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Q6NDI4 (CPDA_RHOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 51. 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:RPA0124
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length274 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 – 2742743',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000413377

Regions

Nucleotide binding79 – 802cAMP By similarity

Sites

Metal binding81Metal cation 1 By similarity
Metal binding101Metal cation 1 By similarity
Metal binding491Metal cation 1 By similarity
Metal binding491Metal cation 2 By similarity
Metal binding791Metal cation 2 By similarity
Metal binding1551Metal cation 2 By similarity
Metal binding1941Metal cation 2 By similarity
Metal binding1961Metal cation 1 By similarity
Binding site101cAMP By similarity
Binding site491cAMP By similarity
Binding site1961cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NDI4 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 2144858507B12CCE

FASTA27430,646
        10         20         30         40         50         60 
MKFVVLTDTH FVARGRRIYG LDPAERLSAA VARINREHPD IAFVIVTGDL AHWGEEPAYD 

        70         80         90        100        110        120 
NLASVLAGLR APTILMMGNH DKREAFAKFF PGVPRDASGF VQTVQVFEAA TIVTLDTLNE 

       130        140        150        160        170        180 
AAPNHEGFLC EARLAFLEHA LAEAPADRPL LLFQHHPPFD TGLRYMDTIR LANPDAEWEV 

       190        200        210        220        230        240 
IARTRKPDYL FMGHLHRPIS GVWRGIPFHI QRGLAHQVAF DLVAEGHIPG SHEPPDYAHV 

       250        260        270 
SVEADRIVIH QCSFMYDGPL FSLHDSVALH RVSF 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris."
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.
Nat. Biotechnol. 22:55-61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX572593 Genomic DNA. Translation: CAE25568.1.
RefSeqNP_945477.1. NC_005296.1.

3D structure databases

ProteinModelPortalQ6NDI4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING258594.RPA0124.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE25568; CAE25568; RPA0124.
GeneID2689514.
KEGGrpa:RPA0124.
PATRIC23284351. VBIRhoPal84835_0128.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000238352.
OMAAAPNHEG.
OrthoDBEOG6DG2VB.
PhylomeDBQ6NDI4.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR024654. Calcineurin-like_PHP_lpxH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF12850. Metallophos_2. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCPDA_RHOPA
AccessionPrimary (citable) accession number: Q6NDI4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: July 5, 2004
Last modified: July 9, 2014
This is version 51 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