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CATH Superfamily 3.20.20.70

Aldolase class I

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Aldolase class I
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 14: Probable dual-specificity RNA methyltransferase Rl...

There are 2 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
23S rRNA (adenine(2503)-C(2))-methyltransferase. [EC: 2.1.1.192]
(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).
 4605 A0A045JFF7 A0A045JFF7 A0A045JFF7 A0A045JFF7 A0A045JFF7 A0A045JFF7 A0A045JFF7 A0A045JFF7 A0A045JFF7 A0A045JFF7
(4595 more...)
23S rRNA (adenine(2503)-C(8))-methyltransferase. [EC: 2.1.1.224]
2 S-adenosyl-L-methionine + adenine(2503) in 23S rRNA + 2 reduced [2Fe- 2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine(2503) in 23S rRNA + 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.
  • Cfr is an plasmid-acquired methyltransferase that protects cells from the action of antibiotics.
  • The enzyme methylates adenosine at position 2503 of 23S rRNA by a radical mechanism, transferring a CH(2) group from S-adenosyl-L- methionine while retaining the hydrogen at the C-8 position of the adenine.
  • Cfr first transfers an CH(2) group to a conserved cysteine (Cys(338) in Staphylococcus aureus), 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.
  • The enzyme will also methylate 2-methyladenine produced by the action of EC 2.1.1.192.
 12 A0A0M0A5N7 A0A0M0A5N7 A0A0M0A5N7 A5I5U3 A5I5U3 A5I5U3 A7FX96 A7FX96 A7FX96 A7GH77
(2 more...)
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