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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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

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
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.
 115 A0A037Y8A4 A0A045I525 A0A059I0I5 A0A063XCZ2 A0A069QAV9 A0A069XP94 A0A069ZSX0 A0A070T0V4 A0A070UFS9 A0A0B6U2D1
(105 more...)
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.
 18 A0A069ZSX0 A0A0E9D8B1 A0A0F7WQE2 A0A0H2X2W0 A0A178UTC5 B3LP99 G4NMQ8 O04862 O84619 P29251
(8 more...)
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.
 9 A0A0H2ZRK9 A0A0T8TRH7 B3LP99 P22291 P29251 P53848 P59657 Q4LB35 Q54YD9
GTP cyclohydrolase I. [EC: 3.5.4.16]
GTP + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate.
  • The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic.
  • Involved in the de novo synthesis of tetrahydrobiopterin from GTP, with the other enzymes involved being EC 1.1.1.153 and EC 4.2.3.12.
 6 A0A0M2ZWW1 A0A1E7G3J9 A0A2X0PNK4 A0A3B0GID6 Q8GJP4 Q9CGE3