CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.8 | Helicase, Ruva Protein; domain 3 |
|
1.10.8.10 | DNA helicase RuvA subunit, C-terminal domain |
Domain Context
CATH Clusters
| Superfamily | DNA helicase RuvA subunit, C-terminal domain |
| 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)
| P54646 |
AAPK2_HUMAN
Homo sapiens
5'-AMP-activated protein kinase catalytic subunit alpha-2
|
PDB Structure
| PDB | 2LTU |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
Solution Structure of autoinhibitory domain of human AMP-activated protein kinase catalytic subunit
To be Published
|
