CATH Classification

Domain Context

CATH Clusters

Superfamily Transferase(Phosphotransferase) domain 1
Functional Family Non-specific serine/threonine protein kinase

Enzyme Information

2.7.11.1
Non-specific serine/threonine protein kinase.
based on mapping to UniProt P54646
ATP + a protein = ADP + a phosphoprotein.
-!- This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date. -!- Formerly EC 2.7.1.37 and EC 2.7.1.70.
2.7.11.31
[Hydroxymethylglutaryl-CoA reductase (NADPH)] kinase.
based on mapping to UniProt P54646
ATP + [hydroxymethylglutaryl-CoA reductase (NADPH)] = ADP + [hydroxymethylglutaryl-CoA reductase (NADPH)] phosphate.
-!- Activated by AMP. -!- EC 1.1.1.34 is inactivated by the phosphorylation of the enzyme protein. -!- Histones can also act as acceptors. -!- Can also phosphorylate EC 6.4.1.2 and EC 3.1.1.79. -!- Thr-172 within the catalytic subunit (alpha-subunit) is the major site phosphorylated by the AMP-activated protein kinase kinase. -!- GTP can act instead of ATP. -!- Formerly EC 2.7.1.109.
2.7.11.27
[Acetyl-CoA carboxylase] kinase.
based on mapping to UniProt P54646
ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate.
-!- Phosphorylates and inactivates EC 6.4.1.2, which can be dephosphorylated and reactivated by EC 3.1.3.17. -!- More active toward the dimeric form of acetyl-CoA carboxylase than the polymeric form. -!- Phosphorylates serine residues. -!- Formerly EC 2.7.1.111 and EC 2.7.1.128.

UniProtKB Entries (1)

P54619
AAKG1_HUMAN
Homo sapiens
5'-AMP-activated protein kinase subunit gamma-1

PDB Structure

PDB 4CFF
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structural Basis of Ampk Regulation by Small Molecule Activators.
Xiao, B., Sanders, M.J., Carmena, D., Bright, N.J., Haire, L.F., Underwood, E., Patel, B.R., Heath, R.B., Walker, P.A., Hallen, S., Giordanetto, F., Martin, S.R., Carling, D., Gamblin, S.J.
Nat.Commun.