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Protein

3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA

Gene

cpdA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Hydrolyzes cAMP to 5'-AMP. Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. Specific for cAMP.UniRule annotation1 Publication

Catalytic activityi

Adenosine 3',5'-cyclic phosphate + H2O = adenosine 5'-phosphate.UniRule annotation1 Publication

Cofactori

a metal cationUniRule annotationNote: Binds 2 metal cations per subunit.UniRule annotation

Enzyme regulationi

Activated by iron.1 Publication

Kineticsi

  1. KM=0.5 mM for cAMP1 Publication

Vmax=2.0 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi22 – 221Metal cation 1UniRule annotation
Metal bindingi24 – 241Metal cation 1UniRule annotation
Binding sitei24 – 241cAMPUniRule annotation
Metal bindingi64 – 641Metal cation 1UniRule annotation
Metal bindingi64 – 641Metal cation 2UniRule annotation
Binding sitei64 – 641cAMPUniRule annotation
Metal bindingi94 – 941Metal cation 2UniRule annotation
Metal bindingi164 – 1641Metal cation 2UniRule annotation
Metal bindingi203 – 2031Metal cation 2UniRule annotation
Metal bindingi205 – 2051Metal cation 1UniRule annotation
Binding sitei205 – 2051cAMPUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi94 – 952cAMPUniRule annotation

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: EcoCyc
  2. ferrous iron binding Source: EcoCyc
  3. nucleotide binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. metabolic process Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7579-MONOMER.
ECOL316407:JW3000-MONOMER.
MetaCyc:G7579-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdAUniRule annotation (EC:3.1.4.17UniRule annotation)
Short name:
3',5'-cyclic AMP phosphodiesteraseUniRule annotation
Short name:
cAMP phosphodiesteraseUniRule annotation
Gene namesi
Name:cpdAUniRule annotation
Synonyms:icc
Ordered Locus Names:b3032, JW3000
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12187. cpdA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 2752753',5'-cyclic adenosine monophosphate phosphodiesterase CpdAPRO_0000084146Add
BLAST

Proteomic databases

PaxDbiP0AEW4.
PRIDEiP0AEW4.

Expressioni

Gene expression databases

GenevestigatoriP0AEW4.

Interactioni

Protein-protein interaction databases

IntActiP0AEW4. 10 interactions.
STRINGi511145.b3032.

Structurei

3D structure databases

ProteinModelPortaliP0AEW4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cAMP phosphodiesterase class-III family.UniRule annotation

Phylogenomic databases

eggNOGiCOG1409.
HOGENOMiHOG000238351.
InParanoidiP0AEW4.
KOiK03651.
OMAiSEYQLEW.
OrthoDBiEOG6QG8GQ.
PhylomeDBiP0AEW4.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
HAMAPiMF_00905. cAMP_phophodiest_CpdA.
InterProiIPR013622. Calcineurin-like_phos_C.
IPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
ProDomiPD587589. Calcineurin-like_phos_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56300. SSF56300. 1 hit.

Sequencei

Sequence statusi: Complete.

P0AEW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MESLLTLPLA GEARVRILQI TDTHLFAQKH EALLGVNTWE SYQAVLEAIR
60 70 80 90 100
PHQHEFDLIV ATGDLAQDQS SAAYQHFAEG IASFRAPCVW LPGNHDFQPA
110 120 130 140 150
MYSALQDAGI SPAKRVFIGE QWQILLLDSQ VFGVPHGELS EFQLEWLERK
160 170 180 190 200
LADAPERHTL LLLHHHPLPA GCSWLDQHSL RNAGELDTVL AKFPHVKYLL
210 220 230 240 250
CGHIHQELDL DWNGRRLLAT PSTCVQFKPH CSNFTLDTIA PGWRTLELHA
260 270
DGTLTTEVHR LADTRFQPDT ASEGY
Length:275
Mass (Da):30,938
Last modified:December 20, 2005 - v1
Checksum:i97696478536CFBF1
GO

Sequence cautioni

The sequence AAA69200.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16557 Genomic DNA. Translation: BAA03989.1.
U28377 Genomic DNA. Translation: AAA69200.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76068.1.
AP009048 Genomic DNA. Translation: BAE77088.1.
PIRiF65090.
RefSeqiNP_417504.1. NC_000913.3.
YP_491224.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76068; AAC76068; b3032.
BAE77088; BAE77088; BAE77088.
GeneIDi12933401.
947515.
KEGGiecj:Y75_p2958.
eco:b3032.
PATRICi32121474. VBIEscCol129921_3124.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D16557 Genomic DNA. Translation: BAA03989.1.
U28377 Genomic DNA. Translation: AAA69200.1. Different initiation.
U00096 Genomic DNA. Translation: AAC76068.1.
AP009048 Genomic DNA. Translation: BAE77088.1.
PIRiF65090.
RefSeqiNP_417504.1. NC_000913.3.
YP_491224.1. NC_007779.1.

3D structure databases

ProteinModelPortaliP0AEW4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP0AEW4. 10 interactions.
STRINGi511145.b3032.

Proteomic databases

PaxDbiP0AEW4.
PRIDEiP0AEW4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76068; AAC76068; b3032.
BAE77088; BAE77088; BAE77088.
GeneIDi12933401.
947515.
KEGGiecj:Y75_p2958.
eco:b3032.
PATRICi32121474. VBIEscCol129921_3124.

Organism-specific databases

EchoBASEiEB2104.
EcoGeneiEG12187. cpdA.

Phylogenomic databases

eggNOGiCOG1409.
HOGENOMiHOG000238351.
InParanoidiP0AEW4.
KOiK03651.
OMAiSEYQLEW.
OrthoDBiEOG6QG8GQ.
PhylomeDBiP0AEW4.

Enzyme and pathway databases

BioCyciEcoCyc:G7579-MONOMER.
ECOL316407:JW3000-MONOMER.
MetaCyc:G7579-MONOMER.

Miscellaneous databases

PROiP0AEW4.

Gene expression databases

GenevestigatoriP0AEW4.

Family and domain databases

Gene3Di3.60.21.10. 1 hit.
HAMAPiMF_00905. cAMP_phophodiest_CpdA.
InterProiIPR013622. Calcineurin-like_phos_C.
IPR004843. Calcineurin-like_PHP_apaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR029052. Metallo-depent_PP-like.
[Graphical view]
PfamiPF00149. Metallophos. 1 hit.
[Graphical view]
ProDomiPD587589. Calcineurin-like_phos_C. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SUPFAMiSSF56300. SSF56300. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the cpdA gene encoding cyclic 3',5'-adenosine monophosphate phosphodiesterase in Escherichia coli."
    Imamura R., Yamanaka K., Ogura T., Hiraga S., Fujita N., Ishihama A., Niki H.
    J. Biol. Chem. 271:25423-25429(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18, GENE NAME, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: K12.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "3',5' Cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism."
    Richter W.
    Proteins 46:278-286(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENE FAMILY, NOMENCLATURE, MODELING OF METAL-BINDING SITES.

Entry informationi

Entry nameiCPDA_ECOLI
AccessioniPrimary (citable) accession number: P0AEW4
Secondary accession number(s): P36650, Q2M9G8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: January 7, 2015
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.