ID   CPDA_ECO57              Reviewed;         275 AA.
AC   P0AEW5; P36650;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA {ECO:0000255|HAMAP-Rule:MF_00905};
DE            Short=3',5'-cyclic AMP phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_00905};
DE            Short=cAMP phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_00905};
DE            EC=3.1.4.53 {ECO:0000255|HAMAP-Rule:MF_00905};
GN   Name=cpdA {ECO:0000255|HAMAP-Rule:MF_00905}; Synonyms=icc;
GN   OrderedLocusNames=Z4389, ECs3920;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00905}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00905};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00905};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00905};
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC       III family. {ECO:0000255|HAMAP-Rule:MF_00905}.
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DR   EMBL; AE005174; AAG58171.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37343.1; -; Genomic_DNA.
DR   PIR; G85963; G85963.
DR   PIR; H91118; H91118.
DR   RefSeq; NP_311947.1; NC_002695.1.
DR   RefSeq; WP_000444747.1; NZ_VOAI01000009.1.
DR   AlphaFoldDB; P0AEW5; -.
DR   SMR; P0AEW5; -.
DR   STRING; 155864.Z4389; -.
DR   GeneID; 75203574; -.
DR   GeneID; 916255; -.
DR   KEGG; ece:Z4389; -.
DR   KEGG; ecs:ECs_3920; -.
DR   PATRIC; fig|386585.9.peg.4088; -.
DR   eggNOG; COG1409; Bacteria.
DR   HOGENOM; CLU_070320_0_0_6; -.
DR   OMA; CAWLDQH; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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   HAMAP; MF_00905; cAMP_phosphodiest_CpdA; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR046379; cAMP_phosphodiest_CpdA.
DR   InterPro; IPR026575; GpdQ/CpdA-like.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   PANTHER; PTHR42988:SF2; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE CBUA0032-RELATED; 1.
DR   PANTHER; PTHR42988; PHOSPHOHYDROLASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   cAMP; Hydrolase; Iron; Metal-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..275
FT                   /note="3',5'-cyclic adenosine monophosphate
FT                   phosphodiesterase CpdA"
FT                   /id="PRO_0000084147"
FT   BINDING         22
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         24
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         24
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         64
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         94..95
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         164
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         203
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         205
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00905"
SQ   SEQUENCE   275 AA;  30938 MW;  97696478536CFBF1 CRC64;
     MESLLTLPLA GEARVRILQI TDTHLFAQKH EALLGVNTWE SYQAVLEAIR PHQHEFDLIV
     ATGDLAQDQS SAAYQHFAEG IASFRAPCVW LPGNHDFQPA MYSALQDAGI SPAKRVFIGE
     QWQILLLDSQ VFGVPHGELS EFQLEWLERK LADAPERHTL LLLHHHPLPA GCSWLDQHSL
     RNAGELDTVL AKFPHVKYLL CGHIHQELDL DWNGRRLLAT PSTCVQFKPH CSNFTLDTIA
     PGWRTLELHA DGTLTTEVHR LADTRFQPDT ASEGY
//