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Q7U7W2 (CPDA_SYNPX) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 54. 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:SYNW0868
OrganismSynechococcus sp. (strain WH8102) [Complete proteome] [HAMAP]
Taxonomic identifier84588 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length253 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)
   Biological_processmetabolic process

Inferred from electronic annotation. Source: GOC

   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 – 2532533',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000413381

Regions

Nucleotide binding79 – 802cAMP By similarity

Sites

Metal binding81Metal cation 1 By similarity
Metal binding101Metal cation 1 By similarity
Metal binding481Metal cation 1 By similarity
Metal binding481Metal cation 2 By similarity
Metal binding791Metal cation 2 By similarity
Metal binding1501Metal cation 2 By similarity
Metal binding1891Metal cation 2 By similarity
Metal binding1911Metal cation 1 By similarity
Binding site101cAMP By similarity
Binding site481cAMP By similarity
Binding site1911cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7U7W2 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 9369C1267CB53C56

FASTA25327,994
        10         20         30         40         50         60 
MRILQLSDPH LVAADAALVR ERPAMTLLDR ALLEGQRSHP DLVLISGDLC QDESWGGYVR 

        70         80         90        100        110        120 
LGRLLDRHVN VPVGLLPGNH DDPLLLKAVL GRRFCTAPAE LIVQGTRLVL LNSHRSGCSA 

       130        140        150        160        170        180 
GWLGPHQLQW LQERLADPLR RDLPLVVALH HPPVAIGHPV MDTMNLSDHH QLAAILQPHA 

       190        200        210        220        230        240 
ALRAVVFGHI HQHWHGTWPQ RPDVPLLGCP STLRSFQCVQ PCPLGRAEDP GGRLLEIHND 

       250 
GSLSHQVLRW SPC 

« Hide

References

[1]"The genome of a motile marine Synechococcus."
Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.
Nature 424:1037-1042(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: WH8102.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX569691 Genomic DNA. Translation: CAE07383.1.
RefSeqNP_896961.1. NC_005070.1.

3D structure databases

ProteinModelPortalQ7U7W2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING84588.SYNW0868.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE07383; CAE07383; SYNW0868.
GeneID1730957.
KEGGsyw:SYNW0868.
PATRIC23833193. VBISynSp27240_0903.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238351.
KOK03651.
OMAGHIHQHW.
OrthoDBEOG6QG8GQ.
ProtClustDBCLSK826164.

Family and domain databases

HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR026575. cAMP_Pdiest_CpdA.
IPR004843. PEstase_dom.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPDA_SYNPX
AccessionPrimary (citable) accession number: Q7U7W2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: October 1, 2003
Last modified: February 19, 2014
This is version 54 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