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: | 1.14.11.47 |
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Description: | [50S ribosomal protein L16]-arginine 3-hydroxylase. |
Cath: | 1.10.10.2510; 2.60.120.650; |
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.UniProtKB Enzyme Link: | UniProtKB 1.14.11.47 |
BRENDA Enzyme Link: | BRENDA 1.14.11.47 |
KEGG Enzyme Link: | KEGG1.14.11.47 |
BioCyc Enzyme Link: | BioCyc 1.14.11.47 |
ExPASy Enzyme Link: | ExPASy1.14.11.47 |
EC2PDB Enzyme Link: | EC2PDB 1.14.11.47 |
ExplorEnz Enzyme Link: | ExplorEnz 1.14.11.47 |
PRIAM enzyme-specific profiles Link: | PRIAM 1.14.11.47 |
IntEnz Enzyme Link: | IntEnz 1.14.11.47 |
MEDLINE Enzyme Link: | MEDLINE 1.14.11.47 |
MSA: | |
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Phylogenetic Tree: | |
Uniprot: | |
M-CSA: |
RHEA:41556 | 2-oxoglutarate + L-arginyl-[ribosomal protein uL16] + O2 = (3R)-3-hydroxy-L-arginyl-[ribosomal protein uL16] + CO2 + succinate |
RULE(radius=1) | [*:1]-[CH2;+0:2]-[*:3].[*:4]=[C;H0;+0:5](-[OH;+0:6])-[C;H0;+0:7](=[*:8])-[*:9].[O;H0;+0:10]=[O;H0;+0:11]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:10].[*:8]=[C;H0;+0:7](-[*:9])-[OH;+0:11].[*:4]=[C;H0;+0:5]=[O;H0;+0:6] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans. | Ge W, Wolf A, Feng T, Ho CH, Sekirnik R, Zayer A, Granatino N, Cockman ME, Loenarz C, Loik ND, Hardy AP, Claridge TDW, Hamed RB, Chowdhury R, Gong L, Robinson CV, Trudgian DC, Jiang M, Mackeen MM, Mccullagh JS, Gordiyenko Y, Thalhammer A, Yamamoto A, Yang M, Liu-Yi P, Zhang Z, Schmidt-Zachmann M, Kessler BM, Ratcliffe PJ, Preston GM, Coleman ML, Schofield CJ | 2012 Dec | 23103944 |
Structure and functional analysis of YcfD, a novel 2-oxoglutarate/Fe²⁺-dependent oxygenase involved in translational regulation in Escherichia coli. | van Staalduinen LM, Novakowski SK, Jia Z | 2014 May 1 | 24530688 |