ID   CPDA_HAEIN              Reviewed;         274 AA.
AC   P44685;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   27-MAR-2024, entry version 126.
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=HI_0399;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=9721275; DOI=10.1128/jb.180.17.4401-4405.1998;
RA   Macfadyen L.P., Ma C., Redfield R.J.;
RT   "A 3',5' cyclic AMP (cAMP) phosphodiesterase modulates cAMP levels and
RT   optimizes competence in Haemophilus influenzae Rd.";
RL   J. Bacteriol. 180:4401-4405(1998).
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. May coordinate responses to
CC       nutritional stress, ensuring optimal competence development.
CC       {ECO:0000255|HAMAP-Rule:MF_00905, ECO:0000269|PubMed:9721275}.
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   -!- DISRUPTION PHENOTYPE: Mutants show increased levels of cellular cAMP.
CC       {ECO:0000269|PubMed:9721275}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC       III family. {ECO:0000255|HAMAP-Rule:MF_00905}.
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DR   EMBL; L42023; AAC22058.1; -; Genomic_DNA.
DR   PIR; E64065; E64065.
DR   RefSeq; NP_438561.1; NC_000907.1.
DR   AlphaFoldDB; P44685; -.
DR   SMR; P44685; -.
DR   STRING; 71421.HI_0399; -.
DR   DNASU; 949501; -.
DR   EnsemblBacteria; AAC22058; AAC22058; HI_0399.
DR   KEGG; hin:HI_0399; -.
DR   PATRIC; fig|71421.8.peg.418; -.
DR   eggNOG; COG1409; Bacteria.
DR   HOGENOM; CLU_070320_0_0_6; -.
DR   OrthoDB; 9784378at2; -.
DR   PhylomeDB; P44685; -.
DR   BioCyc; HINF71421:G1GJ1-414-MONOMER; -.
DR   Proteomes; UP000000579; 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..274
FT                   /note="3',5'-cyclic adenosine monophosphate
FT                   phosphodiesterase CpdA"
FT                   /id="PRO_0000084148"
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;  31556 MW;  A810BF2072CA4957 CRC64;
     MKNTFVYQAE KPVIKLLQIT DPHLFKDESA ELLGVNTQAS FAQVLKEIQQ ENNEFDVILA
     TGDLVQDSSD EGYIRFVEMM KPFNKPVFWI PGNHDFQPKM AEFLNQPPMN AAKHLLLGEH
     WQALLLDSQV YGVPHGQLSQ HQLDLLKETL GKNPERYTLV VLHHHLLPTN SAWLDQHNLR
     NSHELAEVLA PFTNVKAILY GHIHQEVNSE WNGYQVMATP ATCIQFKPDC QYFSLDTLQP
     GWREIELHSD GSIRTEVKRI QQAEFFPNMQ EEGY
//