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CATH Superfamily 3.30.70.560

7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK

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:

"
7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK
".

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 15: Folic acid synthesis protein fol1

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
Dihydroneopterin aldolase. [EC: 4.1.2.25]
7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde.
  • The enzyme participates in folate (in bacteria, plants and fungi) and methanopterin (in archaea) biosynthesis.
  • The enzymes from the bacterium Escherichia coli and the plant Arabidopsis thaliana also catalyze the epimerisation of the 2' hydroxy-group (EC 5.1.99.8).
  • The enzyme from the bacterium Mycobacterium tuberculosis is trifunctional and also catalyzes EC 5.1.99.8 and EC 1.13.11.81.
  • The enzyme from the yeast Saccharomyces cerevisiae also catalyzes the two subsequent steps in the folate biosynthesis pathway - EC 2.7.6.3 and EC 2.5.1.15.
 1 Q4LB35
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase. [EC: 2.7.6.3]
ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP + 6-hydroxymethyl-7,8- dihydropterin diphosphate.
  • The enzyme participates in the pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea).
  • The enzyme exists in varying types of multifunctional proteins in different organisms.
  • The enzyme from the bacterium Streptococcus pneumoniae also harbors the activity of EC 4.1.2.25, the enzyme from the plant Arabidopsis thaliana harbors the activity of EC 2.5.1.15, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with both of the two above mentioned activities.
 1 Q4LB35
Dihydropteroate synthase. [EC: 2.5.1.15]
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.
  • The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea).
  • The enzyme exists in varying types of multifunctional proteins in different organisms.
  • The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25.
 1 Q4LB35
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