CATH Classification

Domain Context

CATH Clusters

Superfamily JmjC domain-containing ribosomal oxygenase (ROX), dimer domain
Functional Family ribosomal oxygenase 1 isoform X1

Enzyme Information

1.14.11.-
With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors.
based on mapping to UniProt Q9H6W3
1.14.11.27
[Histone H3]-dimetyl-L-lysine-36 demethylase.
based on mapping to UniProt Q9H6W3
[Protein]-N(6),N(6)-dimethyl-L-lysine + 2 2-oxoglutarate + 2 O(2) = [protein]-L-lysine + 2 succinate + 2 formaldehyde + 2 CO(2).
-!- Of the seven potential methylation sites in histones H3 (K4, K9, K27, K36, K79) and H4 (K20, R3) from HeLa cells, the enzyme is specific for Lys-36. -!- Lysine residues exist in three methylation states (mono-, di- and trimethylated). -!- The enzyme preferentially demethylates the dimethyl form of Lys-36 (K36me2), which is its natural substrate, to form the monomethyl and unmethylated forms of Lys-36. -!- It can also demethylate the monomethyl- but not the trimethyl form of Lys-36.

UniProtKB Entries (1)

P62917
RL8_HUMAN
Homo sapiens
60S ribosomal protein L8

PDB Structure

PDB 4CCM
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Chowdhury, R., Sekirnik, R., Brissett, N.C., Krojer, T., Ho, C.H., Ng, S.S., Clifton, I.J., Ge, W., Kershaw, N.J., Fox, G.C., Muniz, J.R.C., Vollmar, M., Phillips, C., Pilka, E.S., Kavanagh, K.L., von Delft, F., Oppermann, U., McDonough, M.A., Doherty, A.J., Schofield, C.J.
Nature