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Q93GX3 (CPDA_STRAW) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 66. 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:SAV_1247
OrganismStreptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680) [Complete proteome] [HAMAP]
Taxonomic identifier227882 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length257 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 – 2572573',5'-cyclic adenosine monophosphate phosphodiesterase CpdA HAMAP-Rule MF_00905
PRO_0000413379

Regions

Nucleotide binding74 – 752cAMP By similarity

Sites

Metal binding61Metal cation 1 By similarity
Metal binding81Metal cation 1 By similarity
Metal binding441Metal cation 1 By similarity
Metal binding441Metal cation 2 By similarity
Metal binding741Metal cation 2 By similarity
Metal binding1481Metal cation 2 By similarity
Metal binding1871Metal cation 2 By similarity
Metal binding1891Metal cation 1 By similarity
Binding site81cAMP By similarity
Binding site441cAMP By similarity
Binding site1891cAMP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q93GX3 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: C308521452EDFA66

FASTA25727,129
        10         20         30         40         50         60 
MAHLSDPHLT TGLLAVDRVA AFSRALRCVL ALDPRPACVV VTGDLVDRGE AEEYEVLREV 

        70         80         90        100        110        120 
IARFPLPVHL VPGNHDDPGT LLEAFGGGPH TGGARAFPYA VEYPNATVVV LSSTVPGAPS 

       130        140        150        160        170        180 
GRLGDEQLDR LEELLSRRPE VPAFVCLHHP PVDIGIPYLD GMNLADADAF GEVIGRHPQV 

       190        200        210        220        230        240 
VRVLAGHVHR AVTGEFAGST MVTAPSTYLQ SNLNLRVGGP VGYVDEPTAF LLHHLTGTGC 

       250 
VTHTAQVSHA GGLIGGY 

« Hide

References

[1]"Genome sequence of an industrial microorganism Streptomyces avermitilis: deducing the ability of producing secondary metabolites."
Omura S., Ikeda H., Ishikawa J., Hanamoto A., Takahashi C., Shinose M., Takahashi Y., Horikawa H., Nakazawa H., Osonoe T., Kikuchi H., Shiba T., Sakaki Y., Hattori M.
Proc. Natl. Acad. Sci. U.S.A. 98:12215-12220(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.
[2]"Complete genome sequence and comparative analysis of the industrial microorganism Streptomyces avermitilis."
Ikeda H., Ishikawa J., Hanamoto A., Shinose M., Kikuchi H., Shiba T., Sakaki Y., Hattori M., Omura S.
Nat. Biotechnol. 21:526-531(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 31267 / DSM 46492 / JCM 5070 / NCIMB 12804 / NRRL 8165 / MA-4680.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB070957 Genomic DNA. Translation: BAB69418.1.
BA000030 Genomic DNA. Translation: BAC68957.1.
RefSeqNP_822422.1. NC_003155.4.

3D structure databases

ProteinModelPortalQ93GX3.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING227882.SAV_1247.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC68957; BAC68957; SAV_1247.
GeneID1210161.
KEGGsma:SAV_1247.
PATRIC23715829. VBIStrAve112782_1332.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000238352.
OMATERTLLW.
OrthoDBEOG6QG8GQ.

Enzyme and pathway databases

BioCycSAVE227882:GJU1-1254-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_STRAW
AccessionPrimary (citable) accession number: Q93GX3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 66 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