(data stored in ACNUC1104 zone)

SWISSPROT: A4F6Q6_SACEN

ID   A4F6Q6_SACEN            Unreviewed;       255 AA.
AC   A4F6Q6;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 69.
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   ECO:0000313|EMBL:CAL99730.1};
GN   OrderedLocusNames=SACE_0382 {ECO:0000313|EMBL:CAL99730.1};
GN   ORFNames=A8924_0778 {ECO:0000313|EMBL:PFG93533.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99730.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99730.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728}, and NRRL 2338
RC   {ECO:0000313|EMBL:CAL99730.1};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
RN   [2] {ECO:0000313|EMBL:PFG93533.1, ECO:0000313|Proteomes:UP000225825}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40517 {ECO:0000313|EMBL:PFG93533.1,
RC   ECO:0000313|Proteomes:UP000225825};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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; AM420293; CAL99730.1; -; Genomic_DNA.
DR   EMBL; PDBV01000001; PFG93533.1; -; Genomic_DNA.
DR   STRING; 405948.SACE_0382; -.
DR   EnsemblBacteria; CAL99730; CAL99730; SACE_0382.
DR   KEGG; sen:SACE_0382; -.
DR   eggNOG; ENOG41070EG; Bacteria.
DR   eggNOG; COG1409; LUCA.
DR   HOGENOM; HOG000238352; -.
DR   KO; K03651; -.
DR   OMA; TGIGHMD; -.
DR   Proteomes; UP000006728; Chromosome.
DR   Proteomes; UP000225825; 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   HAMAP; MF_00905; cAMP_phophodiest_CpdA; 1.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR026575; cAMP_Pdiest_CpdA.
DR   Pfam; PF00149; Metallophos; 1.
PE   3: Inferred from homology;
DR   PRODOM; A4F6Q6.
DR   SWISS-2DPAGE; A4F6Q6.
KW   cAMP {ECO:0000256|HAMAP-Rule:MF_00905};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728,
KW   ECO:0000313|Proteomes:UP000225825};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728}.
FT   DOMAIN        4    194       Metallophos. {ECO:0000259|Pfam:PF00149}.
FT   NP_BIND      78     79       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   METAL        10     10       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        12     12       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        48     48       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        48     48       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL        78     78       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       152    152       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       191    191       Metal cation 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   METAL       193    193       Metal cation 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_00905}.
FT   BINDING      12     12       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   BINDING      48     48       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
FT   BINDING     193    193       cAMP. {ECO:0000256|HAMAP-Rule:MF_00905}.
SQ   SEQUENCE   255 AA;  26727 MW;  739EAE68EB531F0B CRC64;
     MTMAIAHLSD PHTTTGAQGD ESVERLRRGL DCVRALDRLP DCVVITGDVA DGGHRQEYEA
     VRAVIADFPV PVHLTTGNHD DPRGLAEVFG GTDVLGGARE ARYAVDYPGF TLVALDSHMP
     GSPGGRLGAD QLAWLDDVLA RRPDVPAVVC VHHPPVAVGI PYLDGMGMED AAEFAGVIAR
     HRNVARVLAG HVHRAVVADF AGATLTTAPS THIQIGFTTG EDVPPLHADP ASFLLHLIDG
     ASAVTHTLPI PPATG
//

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