×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

CATH Classification

Domain Context

CATH Clusters

Superfamily Aldolase class I
Functional Family Dual-specificity RNA methyltransferase RlmN

Enzyme Information

2.1.1.192
23S rRNA (adenine(2503)-C(2))-methyltransferase.
based on mapping to UniProt P36979
(1) 2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(2503) in 23S rRNA + 2 oxidized [2Fe- 2S] ferredoxin. (2) 2 S-adenosyl-L-methionine + adenine(37) in tRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine(37) in tRNA + 2 oxidized [2Fe-2S] ferredoxin.
-!- This enzyme is a member of the 'AdoMet radical' (radical SAM) family. -!- S-adenosyl-L-methionine acts as both a radical generator and as the source of the appended methyl group. -!- RlmN first transfers an CH(2) group to a conserved cysteine (Cys(355) in Escherichia coli), the generated radical from a second S-adenosyl- L-methionine then attacks the methyl group, exctracting a hydrogen. -!- The formed radical forms a covalent intermediate with the adenine group of the tRNA. -!- RlmN is an endogenous enzyme used by the cell to refine functions of the ribosome in protein synthesis. -!- The enzyme methylates adenosine by a radical mechanism with CH(2) from the S-adenosyl-L-methionine and retention of the hydrogen at C-2 of adenosine(2503) of 23S rRNA. -!- It will also methylate 8-methyladenosine(2503) of 23S rRNA (cf. EC 2.1.1.224).

UniProtKB Entries (1)

P36979
RLMN_ECOLI
Escherichia coli K-12
Dual-specificity RNA methyltransferase RlmN

PDB Structure

PDB 5HR7
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystallographic capture of a radical S-adenosylmethionine enzyme in the act of modifying tRNA.
Schwalm, E.L., Grove, T.L., Booker, S.J., Boal, A.K.
Science
CATH-Gene3D is a Global Biodata Core Resource Learn more...