Enzyme

Download
EC Tree
     1. Oxidoreductases
        1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
            1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
ID:1.14.11.27
Description:[Histone H3]-dimetyl-L-lysine-36 demethylase.
Alternative Name: JmjC domain-containing histone demethylase 1A.
JHDM1A.
Histone-lysine (H3-K36) demethylase.
Histone demethylase.
H3-K36-specific demethylase.
Cath: 1.10.10.1500; 1.10.10.1520; 3.20.20.60; 3.30.40.10; 1.20.58.1360; 1.20.58.2210; 2.60.120.650;

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.14.11.27
BRENDA Enzyme Link: BRENDA 1.14.11.27
KEGG Enzyme Link: KEGG1.14.11.27
BioCyc Enzyme Link: BioCyc 1.14.11.27
ExPASy Enzyme Link: ExPASy1.14.11.27
EC2PDB Enzyme Link: EC2PDB 1.14.11.27
ExplorEnz Enzyme Link: ExplorEnz 1.14.11.27
PRIAM enzyme-specific profiles Link: PRIAM 1.14.11.27
IntEnz Enzyme Link: IntEnz 1.14.11.27
MEDLINE Enzyme Link: MEDLINE 1.14.11.27
MSA:

1.14.11.27;

Phylogenetic Tree:

1.14.11.27;

Uniprot:
M-CSA:
RHEA:42032 2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysine(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysine(36)-[histone H3] + 2 succinate
RULE(radius=1) [*:1]-[N;H0;+0:2](-[CH3;+0:3])-[CH3;+0:4].[*:5]=[C;H0;+0:6](-[OH;+0:7])-[C;H0;+0:8](=[*:9])-[*:10].[*:11]=[C;H0;+0:12](-[OH;+0:13])-[C;H0;+0:14](=[*:15])-[*:16].[O;H0;+0:17]=[O;H0;+0:18].[O;H0;+0:19]=[O;H0;+0:20]>>[*:1]-[NH2;+0:2].[*:9]=[C;H0;+0:8](-[*:10])-[OH;+0:17].[*:15]=[C;H0;+0:14](-[*:16])-[OH;+0:18].[*:5]=[C;H0;+0:6]=[O;H0;+0:7].[*:11]=[C;H0;+0:12]=[O;H0;+0:13].[CH2;+0:3]=[O;H0;+0:19].[CH2;+0:4]=[O;H0;+0:20]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Histone demethylation by a family of JmjC domain-containing proteins.Tsukada Y, Fang J, Erdjument-Bromage H, Warren ME, Borchers CH, Tempst P, Zhang Y2006 Feb 1616362057