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CATH Superfamily 3.20.70.20

The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_0). At the point of the last release, this superfamily was: waiting to be named.

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 6: Anaerobic ribonucleoside-triphosphate reductase Nr...

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
Ribonucleoside-triphosphate reductase (formate). [EC: 1.1.98.6]
Ribonucleoside 5'-triphosphate + formate = 2'-deoxyribonucleoside 5'-triphosphate + CO(2) + H(2)O.
  • The enzyme, which is expressed in the bacterium Escherichia coli during anaerobic growth, contains an iron sulfur center.
  • The active form of the enzyme contains an oxygen-sensitive glycyl (1-amino-2-oxoethan-1-yl) radical that is generated by the activating enzyme NrdG via chemistry involving S-adenosylmethionine (SAM) and a [4Fe-4S] cluster.
  • The glycyl radical is involved in generation of a transient thiyl (sulfanyl) radical on a cysteine residue, which attacks the substrate, forming a ribonucleotide 3'-radical, followed by water loss to form a ketyl (alpha-oxoalkyl) radical.
  • The ketyl radical gains an electron from a cysteine residue and a proton from formic acid, forming 3'-keto-deoxyribonucleotide and generating a thiosulfuranyl (1-lambda(4)-disulfan-1-yl) radical bridge between methionine and cysteine residues.
  • Oxidation of formate by the thiosulfuranyl radical results in the release of CO(2) and regeneration of the thiyl radical.
  • Cf. EC 1.17.4.1 and EC 1.17.4.2.
 5158 A0A023Z6Y4 A0A023Z6Y4 A0A023Z6Y4 A0A023Z6Y4 A0A023Z6Y4 A0A023Z6Y4 A0A023Z6Y4 A0A023Z6Y4 A0A023Z6Y4 A0A023Z6Y4
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