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C1A2D8 (CPDA_RHOE4) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 28. 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
Ordered Locus Names:RER_40650
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length301 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 – 3013013',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000413376

Regions

Nucleotide binding95 – 962cAMP By similarity

Sites

Metal binding201Metal cation 1 By similarity
Metal binding221Metal cation 1 By similarity
Metal binding611Metal cation 1 By similarity
Metal binding611Metal cation 2 By similarity
Metal binding951Metal cation 2 By similarity
Metal binding1671Metal cation 2 By similarity
Metal binding2051Metal cation 2 By similarity
Metal binding2071Metal cation 1 By similarity
Binding site221cAMP By similarity
Binding site611cAMP By similarity
Binding site2071cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
C1A2D8 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: BA8DC406C6774B8F

FASTA30132,343
        10         20         30         40         50         60 
MSVRSAEYPR PKHFLVHLSD THLVAQGELY DAVDASTRLR EVLSGIVASG ARPDALIFTG 

        70         80         90        100        110        120 
DLTDQGHPDA YAELKAIVEP VAAEIDAQVI WAMGNHDDRS TFRSLLLGED ATDHPVDNVY 

       130        140        150        160        170        180 
DLDGLRVITL DSSVPGHHYG EISDRQLDWL RSELAVPAPD GTILALHHPP VPCIQDLAVL 

       190        200        210        220        230        240 
VELRDQSRLA DVLRGSDVRA ILAGHLHYST TATFAGIPVS VASSTCYTQD LNVEVGGQRG 

       250        260        270        280        290        300 
RDGAQGCNLV HVYDETIVHS VVPLGAHVTV GEPVDADEGA RRLSAAGIRI LESEKAGRSI 


V 

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References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008957 Genomic DNA. Translation: BAH34773.1.
RefSeqYP_002767512.1. NC_012490.1.

3D structure databases

ProteinModelPortalC1A2D8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING234621.RER_40650.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAH34773; BAH34773; RER_40650.
GeneID7711563.
KEGGrer:RER_40650.
PATRIC23194675. VBIRhoEry66701_4600.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238352.
OMATGIGHMD.
OrthoDBEOG6QG8GQ.
ProtClustDBCLSK790749.

Enzyme and pathway databases

BioCycRERY234621:GHDE-4123-MONOMER.

Family and domain databases

HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCPDA_RHOE4
AccessionPrimary (citable) accession number: C1A2D8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: May 26, 2009
Last modified: April 16, 2014
This is version 28 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