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P05675 (CPDA_SYNP6) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 78. 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:syc0937_d
OrganismSynechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) [Complete proteome] [HAMAP]
Taxonomic identifier269084 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus

Protein attributes

Sequence length255 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.

Sequence caution

The sequence CAA27241.1 differs from that shown. Reason: Frameshift at position 102.

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 – 2552553',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000066100

Regions

Nucleotide binding89 – 902cAMP By similarity

Sites

Metal binding191Metal cation 1 By similarity
Metal binding211Metal cation 1 By similarity
Metal binding591Metal cation 1 By similarity
Metal binding591Metal cation 2 By similarity
Metal binding891Metal cation 2 By similarity
Metal binding1571Metal cation 2 By similarity
Metal binding1961Metal cation 2 By similarity
Metal binding1981Metal cation 1 By similarity
Binding site211cAMP By similarity
Binding site591cAMP By similarity
Binding site1981cAMP By similarity

Experimental info

Sequence conflict441G → A in CAA27241. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P05675 [UniParc].

Last modified March 1, 2005. Version 2.
Checksum: 1290DCCF13D726E6

FASTA25528,172
        10         20         30         40         50         60 
MVEDFAGDAM TLSIAQITDL HLLVDPQAAL RGCVTTPRAA AVFGNLKQRS PDLLLLSGDL 

        70         80         90        100        110        120 
SEDGSPASYE RLRDWVEELG CPAIAIAGNH DQPERLTEIC GRSPFMGEPV YSIQGWRIIA 

       130        140        150        160        170        180 
LDSYQPKRID GRLRGDQLDW LDQRLGEDSS PTLLMLHHPP VLIGVTKMDA IGLKDGPEFL 

       190        200        210        220        230        240 
EVIAHHQQVR LVLSGHAHQA FIQGRGLTTF LGCPATAMQF DQPELPAGWR SLELEPDGSW 

       250 
RSQIHWVDTD SIHFA 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the promoter region in the rrnA operon from a blue-green alga, Anacystis nidulans 6301."
Kumano M., Tomioka N., Shinozaki K., Sugiura M.
Mol. Gen. Genet. 202:173-178(1986)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.
[2]"Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization."
Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M., Kanehisa M., Omata T., Sugiura M., Sugita M.
Photosyn. Res. 93:55-67(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27144 / PCC 6301 / SAUG 1402/1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03538 Genomic DNA. Translation: CAA27240.1. Frameshift.
X03538 Genomic DNA. Translation: CAA27241.1. Frameshift.
AP008231 Genomic DNA. Translation: BAD79127.1.
PIRS10913.
S10914.
RefSeqYP_171647.1. NC_006576.1.

3D structure databases

ProteinModelPortalP05675.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269084.syc0937_d.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD79127; BAD79127; syc0937_d.
GeneID3198083.
KEGGsyc:syc0937_d.
PATRIC32487662. VBISynElo117686_1092.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238351.
KOK03651.
OMAWQIIMLD.
OrthoDBEOG6QG8GQ.

Enzyme and pathway databases

BioCycSELO269084:GCDQ-960-MONOMER.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF00149. Metallophos. 1 hit.
[Graphical view]
SUPFAMSSF56300. SSF56300. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCPDA_SYNP6
AccessionPrimary (citable) accession number: P05675
Secondary accession number(s): P05677, Q5N3J3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: March 1, 2005
Last modified: June 11, 2014
This is version 78 of the entry and version 2 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