CNPD3_PSEAI
ID CNPD3_PSEAI Reviewed; 272 AA.
AC D4P095;
DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA {ECO:0000305};
DE Short=3',5'-cyclic AMP phosphodiesterase {ECO:0000305};
DE Short=cAMP phosphodiesterase {ECO:0000303|PubMed:20348254};
DE EC=3.1.4.53 {ECO:0000269|PubMed:20348254};
GN Name=cpdA {ECO:0000303|PubMed:20348254};
OS Pseudomonas aeruginosa.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF HIS-23; ASP-63 AND ASN-93.
RC STRAIN=PAK;
RX PubMed=20348254; DOI=10.1128/jb.00168-10;
RA Fuchs E.L., Brutinel E.D., Klem E.R., Fehr A.R., Yahr T.L., Wolfgang M.C.;
RT "In vitro and in vivo characterization of the Pseudomonas aeruginosa cyclic
RT AMP (cAMP) phosphodiesterase CpdA, required for cAMP homeostasis and
RT virulence factor regulation.";
RL J. Bacteriol. 192:2779-2790(2010).
CC -!- FUNCTION: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role
CC in modulating the intracellular concentration of cAMP, thereby
CC influencing cAMP-dependent processes. Specifically required for
CC regulation of virulence factors. Can also hydrolyze cGMP, but cGMP is
CC unlikely to be synthesized by P.aeruginosa and cAMP is probably the
CC biologically relevant substrate for CpdA in vivo.
CC {ECO:0000269|PubMed:20348254}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic AMP + H2O = AMP + H(+); Xref=Rhea:RHEA:25277,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58165,
CC ChEBI:CHEBI:456215; EC=3.1.4.53;
CC Evidence={ECO:0000269|PubMed:20348254};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:20348254};
CC Note=Binds 2 metal cations per subunit. Site 1 may preferentially bind
CC Fe(3+) ions, while site 2 may have a preference for Fe(2+) ions.
CC {ECO:0000269|PubMed:20348254};
CC -!- ACTIVITY REGULATION: Activated by iron. Other divalent metal ions have
CC no effect. {ECO:0000269|PubMed:20348254}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.2 uM for cAMP {ECO:0000269|PubMed:20348254};
CC Vmax=3.4 nmol/min/ng enzyme {ECO:0000269|PubMed:20348254};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20348254}.
CC -!- INDUCTION: Positively regulated by Vfr in response to elevated
CC intracellular cAMP. {ECO:0000269|PubMed:20348254}.
CC -!- DISRUPTION PHENOTYPE: Mutants show increased levels of cellular cAMP.
CC In rich medium, mutants exhibit a significantly reduced growth rate
CC compared to wild-type strain. {ECO:0000269|PubMed:20348254}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC III family. {ECO:0000305}.
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DR EMBL; GU551724; ADD69827.1; -; Genomic_DNA.
DR RefSeq; WP_016253970.1; NZ_MCMY01000004.1.
DR AlphaFoldDB; D4P095; -.
DR SMR; D4P095; -.
DR eggNOG; COG1409; Bacteria.
DR BRENDA; 3.1.4.53; 5087.
DR SABIO-RK; D4P095; -.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR CDD; cd07402; MPP_GpdQ; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR026575; GpdQ/CpdA-like.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 1: Evidence at protein level;
KW cAMP; Hydrolase; Iron; Metal-binding; Nucleotide-binding.
FT CHAIN 1..272
FT /note="3',5'-cyclic adenosine monophosphate
FT phosphodiesterase CpdA"
FT /id="PRO_0000413373"
FT BINDING 21
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 23
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 23
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 63
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 63
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 93..94
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 93
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 161
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 200
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT BINDING 202
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250|UniProtKB:P9WP65"
FT BINDING 202
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT MUTAGEN 23
FT /note="H->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20348254"
FT MUTAGEN 63
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20348254"
FT MUTAGEN 93
FT /note="N->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:20348254"
SQ SEQUENCE 272 AA; 30472 MW; 1C22AEBA58FD867F CRC64;
MSRHSNTPAT DASVLLVQLS DSHLFAEDGA RLLGMDTAHS LEKVVERVAR EQPRIDLILA
TGDVSQDGSL DSYTRFRRLS APLAAPLRWF AGNHDEREPM QRATEGSDLL EQIVDVGNWR
VVLLDSSIPG AVPGYLEDDQ LDLLRRAIDS AGERFLLVSF HHHPVPIGSD WMDPIGLRNP
QALFDLLAPY PQLRCLLWGH IHQEFDRQRG PLRLLASPST CVQFAPGSSD FTLDRLAPGY
RWLRLHDDGR LETGISRVDD VVFEVDYDTA GY
