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Database: UniProt
Entry: Q6DAC2_PECAS
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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
//
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