(data stored in SCRATCH zone)

SWISSPROT: Q3KJ15_PSEPF

ID   Q3KJ15_PSEPF            Unreviewed;       271 AA.
AC   Q3KJ15;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 93.
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   OrderedLocusNames=Pfl01_0497 {ECO:0000313|EMBL:ABA72241.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72241.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72241.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72241.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
CC   -!- FUNCTION: Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory
CC       role in modulating the intracellular concentration of cAMP,
CC       thereby influencing cAMP-dependent processes. {ECO:0000256|HAMAP-
CC       Rule:MF_00905}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3',5'-cyclic AMP + H2O = AMP + H(+);
CC         Xref=Rhea:RHEA:25277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58165, ChEBI:CHEBI:456215; EC=3.1.4.53;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00905};
CC   -!- COFACTOR:
CC       Name=a metal cation; Xref=ChEBI:CHEBI:25213;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00905};
CC       Note=Binds 2 metal cations per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00905};
CC   -!- SIMILARITY: Belongs to the cAMP phosphodiesterase class-III
CC       family. {ECO:0000256|HAMAP-Rule:MF_00905}.
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DR   EMBL; CP000094; ABA72241.1; -; Genomic_DNA.
DR   RefSeq; WP_011332161.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0497; -.
DR   EnsemblBacteria; ABA72241; ABA72241; Pfl01_0497.
DR   KEGG; pfo:Pfl01_0497; -.
DR   eggNOG; ENOG41070EG; Bacteria.
DR   eggNOG; COG1409; LUCA.
DR   HOGENOM; HOG000238351; -.
DR   KO; K03651; -.
DR   OMA; CAWLDQH; -.
DR   BioCyc; PFLU205922:G1G4S-502-MONOMER; -.
DR   Proteomes; UP000002704; 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_phophodiest_CpdA; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR026575; cAMP_Pdiest_CpdA.
DR   InterPro; IPR013622; CpdA_C.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   ProDom; PD587589; Calcineurin-like_phos_C; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3KJ15.
DR   SWISS-2DPAGE; Q3KJ15.
KW   cAMP {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   DOMAIN       16    202       Metallophos. {ECO:0000259|Pfam:PF00149}.
FT   NP_BIND      92     93       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   METAL        20     20       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        22     22       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        62     62       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        62     62       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        92     92       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       160    160       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       199    199       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       201    201       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   BINDING      22     22       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   BINDING      62     62       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   BINDING     201    201       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
SQ   SEQUENCE   271 AA;  30124 MW;  70358A854E38CAB4 CRC64;
     MPSVSTLTTA DTALLVQLSD SHLFAEADGT LLGMNTRESL QKVIDLVLEQ QPRIDLIVAS
     GDLSQDGTLE SYQLFRQMTA QIDAPARWIP GNHDEPQIMA RATVKSALLE SVVDVGNWRV
     TLLDSAVPGS VPGYLQDDQL QLLARSLSEA PDRHHLVCFH HHPVSIGCAW MEPIGLRNPE
     AFFEVLDRFP QARAVLWGHV HQEIDRERNG VRLIASPSTC IQFEPGSEDF KVGEQAPGYR
     WLRLLPDGRL ETGVERVTGF DFQVDYGSNG Y
//

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