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ENZYME entry: EC 3.1.4.52

Accepted Name
Cyclic-guanylate-specific phosphodiesterase.
Alternative Name(s)
C-di-GMP-specific phosphodiesterase.
PDEA1.
Phosphodiesterase A1.
Reaction catalysed
Cyclic di-3',5'-guanylate + H(2)O <=> 5'-phosphoguanylyl(3'->5')guanosine
Cofactor(s)
Heme; Mg(2+); Mn(2+).
Comment(s)
  • Inhibited by Ca(2+) and Zn(2+).
  • Linearizes cyclic di-3',5'-guanylate, the product of EC 2.7.7.65 and an allosteric activator of EC 2.4.1.12 rendering it inactive.
  • It is the balance between these two enzymes that determines the cellular level of cyclic di-3',5'-guanylate.
Cross-references
BRENDA3.1.4.52
EC2PDB3.1.4.52
ExplorEnz3.1.4.52
PRIAM enzyme-specific profiles3.1.4.52
KEGG Ligand Database for Enzyme Nomenclature3.1.4.52
IUBMB Enzyme Nomenclature3.1.4.52
IntEnz3.1.4.52
MEDLINEFind literature relating to 3.1.4.52
MetaCyc3.1.4.52
UniProtKB/Swiss-Prot
Q9KVK6, CDGJ_VIBCH;  Q9KVL2, CDPA_VIBCH;  P76129, DOSP_ECOLI;  
O51338, PDEA_BORBU;  P23842, PDEA_ECOLI;  P77473, PDEB_ECOLI;  
Q8EJM6, PDEB_SHEON;  P32701, PDEC_ECOLI;  P76261, PDED_ECOLI;  
P77172, PDEF_ECOLI;  P75995, PDEG_ECOLI;  P37646, PDEH_ECOLI;  
P75800, PDEI_ECOLI;  P37649, PDEK_ECOLI;  P21514, PDEL_ECOLI;  
P76446, PDEN_ECOLI;  P77334, PDER_ECOLI;  

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All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.4.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.1.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-