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CATH Superfamily 1.10.286.10

GTP cyclohydrolase I, N-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_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 1694: GTP cyclohydrolase 1

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
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.
 243 A0A010NK48 A0A024DCU3 A0A062WL35 A0A068LDT6 A0A072X0K2 A0A072XD80 A0A072YD11 A0A072YR49 A0A081PT99 A0A081Q4D0
(233 more...)
Dihydrofolate synthase. [EC: 6.3.2.12]
ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8- dihydropteroylglutamate.
  • In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.17, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates.
  • In contrast, the activities are located on separate proteins in most eukaryotes studied to date.
  • This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa.
 1 A0A0U0KHT7
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