ID CPDA_VIBVU Reviewed; 274 AA. AC Q8DEI1; DT 19-OCT-2011, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, 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}; GN OrderedLocusNames=VV1_0608; OS Vibrio vulnificus (strain CMCP6). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=216895; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMCP6; RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.; RT "Complete genome sequence of Vibrio vulnificus CMCP6."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. RN [2] RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE. RC STRAIN=ATCC 29307 / CDC A8694; RX PubMed=19028903; DOI=10.1128/jb.01350-08; RA Kim H.S., Kim S.M., Lee H.J., Park S.J., Lee K.H.; RT "Expression of the cpdA gene, encoding a 3',5'-cyclic AMP (cAMP) RT phosphodiesterase, is positively regulated by the cAMP-cAMP receptor RT protein complex."; RL J. Bacteriol. 191:922-930(2009). 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:0000305|PubMed:19028903}. 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 -!- INDUCTION: Positively regulated by the cAMP-CRP complex. CC {ECO:0000269|PubMed:19028903}. CC -!- DISRUPTION PHENOTYPE: Mutants show increased levels of cellular cAMP. CC {ECO:0000269|PubMed:19028903}. CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class- CC III family. {ECO:0000255|HAMAP-Rule:MF_00905}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016795; AAO09123.1; -; Genomic_DNA. DR RefSeq; WP_011078692.1; NC_004459.3. DR AlphaFoldDB; Q8DEI1; -. DR SMR; Q8DEI1; -. DR KEGG; vvu:VV1_0608; -. DR HOGENOM; CLU_070320_0_0_6; -. DR Proteomes; UP000002275; Chromosome 1. 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 2: Evidence at transcript level; KW cAMP; Hydrolase; Iron; Metal-binding; Nucleotide-binding. FT CHAIN 1..274 FT /note="3',5'-cyclic adenosine monophosphate FT phosphodiesterase CpdA" FT /id="PRO_0000413383" FT BINDING 21 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 23 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 23 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 63 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 63 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 63 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 93..94 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 93 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 163 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 202 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 204 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" FT BINDING 204 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00905" SQ SEQUENCE 274 AA; 30578 MW; 742F2E48490227E7 CRC64; MQHTSSDTLS ENSIKLLQIT DTHLFASDEG SLLSVKTLQS FQAVVEQVMA RHVEFDYLLA TGDISQDHSA ASYQRFADGI APLEKACFWL PGNHDYKPNM SSVLPSPQIT TPEQVELNAH WQLILLDSQV VGVPHGRLSD QQLLMLEHHL QASPEKNTLI LLHHHPLLVG SAWLDQHTLK DAEAFWQIVE RFPMVKGIVC GHVHQDMNVM HKGIRVMATP STCVQFKPKS DDFALDTVSP GWRELTLHAN GEITTQVQRL ASGSFLPDFT SSGY //