CPDA_ECOLI
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 03-AUG-2022, entry version 120.
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, ECO:0000303|PubMed:8810311};
GN Synonyms=icc; OrderedLocusNames=b3032, JW3000;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; 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=2.0 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; P0AEW4; -.
DR PRIDE; P0AEW4; -.
DR EnsemblBacteria; AAC76068; AAC76068; b3032.
DR EnsemblBacteria; BAE77088; BAE77088; BAE77088.
DR GeneID; 66673069; -.
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 PhylomeDB; P0AEW4; -.
DR BioCyc; EcoCyc:G7579-MON; -.
DR BioCyc; MetaCyc:G7579-MON; -.
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 GO; GO:0042545; P:cell wall modification; IBA:GO_Central.
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 Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 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
