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Q8YLG0 (CPDA_NOSS1) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 63. 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:alr5338
OrganismNostoc sp. (strain PCC 7120 / UTEX 2576) [Complete proteome] [HAMAP]
Taxonomic identifier103690 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaNostocalesNostocaceaeNostoc

Protein attributes

Sequence length266 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Can also hydrolyze cGMP. Ref.2

Catalytic activity

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate. Ref.2

Cofactor

Binds 2 metal cations per subunit Probable. Ref.2

Enzyme regulation

Activated by iron and manganese. Ref.2

Sequence similarities

Belongs to the cAMP phosphodiesterase class-III family.

Biophysicochemical properties

Kinetic parameters:

KM=45 µM for cAMP Ref.2

Vmax=4.9 µmol/min/mg enzyme with cAMP as substrate

Vmax=4.4 µmol/min/mg enzyme with cGMP as substrate

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 – 2662663',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000413371

Regions

Nucleotide binding86 – 872cAMP By similarity

Sites

Metal binding141Metal cation 1 By similarity
Metal binding161Metal cation 1 By similarity
Metal binding561Metal cation 1 By similarity
Metal binding561Metal cation 2 By similarity
Metal binding861Metal cation 2 By similarity
Metal binding1551Metal cation 2 By similarity
Metal binding1941Metal cation 2 By similarity
Metal binding1961Metal cation 1 By similarity
Binding site161cAMP By similarity
Binding site561cAMP By similarity
Binding site1961cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8YLG0 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 46B3475509226736

FASTA26630,432
        10         20         30         40         50         60 
MNEKLPISIA QITDIHLLAS ESQRLQGIST TESFLAVMKR LEELRPELDL LLMTGDLSDD 

        70         80         90        100        110        120 
GTPESYENLQ HYLNSLQIAT YWLPGNHDCA IAMDKILNLG MVSRRKSFQR GNWNFILLNS 

       130        140        150        160        170        180 
SVTDCVYGYL SATTLDWLDS ELKMLPNNPT LIALHHPPLS VNSAWIDRSC LQNSQELFAV 

       190        200        210        220        230        240 
IDRYPQVKLV LFGHIHQEFR RQRHNVHYLG SPSTCYQFQS QSTTFAINQE LPGFRLLKLY 

       250        260 
ADGTWTTKIE RVPYSLPIEP TVTVSY 

« Hide

References

« Hide 'large scale' references
[1]"Complete genomic sequence of the filamentous nitrogen-fixing cyanobacterium Anabaena sp. strain PCC 7120."
Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A., Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takazawa M., Yamada M., Yasuda M., Tabata S.
DNA Res. 8:205-213(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PCC 7120 / UTEX 2576.
[2]"Biochemical properties of a cAMP phosphodiesterase in the cyanobacterium Anabaena sp. strain PCC 7120."
Fujisawa T., Ohmori M.
Microbes Environ. 20:92-96(2005)
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: PCC 7120 / UTEX 2576.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000019 Genomic DNA. Translation: BAB77037.1.
PIRAB2473.
RefSeqNP_489378.1. NC_003272.1.

3D structure databases

ProteinModelPortalQ8YLG0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING103690.alr5338.

Protocols and materials databases

DNASU1108942.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB77037; BAB77037; BAB77037.
GeneID1108942.
KEGGana:alr5338.
PATRIC22781413. VBINosSp37423_6142.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1409.
HOGENOMHOG000238351.
KOK03651.
OMATERTLLW.
OrthoDBEOG6QG8GQ.

Family and domain databases

Gene3D3.60.21.10. 1 hit.
HAMAPMF_00905. cAMP_phophodiest_CpdA.
InterProIPR013622. Calcineurin-like_phos_C.
IPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamPF00149. Metallophos. 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_NOSS1
AccessionPrimary (citable) accession number: Q8YLG0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 63 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