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P0AEW4 (CPDA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
Short name=3',5'-cyclic AMP phosphodiesterase
Short name=cAMP phosphodiesterase
EC=3.1.4.17
Gene names
Name:cpdA
Synonyms:icc
Ordered Locus Names:b3032, JW3000
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Specific for cAMP. Ref.1

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. Ref.1

Cofactor

Binds 2 metal cations per subunit By similarity.

Enzyme regulation

Activated by iron. Ref.1

Sequence similarities

Belongs to the cAMP phosphodiesterase class-III family.

Biophysicochemical properties

Kinetic parameters:

KM=0.5 mM for cAMP Ref.1

Vmax=2.0 µmol/min/mg enzyme

Sequence caution

The sequence AAA69200.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2752753',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000084146

Regions

Nucleotide binding94 – 952cAMP By similarity

Sites

Metal binding221Metal cation 1 By similarity
Metal binding241Metal cation 1 By similarity
Metal binding641Metal cation 1 By similarity
Metal binding641Metal cation 2 By similarity
Metal binding941Metal cation 2 By similarity
Metal binding1641Metal cation 2 By similarity
Metal binding2031Metal cation 2 By similarity
Metal binding2051Metal cation 1 By similarity
Binding site241cAMP By similarity
Binding site641cAMP By similarity
Binding site2051cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
P0AEW4 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: 97696478536CFBF1

FASTA27530,938
        10         20         30         40         50         60 
MESLLTLPLA GEARVRILQI TDTHLFAQKH EALLGVNTWE SYQAVLEAIR PHQHEFDLIV 

        70         80         90        100        110        120 
ATGDLAQDQS SAAYQHFAEG IASFRAPCVW LPGNHDFQPA MYSALQDAGI SPAKRVFIGE 

       130        140        150        160        170        180 
QWQILLLDSQ VFGVPHGELS EFQLEWLERK LADAPERHTL LLLHHHPLPA GCSWLDQHSL 

       190        200        210        220        230        240 
RNAGELDTVL AKFPHVKYLL CGHIHQELDL DWNGRRLLAT PSTCVQFKPH CSNFTLDTIA 

       250        260        270 
PGWRTLELHA DGTLTTEVHR LADTRFQPDT ASEGY

« Hide

References

« Hide 'large scale' references
[1]"Identification of the cpdA gene encoding cyclic 3',5'-adenosine monophosphate phosphodiesterase in Escherichia coli."
Imamura R., Yamanaka K., Ogura T., Hiraga S., Fujita N., Ishihama A., Niki H.
J. Biol. Chem. 271:25423-25429(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18, GENE NAME, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: K12.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"3',5' Cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism."
Richter W.
Proteins 46:278-286(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY, NOMENCLATURE, MODELING OF METAL-BINDING SITES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D16557 Genomic DNA. Translation: BAA03989.1.
U28377 Genomic DNA. Translation: AAA69200.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76068.1.
AP009048 Genomic DNA. Translation: BAE77088.1.
PIRF65090.
RefSeqNP_417504.1. NC_000913.2.
YP_491224.1. NC_007779.1.

3D structure databases

ProteinModelPortalP0AEW4.
ModBaseSearch...

Protein-protein interaction databases

IntActP0AEW4. 8 interactions.
STRING511145.b3032.

Proteomic databases

PaxDbP0AEW4.
PRIDEP0AEW4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76068; AAC76068; b3032.
BAE77088; BAE77088; BAE77088.
GeneID12933401.
947515.
KEGGecj:Y75_p2958.
eco:b3032.
PATRIC32121474. VBIEscCol129921_3124.

Organism-specific databases

EchoBASEEB2104.
EcoGeneEG12187. cpdA.

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238351.
KOK03651.
OMACAWLDQH.
ProtClustDBPRK11148.

Enzyme and pathway databases

BioCycEcoCyc:G7579-MONOMER.
ECOL316407:JW3000-MONOMER.
MetaCyc:G7579-MONOMER.

Gene expression databases

GenevestigatorP0AEW4.

Family and domain databases

HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR013622. Calcineurin-like_phos_C.
IPR026575. cAMP_Pdiest_CpdA.
IPR004843. Metallo_PEstase_dom.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProDomPD587589. Calcineurin-like_phos_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
ProtoNetSearch...

Entry information

Entry nameCPDA_ECOLI
AccessionPrimary (citable) accession number: P0AEW4
Secondary accession number(s): P36650, Q2M9G8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 1, 2013
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

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