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CATH Superfamily 3.20.20.20

Dihydropteroate synthase-like

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:

"
Dihydropteroate synthase-like
".

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: Probable bifunctional folylpolyglutamate synthase/...

There are 4 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
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.
 21 A0A0E9D8B1 A0A0E9D8B1 A0A0E9D8B1 A0A0E9D8B1 A0A0H2X2W0 A0A0H2X2W0 A0A0H2X2W0 A0A0H2X2W0 B0R3B1 B0R3B1
(11 more...)
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.
 17 A0A0E9D8B1 A0A0E9D8B1 A0A0E9D8B1 A0A0E9D8B1 A0A0H2X2W0 A0A0H2X2W0 A0A0H2X2W0 A0A0H2X2W0 G4NMQ8 G4NMQ8
(7 more...)
Tetrahydrofolate synthase. [EC: 6.3.2.17]
ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
  • In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.12, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates (H(4)folate).
  • In contrast, the activities are located on separate proteins in most eukaryotes studied to date.
  • In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast.
  • Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes.
  • As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C(1) metabolism.
  • The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates.
 4 B0R3B1 B0R3B1 Q9HS44 Q9HS44
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 Q54YD9