CPDA_VIBVU
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 03-AUG-2022, entry version 103.
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}; OrderedLocusNames=VV1_0608;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; AE016795; AAO09123.1; -; Genomic_DNA.
DR RefSeq; WP_011078692.1; NC_004459.3.
DR AlphaFoldDB; Q8DEI1; -.
DR SMR; Q8DEI1; -.
DR EnsemblBacteria; AAO09123; AAO09123; VV1_0608.
DR KEGG; vvu:VV1_0608; -.
DR HOGENOM; CLU_070320_0_0_6; -.
DR OMA; CAWLDQH; -.
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 Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 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
