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Database: UniProt
Entry: G5SGZ0_SALET
LinkDB: G5SGZ0_SALET
Original site: G5SGZ0_SALET 
ID   G5SGZ0_SALET            Unreviewed;       275 AA.
AC   G5SGZ0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 45.
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=cpdA {ECO:0000256|HAMAP-Rule:MF_00905};
GN   ORFNames=LTSEWAN_4833 {ECO:0000313|EMBL:EHC99765.1};
OS   Salmonella enterica subsp. enterica serovar Wandsworth str. A4-580.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913086 {ECO:0000313|EMBL:EHC99765.1, ECO:0000313|Proteomes:UP000003536};
RN   [1] {ECO:0000313|EMBL:EHC99765.1, ECO:0000313|Proteomes:UP000003536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-580 {ECO:0000313|EMBL:EHC99765.1,
RC   ECO:0000313|Proteomes:UP000003536};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHC99765.1}.
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DR   EMBL; AFCX01001570; EHC99765.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5SGZ0; -.
DR   PATRIC; fig|913086.3.peg.3732; -.
DR   Proteomes; UP000003536; Unassembled WGS sequence.
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}.
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;  31021 MW;  3147959700D95DFD CRC64;
     MESLLTLPLA GEARVRILQI TDTHLFAEKH ETLLGVNTWE SYQAVLEAIR AQQYEYDLIV
     ATGDLAQDQS AAAYQHFAEG IASFRAPCVW LPGNHDFQPA MYSALQEAGI SPAKRVLIGE
     QWQILLLDSQ VFGVPHGELS EFQLEWLERK LADAPERQTL LLLHHHPLPA GCSWLDQHSL
     RNAGELDSVL ANFPRVKYLL CGHIHQELDL DWNGRRLLAS PSTCVQFKPH CANFTLDTIA
     PGWRTLELRA NGVLETEVHR LQDTRFRPDT ASEGY
//
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