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CATH Superfamily 2.40.50.140

Nucleic acid-binding proteins

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Nucleic acid-binding proteins
".

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 68085: Ribosomal protein S12 methylthiotransferase

There are 1 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
[Ribosomal protein S12] (aspartate(89)-C(3))-methylthiotransferase. [EC: 2.8.4.4]
L-aspartate-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine = 3-methylthio-L-aspartate-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine.
  • This bacterial enzyme binds two [4Fe-4S] clusters.
  • A bridge of five sulfur atoms is formed between the free Fe atoms of the two [4Fe-4S] clusters.
  • In the first reaction the enzyme transfers a methyl group from AdoMet to the external sulfur ion of the sulfur bridge.
  • In the second reaction the enzyme catalyzes the reductive fragmentation of a second molecule of AdoMet, yielding a 5'-deoxyadenosine radical, which then attacks the methylated sulfur atom of the polysulfide bridge, resulting in the transfer of a methylthiol group to aspartate(89) (Escherichia coli numbering).
  • The enzyme is a member of the superfamily of S-adenosyl-L-methionine- dependent radical (radical AdoMet) enzymes.
 11 A0A061D069 A0A087F5S0 A0A0F3GGT1 A0A0Q4SCM7 A0A1H2L995 A0A1L7FYE8 A4XT11 F4DM46 U1SRA5 U1ZQS7
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