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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
  1. Vmax=2.0 µmol/min/mg enzyme1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi22Metal cation 1UniRule annotation1
Metal bindingi24Metal cation 1UniRule annotation1
Binding sitei24cAMPUniRule annotation1
Metal bindingi64Metal cation 1UniRule annotation1
Metal bindingi64Metal cation 2UniRule annotation1
Binding sitei64cAMPUniRule annotation1
Metal bindingi94Metal cation 2UniRule annotation1
Metal bindingi164Metal cation 2UniRule annotation1
Metal bindingi203Metal cation 2UniRule annotation1
Metal bindingi205Metal cation 1UniRule annotation1
Binding sitei205cAMPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi94 – 95cAMPUniRule annotation2

GO - Molecular functioni

  • 3',5'-cyclic-AMP phosphodiesterase activity Source: EcoCyc
  • ferrous iron binding Source: EcoCyc
  • nucleotide binding Source: UniProtKB-KW

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandcAMP, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:G7579-MONOMER.
MetaCyc:G7579-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
3',5'-cyclic adenosine monophosphate phosphodiesterase CpdAUniRule annotation (EC:3.1.4.53UniRule 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12187. cpdA.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000841461 – 2753',5'-cyclic adenosine monophosphate phosphodiesterase CpdAAdd BLAST275

Proteomic databases

PaxDbiP0AEW4.
PRIDEiP0AEW4.

Interactioni

Protein-protein interaction databases

BioGridi4262395. 9 interactors.
IntActiP0AEW4. 10 interactors.
STRINGi316385.ECDH10B_3206.

Structurei

3D structure databases

ProteinModelPortaliP0AEW4.
SMRiP0AEW4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG41070EG. Bacteria.
COG1409. LUCA.
HOGENOMiHOG000238351.
InParanoidiP0AEW4.
KOiK03651.
PhylomeDBiP0AEW4.

Family and domain databases

CDDicd07402. MPP_GpdQ. 1 hit.
Gene3Di3.60.21.10. 1 hit.
HAMAPiMF_00905. cAMP_phophodiest_CpdA. 1 hit.
InterProiView protein in InterPro
IPR004843. Calcineurin-like_PHP_ApaH.
IPR026575. cAMP_Pdiest_CpdA.
IPR013622. CpdA_C.
IPR029052. Metallo-depent_PP-like.
PfamiView protein in Pfam
PF00149. Metallophos. 1 hit.
ProDomiView protein in ProDom or Entries sharing at least one domain
PD587589. Calcineurin-like_phos_C. 1 hit.
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 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.
WP_000444747.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76068; AAC76068; b3032.
BAE77088; BAE77088; BAE77088.
GeneIDi947515.
KEGGiecj:JW3000.
eco:b3032.
PATRICifig|1411691.4.peg.3699.

Similar proteinsi

Entry informationi

Entry nameiCPDA_ECOLI
AccessioniPrimary (citable) accession number: P0AEW4
Secondary accession number(s): P36650, Q2M9G8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: August 30, 2017
This is version 90 of the entry and version 1 of the sequence. See 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