View in Gene3D

CATH Superfamily 3.80.30.20

tm_1862 like domain

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:

"
tm_1862 like domain
".

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.
« Back to all FunFams

FunFam 1: tRNA-2-methylthio-N(6)-dimethylallyladenosine synt...

There are 3 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 methylsulfanyl 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.
 27526 A0A023YUJ6 A0A023YUJ6 A0A023YUJ6 A0A023YUJ6 A0A023YUJ6 A0A023YUJ6 A0A023YUJ6 A0A023YUJ6 A0A023YUJ6 A0A023YUJ6
(27516 more...)
TRNA-2-methylthio-N(6)-dimethylallyladenosine synthase. [EC: 2.8.4.3]
N(6)-dimethylallyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylthio- N(6)-dimethylallyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor.
  • This bacterial enzyme binds two [4Fe-4S] clusters as well as the transferred sulfur.
  • The enzyme is a member of the superfamily of S-adenosyl-L-methionine- dependent radical (radical AdoMet) enzymes.
  • The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover.
  • The identity of the electron donor is not known.
 23109 A0A023YTJ6 A0A023YTJ6 A0A023YTJ6 A0A023YTJ6 A0A023YTJ6 A0A023YTJ6 A0A023YTJ6 A0A023YTJ6 A0A023YTJ6 A0A023YTJ6
(23099 more...)
TRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase. [EC: 2.8.4.5]
N(6)-L-threonylcarbamoyladenine(37) in tRNA + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced electron acceptor = 2-methylthio- N(6)-L-threonylcarbamoyladenine(37) in tRNA + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron acceptor.
  • The enzyme, which is a member of the S-adenosyl-L-methionine- dependent radical (radical AdoMet) enzymes superfamily, binds two [4Fe-4S] clusters as well as the transferred sulfur.
  • The sulfur donor is believed to be one of the [4Fe-4S] clusters, which is sacrificed in the process, so that in vitro the reaction is a single turnover.
  • The identity of the electron donor is not known.
 85 A0A085C7R8 A0A085C7R8 A0A085C7R8 A0A085C7R8 A0A085C7R8 A0A085C7R8 A0A085C7R8 A0A085C7R8 A0A085C7R8 A0A2X1X0D4
(75 more...)
CATH-Gene3D is a Global Biodata Core Resource Learn more...