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CATH Superfamily 3.90.190.20

Mur ligase, C-terminal domain

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:

"
Mur ligase, C-terminal domain
".

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 5: Dihydrofolate synthase/folylpolyglutamate synthase

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
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.
 553 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0
(543 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.
 553 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0 A0A069XRP0
(543 more...)