EC number:2.1.1.192
| ID: | 2.1.1.192 |
|---|---|
| Description: | 23S rRNA (adenine(2503)-C(2))-methyltransferase. |
| Cath: | 1.10.150.530; 3.20.20.70; 4.10.180.60; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 2.1.1.192 |
| BRENDA Enzyme Link: | BRENDA 2.1.1.192 |
| KEGG Enzyme Link: | KEGG2.1.1.192 |
| BioCyc Enzyme Link: | BioCyc 2.1.1.192 |
| ExPASy Enzyme Link: | ExPASy2.1.1.192 |
| EC2PDB Enzyme Link: | EC2PDB 2.1.1.192 |
| ExplorEnz Enzyme Link: | ExplorEnz 2.1.1.192 |
| PRIAM enzyme-specific profiles Link: | PRIAM 2.1.1.192 |
| IntEnz Enzyme Link: | IntEnz 2.1.1.192 |
| MEDLINE Enzyme Link: | MEDLINE 2.1.1.192 |
EC number:2.1.1.192
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:43332 | adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[Fe;H0;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[S+;H0:8](-[*:9])-[CH2;+0:10]-[*:11].[*:12]-[S+;H0:13](-[*:14])-[CH3;+0:15].[*:16]:[cH;+0:17]:[*:18]>>[*:11]-[CH3;+0:10].[*:1]-[Fe+;H0:2]-[*:3].[*:4]-[Fe+;H0:5]-[*:6].[*:12]-[S;H0;+0:13]-[*:14].[*:7]-[S;H0;+0:8]-[*:9].[*:16]:[c;H0;+0:17](:[*:18])-[CH3;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN. | Silakov A, Grove TL, Radle MI, Bauerle MR, Green MT, Rosenzweig AC, Boal AK, Booker SJ | 2014 Jun 11 | 24806349 |
| Covalent intermediate in the catalytic mechanism of the radical S-adenosyl-L-methionine methyl synthase RlmN trapped by mutagenesis. | McCusker KP, Medzihradszky KF, Shiver AL, Nichols RJ, Yan F, Maltby DA, Gross CA, Fujimori DG | 2012 Oct 31 | 23088750 |
| The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy. | Benítez-Páez A, Villarroya M, Armengod ME | 2012 Oct | 22891362 |
| Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation. | Grove TL, Radle MI, Krebs C, Booker SJ | 2011 Dec 14 | 21916495 |
| Structural basis for methyl transfer by a radical SAM enzyme. | Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC | 2011 May 27 | 21527678 |
| A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. | Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ | 2011 Apr 29 | 21415317 |
| RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift. | Yan F, Fujimori DG | 2011 Mar 8 | 21368151 |
| RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA. | Yan F, LaMarre JM, Röhrich R, Wiesner J, Jomaa H, Mankin AS, Fujimori DG | 2010 Mar 24 | 20184321 |
| The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA. | Toh SM, Xiong L, Bae T, Mankin AS | 2008 Jan | 18025251 |
| RHEA:42916 | adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine |
| RULE(radius=1) | [*:1]-[Fe;H0;+0:2]-[*:3].[*:4]-[Fe;H0;+0:5]-[*:6].[*:7]-[S+;H0:8](-[*:9])-[CH2;+0:10]-[*:11].[*:12]-[S+;H0:13](-[*:14])-[CH3;+0:15].[*:16]:[cH;+0:17]:[*:18]>>[*:11]-[CH3;+0:10].[*:1]-[Fe+;H0:2]-[*:3].[*:4]-[Fe+;H0:5]-[*:6].[*:12]-[S;H0;+0:13]-[*:14].[*:7]-[S;H0;+0:8]-[*:9].[*:16]:[c;H0;+0:17](:[*:18])-[CH3;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Characterization of a cross-linked protein-nucleic acid substrate radical in the reaction catalyzed by RlmN. | Silakov A, Grove TL, Radle MI, Bauerle MR, Green MT, Rosenzweig AC, Boal AK, Booker SJ | 2014 Jun 11 | 24806349 |
| Covalent intermediate in the catalytic mechanism of the radical S-adenosyl-L-methionine methyl synthase RlmN trapped by mutagenesis. | McCusker KP, Medzihradszky KF, Shiver AL, Nichols RJ, Yan F, Maltby DA, Gross CA, Fujimori DG | 2012 Oct 31 | 23088750 |
| The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy. | Benítez-Páez A, Villarroya M, Armengod ME | 2012 Oct | 22891362 |
| Cfr and RlmN contain a single [4Fe-4S] cluster, which directs two distinct reactivities for S-adenosylmethionine: methyl transfer by SN2 displacement and radical generation. | Grove TL, Radle MI, Krebs C, Booker SJ | 2011 Dec 14 | 21916495 |
| Structural basis for methyl transfer by a radical SAM enzyme. | Boal AK, Grove TL, McLaughlin MI, Yennawar NH, Booker SJ, Rosenzweig AC | 2011 May 27 | 21527678 |
| A radically different mechanism for S-adenosylmethionine-dependent methyltransferases. | Grove TL, Benner JS, Radle MI, Ahlum JH, Landgraf BJ, Krebs C, Booker SJ | 2011 Apr 29 | 21415317 |
| RNA methylation by radical SAM enzymes RlmN and Cfr proceeds via methylene transfer and hydride shift. | Yan F, Fujimori DG | 2011 Mar 8 | 21368151 |
| RlmN and Cfr are radical SAM enzymes involved in methylation of ribosomal RNA. | Yan F, LaMarre JM, Röhrich R, Wiesner J, Jomaa H, Mankin AS, Fujimori DG | 2010 Mar 24 | 20184321 |
| The methyltransferase YfgB/RlmN is responsible for modification of adenosine 2503 in 23S rRNA. | Toh SM, Xiong L, Bae T, Mankin AS | 2008 Jan | 18025251 |