CPDA_HAEIN
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 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};
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; Proteobacteria; 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;
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 -!- 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 RefSeq; WP_005693770.1; 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 OMA; CAWLDQH; -.
DR PhylomeDB; P44685; -.
DR BioCyc; HINF71421:G1GJ1-414-MON; -.
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 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 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
