ID   CPDA_ECOLI              Reviewed;         275 AA.
AC   P0AEW4; P36650; Q2M9G8;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   27-MAR-2024, entry version 128.
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, ECO:0000269|PubMed:8810311};
GN   Name=cpdA {ECO:0000255|HAMAP-Rule:MF_00905,
GN   ECO:0000303|PubMed:8810311}; Synonyms=icc;
GN   OrderedLocusNames=b3032, JW3000;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18, GENE NAME,
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K12;
RX   PubMed=8810311; DOI=10.1074/jbc.271.41.25423;
RA   Imamura R., Yamanaka K., Ogura T., Hiraga S., Fujita N., Ishihama A.,
RA   Niki H.;
RT   "Identification of the cpdA gene encoding cyclic 3',5'-adenosine
RT   monophosphate phosphodiesterase in Escherichia coli.";
RL   J. Biol. Chem. 271:25423-25429(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   GENE FAMILY, NOMENCLATURE, AND MODELING OF METAL-BINDING SITES.
RX   PubMed=11835503; DOI=10.1002/prot.10049;
RA   Richter W.;
RT   "3',5' Cyclic nucleotide phosphodiesterases class III: members, structure,
RT   and catalytic mechanism.";
RL   Proteins 46:278-286(2002).
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. Specific for cAMP.
CC       {ECO:0000255|HAMAP-Rule:MF_00905, ECO:0000269|PubMed:8810311}.
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, ECO:0000269|PubMed:8810311};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000250|UniProtKB:Q6XBH1, ECO:0000305|PubMed:8810311};
CC       Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:Q6XBH1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.5 mM for cAMP {ECO:0000269|PubMed:8810311};
CC         Vmax=2 umol/min/mg enzyme {ECO:0000269|PubMed:8810311};
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC       III family. {ECO:0000255|HAMAP-Rule:MF_00905,
CC       ECO:0000303|PubMed:11835503}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA69200.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; D16557; BAA03989.1; -; Genomic_DNA.
DR   EMBL; U28377; AAA69200.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76068.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77088.1; -; Genomic_DNA.
DR   PIR; F65090; F65090.
DR   RefSeq; NP_417504.1; NC_000913.3.
DR   RefSeq; WP_000444747.1; NZ_STEB01000001.1.
DR   AlphaFoldDB; P0AEW4; -.
DR   SMR; P0AEW4; -.
DR   BioGRID; 4262395; 9.
DR   BioGRID; 851832; 2.
DR   IntAct; P0AEW4; 10.
DR   STRING; 511145.b3032; -.
DR   jPOST; P0AEW4; -.
DR   PaxDb; 511145-b3032; -.
DR   EnsemblBacteria; AAC76068; AAC76068; b3032.
DR   GeneID; 75203574; -.
DR   GeneID; 947515; -.
DR   KEGG; ecj:JW3000; -.
DR   KEGG; eco:b3032; -.
DR   PATRIC; fig|1411691.4.peg.3699; -.
DR   EchoBASE; EB2104; -.
DR   eggNOG; COG1409; Bacteria.
DR   HOGENOM; CLU_070320_0_0_6; -.
DR   InParanoid; P0AEW4; -.
DR   OMA; CAWLDQH; -.
DR   OrthoDB; 9784378at2; -.
DR   PhylomeDB; P0AEW4; -.
DR   BioCyc; EcoCyc:G7579-MONOMER; -.
DR   BioCyc; MetaCyc:G7579-MONOMER; -.
DR   BRENDA; 3.1.4.53; 2026.
DR   SABIO-RK; P0AEW4; -.
DR   PRO; PR:P0AEW4; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IDA:EcoCyc.
DR   GO; GO:0008198; F:ferrous iron binding; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   cAMP; Direct protein sequencing; Hydrolase; Iron; Metal-binding;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..275
FT                   /note="3',5'-cyclic adenosine monophosphate
FT                   phosphodiesterase CpdA"
FT                   /id="PRO_0000084146"
FT   BINDING         22
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         24
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         24
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         64
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         64
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         94..95
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         94
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         164
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         203
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
FT   BINDING         205
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000250|UniProtKB:P9WP65"
FT   BINDING         205
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q6XBH1"
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
//