa
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 18 (01 Oct 2014)
      Sequence version 1 (18 May 2010)
      Previous versions | rss
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    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.1 PublicationUniRule annotation

    Catalytic activityi

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

    Cofactori

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

    Enzyme regulationi

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

    Kineticsi

    1. KM=7.2 µM for cAMP1 Publication

    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

    1. 3',5'-cyclic-AMP phosphodiesterase activity Source: UniProtKB-HAMAP
    2. metal ion binding Source: UniProtKB-HAMAP
    3. nucleotide binding Source: UniProtKB-HAMAP

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    cAMP, Iron, Metal-binding, Nucleotide-binding

    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

    MSRHSNTPAT DASVLLVQLS DSHLFAEDGA RLLGMDTAHS LEKVVERVAR    50
    EQPRIDLILA TGDVSQDGSL DSYTRFRRLS APLAAPLRWF AGNHDEREPM 100
    QRATEGSDLL EQIVDVGNWR VVLLDSSIPG AVPGYLEDDQ LDLLRRAIDS 150
    AGERFLLVSF HHHPVPIGSD WMDPIGLRNP QALFDLLAPY PQLRCLLWGH 200
    IHQEFDRQRG PLRLLASPST CVQFAPGSSD FTLDRLAPGY RWLRLHDDGR 250
    LETGISRVDD VVFEVDYDTA GY 272
    Length:272
    Mass (Da):30,472
    Last modified:May 18, 2010 - v1
    Checksum:i1C22AEBA58FD867F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GU551724 Genomic DNA. Translation: ADD69827.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    GU551724 Genomic DNA. Translation: ADD69827.1 .

    3D structure databases

    ProteinModelPortali D4P095.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 3.60.21.10. 1 hit.
    HAMAPi MF_00905. cAMP_phophodiest_CpdA.
    InterProi IPR004843. Calcineurin-like_PHP_apaH.
    IPR026575. cAMP_Pdiest_CpdA.
    IPR029052. Metallo-depent_PP-like.
    [Graphical view ]
    Pfami PF00149. Metallophos. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56300. SSF56300. 1 hit.
    ProtoNeti Search...

    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: October 1, 2014
    This is version 18 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