ID Q6DAC2_PECAS Unreviewed; 275 AA.
AC Q6DAC2;
DT 16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE RecName: Full=3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA {ECO:0000256|HAMAP-Rule:MF_00905};
DE Short=3',5'-cyclic AMP phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_00905};
DE Short=cAMP phosphodiesterase {ECO:0000256|HAMAP-Rule:MF_00905};
DE EC=3.1.4.53 {ECO:0000256|HAMAP-Rule:MF_00905};
GN Name=icc {ECO:0000313|EMBL:CAG73252.1};
GN Synonyms=cpdA {ECO:0000256|HAMAP-Rule:MF_00905};
GN OrderedLocusNames=ECA0333 {ECO:0000313|EMBL:CAG73252.1};
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491 {ECO:0000313|EMBL:CAG73252.1, ECO:0000313|Proteomes:UP000007966};
RN [1] {ECO:0000313|EMBL:CAG73252.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SCRI1043 {ECO:0000313|EMBL:CAG73252.1};
RA Bell K.S., Sebaihia M., Pritchard L., Holden M., Hyman L.J., Holeva M.C.,
RA Thomson N.R., Bentley S.D., Churcher C., Mungall K., Atkin R., Bason N.,
RA Brooks K., Chillingworth T., Clark K., Doggett J., Fraser A., Hance Z.,
RA Hauser H., Jagels K., Moule S., Norbertczak H., Ormond D., Price C.,
RA Quail M.A., Sanders M., Walker D., Whitehead S., Salmond G.P.C.,
RA Birch P.R.J., Barrell B.G., Parkhill J., Toth I.K.;
RT "The genome sequence of the enterobacterial phytopathogen Erwinia
RT carotovora subsp. atroseptica SCRI1043 and functional genomic
RT identification of novel virulence factors.";
RL Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-
CC Rule:MF_00905}.
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:0000256|HAMAP-
CC Rule:MF_00905};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00905};
CC Note=Binds 2 Fe(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_00905};
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-
CC III family. {ECO:0000256|ARBA:ARBA00025742, ECO:0000256|HAMAP-
CC Rule:MF_00905}.
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DR EMBL; BX950851; CAG73252.1; -; Genomic_DNA.
DR RefSeq; WP_011091963.1; NC_004547.2.
DR AlphaFoldDB; Q6DAC2; -.
DR STRING; 218491.ECA0333; -.
DR KEGG; eca:ECA0333; -.
DR PATRIC; fig|218491.5.peg.334; -.
DR eggNOG; COG1409; Bacteria.
DR HOGENOM; CLU_070320_0_0_6; -.
DR OMA; CAWLDQH; -.
DR OrthoDB; 9784378at2; -.
DR Proteomes; UP000007966; 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; 3',5'-CYCLIC ADENOSINE MONOPHOSPHATE PHOSPHODIESTERASE CPDA; 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 {ECO:0000256|HAMAP-Rule:MF_00905};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00905};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00905};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00905}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00905};
KW Reference proteome {ECO:0000313|Proteomes:UP000007966}.
FT DOMAIN 16..206
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT BINDING 22
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 24
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 24
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 64
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 64
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 94..95
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 94
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 164
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 203
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 205
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
FT BINDING 205
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00905"
SQ SEQUENCE 275 AA; 31048 MW; 99184E51400BF925 CRC64;
MESLLTLPVA SGARVRILQI TDTHLFAGEH ETLLGINTYR SYHAVLDAIK ARQDAFDLIV
ATGDLAQDHT LQAYHHFSRA IAQIPAPCVW LPGNHDFQPA MVDALADAGI APSKHVLLGD
KWQIILLDSQ VFGVPHGELS EYQLEWLERS LKSQPDRFTL LLLHHHPHPS GCTWLDQHSL
RNAHNLSAVL DRYPQVNTVL CGHIHQEMDF DWHGRRLLAT PSTCVQFKPH CTNFTIDNMA
PGWRYLDLLP DGRLETEVYR LSGSEFLPDM DSDGY
//