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CATH Superfamily 3.40.50.620

HUPs

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:

"
HUPs
".

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 21: Riboflavin biosynthesis protein

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
FAD synthetase. [EC: 2.7.7.2]
ATP + FMN = diphosphate + FAD.
  • Highly specific for ATP as phosphate donor.
  • The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B6, vitamin B12 and folates.
  • While monofunctional FAD synthetase is found in eukaryotes and in some prokaryotes, most prokaryotes have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.1.26.
 12331 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52
(12321 more...)
Riboflavin kinase. [EC: 2.7.1.26]
ATP + riboflavin = ADP + FMN.
  • The cofactors FMN and FAD participate in numerous processes in all organisms, including mitochondrial electron transport, photosynthesis, fatty-acid oxidation, and metabolism of vitamin B(6), vitamin B12 and folates.
  • While monofunctional riboflavin kinase is found in eukaryotes, some bacteria have a bifunctional enzyme that exhibits both this activity and that of EC 2.7.7.2.
  • In Bacillus subtilis, ATP can be replaced by other phosphate donors but with decreasing enzyme activity in the order ATP > dATP > CTP > UTP.
 12331 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52 A0A025CL52
(12321 more...)
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