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CATH Superfamily 3.20.20.540

Radical SAM ThiC family, central 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:

"
Radical SAM ThiC family, central 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.
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FunFam 1: Phosphomethylpyrimidine synthase

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
Phosphomethylpyrimidine synthase. [EC: 4.1.99.17]
5-amino-1-(5-phospho-D-ribosyl)imidazole + S-adenosyl-L-methionine = 4-amino-2-methyl-5-(phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + formate + CO.
  • Binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule.
  • The first stage of catalysis is reduction of the S-adenosyl-L- methionine to produce L-methionine and a 5'-deoxyadenosin-5'-yl radical that is crucial for the conversion of the substrate.
  • Part of the pathway for thiamine biosynthesis.
 4011 A0A015VA15 A0A015VA15 A0A015VA15 A0A015VA15 A0A015VA15 A0A015VA15 A0A015VA15 A0A015VA15 A0A015VA15 A0A015VA15
(4001 more...)
5-hydroxybenzimidazole synthase. [EC: 4.1.99.23]
5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + S-adenosyl-L-methionine + reduced acceptor = 5-hydroxybenzimidazole + 5'-deoxyadenosine + L-methionine + formate + formate + NH(3) + phosphate + oxidized acceptor.
  • The enzyme, purified from bacteria, is part of the anaerobic pathway for cobalamin biosynthesis.
  • It binds a [4Fe-4S] cluster that is coordinated by 3 cysteines and an exchangeable S-adenosyl-L-methionine molecule.
  • The first stage of catalysis is reduction of the S-adenosyl-L- methionine to produce L-methionine and a 5'-deoxyadenosin-5'-yl radical that is crucial for the conversion of the substrate.
 5 A0A0D5N546 A0A0D5N546 P61425 P61425 Q39YG0
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