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P0AEW5 (CPDA_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:Z4389, ECs3920
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_00905

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. HAMAP-Rule MF_00905

Cofactor

Binds 2 metal cations per subunit By similarity. HAMAP-Rule MF_00905

Sequence similarities

Belongs to the cAMP phosphodiesterase class-III family.

Ontologies

Keywords
   LigandcAMP
Metal-binding
Nucleotide-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_function3',5'-cyclic-AMP phosphodiesterase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

nucleotide binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2752753',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000084147

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
P0AEW5 [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

[1]"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7."
Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. expand/collapse author list , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R.
Nature 409:529-533(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
[2]"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. expand/collapse author list , Kuhara S., Shiba T., Hattori M., Shinagawa H.
DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG58171.1.
BA000007 Genomic DNA. Translation: BAB37343.1.
PIRG85963.
H91118.
RefSeqNP_289612.1. NC_002655.2.
NP_311947.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0AEW5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING155864.Z4389.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG58171; AAG58171; Z4389.
BAB37343; BAB37343; BAB37343.
GeneID916255.
958507.
KEGGece:Z4389.
ecs:ECs3920.
PATRIC18357331. VBIEscCol44059_3843.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238351.
KOK03651.
OMAWREIELH.
OrthoDBEOG6QG8GQ.

Enzyme and pathway databases

BioCycECOL386585:GJFA-3879-MONOMER.
ECOO157:ICC-MONOMER.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR013622. Calcineurin-like_phos_C.
IPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProDomPD587589. Calcineurin-like_phos_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMSSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCPDA_ECO57
AccessionPrimary (citable) accession number: P0AEW5
Secondary accession number(s): P36650
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: June 11, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families