CATH Classification
Level | CATH Code | Description |
---|---|---|
1 | Mainly Alpha | |
1.10 | Orthogonal Bundle | |
1.10.10 | Arc Repressor Mutant, subunit A | |
1.10.10.1500 | JmjC domain-containing ribosomal oxygenase (ROX), dimer domain |
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)
Q9H6W3 |
RIOX1_HUMAN
Homo sapiens
Ribosomal oxygenase 1
|
PDB Structure
PDB | 4CCK |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Nature
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