ID   2.7.11.12
DE   cGMP-dependent protein kinase.
AN   3':5'-cyclic GMP-dependent protein kinase.
AN   cGMP-dependent protein kinase Ibeta.
AN   guanosine 3':5'-cyclic monophosphate-dependent protein kinase.
AN   PKG.
AN   PKG 1alpha.
AN   PKG 1beta.
AN   PKG II.
CA   (1) ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein].
CA   (2) ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-
CA   [protein].
CC   -!- cGMP is required to activate this enzyme.
CC   -!- The enzyme occurs as a dimer in higher eukaryotes.
CC   -!- The C-terminal region of each polypeptide chain contains the
CC       catalytic domain that includes the ATP and protein substrate binding
CC       sites.
CC   -!- This domain catalyzes the phosphorylation by ATP to specific serine
CC       or threonine residues in protein substrates.
CC   -!- The enzyme also has two allosteric cGMP-binding sites (sites A and
CC       B).
CC   -!- Binding of cGMP causes a conformational change that is associated
CC       with activation of the kinase.
CC   -!- Formerly EC 2.7.1.37.
DR   A8X6H1, EGL4_CAEBR ;  O76360, EGL4_CAEEL ;  P00516, KGP1_BOVIN ;
DR   Q03042, KGP1_DROME ;  Q13976, KGP1_HUMAN ;  P0C605, KGP1_MOUSE ;
DR   O77676, KGP1_RABIT ;  Q03043, KGP24_DROME;  P32023, KGP25_DROME;
DR   Q13237, KGP2_HUMAN ;  Q61410, KGP2_MOUSE ;  Q64595, KGP2_RAT   ;
DR   Q8MMZ8, KGP_EIMTE  ;  A0A509AKL0, KGP_PLABA  ;  Q8I719, KGP_PLAF7  ;
DR   W7JX98, KGP_PLAFO  ;  A5K0N4, KGP_PLAVS  ;  Q8MMZ7, KGP_TOXGO  ;
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