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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
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MetaCyc Enzyme: cAMP phosphodiesterase

Gene: cpdA Accession Numbers: G7579 (MetaCyc), b3032, ECK3023

Synonyms: icc

Species: Escherichia coli K-12 substr. MG1655

Summary:
cAMP phosphodiesterase hydrolyzes the important regulatory molecule cAMP and may thus influence the level of transcription of genes regulated by cAMP-CRP [Imamura96]. However, its rather low affinity for cAMP compared to the dissociation constant of cAMP from CRP suggests that the enzyme does not have a major impact on cAMP concentration in E. coli [Hantke11].

Usage of the unusual translation start codon UUG has been confirmed by amino-terminal sequencing of the purified protein and may be involved in translational regulation of CpdA expression [Imamura96]. CpdA belongs to a family of phosphodiesterases resembling purple acid phosphatases and other dimetallophosphoesterases [Richter02].

Expression of CpdA appears to be itself catabolite-repressed [Aboud71]. A cpdA mutant appears to have slightly increased intracellular levels of cAMP [Imamura96]. Overexpression of cpdA leads to increased resistance to hypochlorous acid stress due to derepression of rpoS [Barth09].

CpdA: "cyclic AMP phosphodiesterase" [Imamura96]

Locations: cytosol

Map Position: [3,174,028 <- 3,174,855]

Molecular Weight of Polypeptide: 30.938 kD (from nucleotide sequence), 30.0 kD (experimental) [Nielsen73 ]

Unification Links: ASAP:ABE-0009957 , EchoBASE:EB2104 , EcoGene:EG12187 , EcoliWiki:b3032 , ModBase:P0AEW4 , OU-Microarray:b3032 , PortEco:cpdA , PR:PRO_000022988 , Pride:P0AEW4 , Protein Model Portal:P0AEW4 , RefSeq:NP_417504 , RegulonDB:G7579 , SMR:P0AEW4 , String:511145.b3032 , UniProt:P0AEW4

Relationship Links: InterPro:IN-FAMILY:IPR004843 , InterPro:IN-FAMILY:IPR013622 , InterPro:IN-FAMILY:IPR026575 , Pfam:IN-FAMILY:PF00149 , ProDom:IN-FAMILY:PD587589

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0008152 - metabolic process Inferred by computational analysis Inferred from experiment [Imamura96, UniProtGOA11a, GOA06, GOA01, GOA01a]
Molecular Function: GO:0004115 - 3',5'-cyclic-AMP phosphodiesterase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, Imamura96]
GO:0008198 - ferrous iron binding Inferred from experiment [Nielsen73]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a, GOA06]
GO:0004114 - 3',5'-cyclic-nucleotide phosphodiesterase activity Inferred by computational analysis [GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a, GOA06]
Cellular Component: GO:0005737 - cytoplasm
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: regulation type of regulation posttranscriptional proteases, cleavage of compounds

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: cAMP phosphodiesterase

Synonyms: cyclic AMP phosphodiesterase, cyclic 3',5'-adenosine monophosphate phosphodiesterase

EC Number: 3.1.4.53

cyclic-AMP + H2O <=> AMP + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
cGMP is not a substrate [Nielsen73].

Cofactors or Prosthetic Groups: Fe2+ [Imamura96, Nielsen73]

Inhibitors (Unknown Mechanism): phosphate [Amin95]

Kinetic Parameters:

Substrate
Km (μM)
Citations
cyclic-AMP
500.0
[Imamura96]

pH(opt): 6.8-7 [Nielsen73]


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 22
[UniProt11a]
UniProt: Metal cation 1; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 24
[UniProt11a]
UniProt: Metal cation 1; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 64
[UniProt11a]
UniProt: Metal cation 1; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 94
[UniProt11a]
UniProt: Metal cation 2; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 94 -> 95
[UniProt11a]
UniProt: cAMP; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 164
[UniProt11a]
UniProt: Metal cation 2; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 203
[UniProt11a]
UniProt: Metal cation 2; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 205
[UniProt11a]
UniProt: Metal cation 1; Non-Experimental Qualifier: by similarity.

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


References

Aboud71: Aboud M, Burger M (1971). "Cyclic 3';5' adenosine monophosphate-phosphodiesterase and the release of catabolite repression of beta-galactosidase by exogenous cyclic 3';5' adenosine monophosphate in Escherichia coli." Biochem Biophys Res Commun 43(1);174-82. PMID: 4325494

Amin95: Amin N, Peterkofsky A (1995). "A dual mechanism for regulating cAMP levels in Escherichia coli." J Biol Chem 270(20);11803-5. PMID: 7744829

Barth09: Barth E, Gora KV, Gebendorfer KM, Settele F, Jakob U, Winter J (2009). "Interplay of cellular cAMP levels, {sigma}S activity and oxidative stress resistance in Escherichia coli." Microbiology 155(Pt 5);1680-9. PMID: 19372151

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Hantke11: Hantke K, Winkler K, Schultz JE (2011). "Escherichia coli exports cyclic AMP via TolC." J Bacteriol 193(5);1086-9. PMID: 21183666

Imamura96: Imamura R, Yamanaka K, Ogura T, Hiraga S, Fujita N, Ishihama A, Niki H (1996). "Identification of the cpdA gene encoding cyclic 3',5'-adenosine monophosphate phosphodiesterase in Escherichia coli." J Biol Chem 1996;271(41);25423-9. PMID: 8810311

Nielsen73: Nielsen LD, Monard D, Rickenberg HV (1973). "Cyclic 3',5'-adenosine monophosphate phosphodiesterase of Escherichia coli." J Bacteriol 116(2);857-66. PMID: 4355491

Richter02: Richter W (2002). "3',5' Cyclic nucleotide phosphodiesterases class III: members, structure, and catalytic mechanism." Proteins 46(3);278-86. PMID: 11835503

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, biocyc14.