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Q4FQ25 (CPDA_PSYA2) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 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
Ordered Locus Names:Psyc_2036
OrganismPsychrobacter arcticus (strain DSM 17307 / 273-4) [Complete proteome] [HAMAP]
Taxonomic identifier259536 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaePsychrobacter

Protein attributes

Sequence length279 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 – 2792793',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000413374

Regions

Nucleotide binding100 – 1012cAMP By similarity

Sites

Metal binding231Metal cation 1 By similarity
Metal binding251Metal cation 1 By similarity
Metal binding701Metal cation 1 By similarity
Metal binding701Metal cation 2 By similarity
Metal binding1001Metal cation 2 By similarity
Metal binding1791Metal cation 2 By similarity
Metal binding2181Metal cation 2 By similarity
Metal binding2201Metal cation 1 By similarity
Binding site251cAMP By similarity
Binding site701cAMP By similarity
Binding site2201cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4FQ25 [UniParc].

Last modified August 30, 2005. Version 1.
Checksum: CC5681C715B10231

FASTA27931,594
        10         20         30         40         50         60 
MPSYPVSTVN TPDGQVNVLQ ITDLHLSSHV PASDDETSSE VAVCQYSFEA IIKQALSKEI 

        70         80         90        100        110        120 
RCDLIVVTGD LVNKVEPAIY DHIFTVLQDT GIPFACIAGN HDVTDETGED LPFYQRTLIT 

       130        140        150        160        170        180 
RAADPRLLSR HLIESEHWQL LLLDSSITGK VEGEITATDI DWVREQLASC TKPALIALHH 

       190        200        210        220        230        240 
HVLPVDSEWI DSHMAKNAEE FWQHILPFEN LRVIINGHTH QEQTRHHQGV TVYSTPSTCY 

       250        260        270 
QFKPFEDNFA YDKKVRPGYR WLQLANNGKV ASWVERLDT 

« Hide

References

[1]"The genome sequence of Psychrobacter arcticus 273-4, a psychroactive Siberian permafrost bacterium, reveals mechanisms for adaptation to low-temperature growth."
Ayala-del-Rio H.L., Chain P.S., Grzymski J.J., Ponder M.A., Ivanova N., Bergholz P.W., Di Bartolo G., Hauser L., Land M., Bakermans C., Rodrigues D., Klappenbach J., Zarka D., Larimer F., Richardson P., Murray A., Thomashow M., Tiedje J.M.
Appl. Environ. Microbiol. 76:2304-2312(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17307 / 273-4.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000082 Genomic DNA. Translation: AAZ19883.1.
RefSeqYP_265317.1. NC_007204.1.

3D structure databases

ProteinModelPortalQ4FQ25.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING259536.Psyc_2036.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ19883; AAZ19883; Psyc_2036.
GeneID3516010.
KEGGpar:Psyc_2036.
PATRIC23059005. VBIPsyArc98534_2402.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000289889.
KOK03651.
OMAWREIELH.
OrthoDBEOG6QG8GQ.

Enzyme and pathway databases

BioCycPARC259536:GI3A-2086-MONOMER.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR013622. Calcineurin-like_phos_C.
IPR024654. Calcineurin-like_PHP_lpxH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF12850. Metallophos_2. 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_PSYA2
AccessionPrimary (citable) accession number: Q4FQ25
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: August 30, 2005
Last modified: June 11, 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