The name of this superfamily has been modified since the most recent official CATH+ release (v4_4_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.
SC:1UDP-N-acetylmuramoylalanine--D-glutamate ligaseDihydrofolate synthase/folylpolyglutamate synthaseFolylpolyglutamate synthase/dihydrofolate synthaseUDP-N-acetylmuramate--L-alanine ligaseUDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligaseDihydrofolate synthase/folylpolyglutamate synthaseUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligaseFolylpolyglutamate synthaseUDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligaseFolylpolyglutamate synthaseDihydrofolate synthetaseFolylpolyglutamate synthaseFolylpolyglutamate synthaseBifunctional folylpolyglutamate synthase/dihydrofolate synthaseDihydrofolate synthetaseDihydrofolate synthase/folylpolyglutamate synthaseUDP-N-acetylmuramate--L-alanine ligaseFolylpolyglutamate synthaseFolylpolyglutamate synthase/dihydrofolate synthaseUDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligaseFolylpolyglutamate synthaseUDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligasePutative dihydrofolate synthetaseBifunctional folylpolyglutamate synthase/dihydrofolate synthaseDihydrofolate synthetaseFolylpolyglutamate synthase/dihydrofolate synthaseUDP-N-acetylmuramoylalanine--D-glutamate ligaseFolylpolyglutamate synthetaseFolylpolyglutamate synthaseBifunctional folylpolyglutamate synthase/dihydrofolate synthaseFolylpolyglutamate synthaseFolylpolyglutamate synthaseBifunctional folylpolyglutamate synthase/dihydrofolate synthaseFolylpolyglutamate synthasePutative folylpolyglutamate synthaseBifunctional folylpolyglutamate synthase/dihydrofolate synthasePutative folylpolyglutamate synthaseFolylpolyglutamate synthaseBifunctional tetrahydrofolate synthase/dihydrofolate synthaseUncharacterized proteinDihydrofolate synthase, putativeFolylpolyglutamate synthase/dihydrofolate synthaseFolyl-polyglutamate synthetaseFolylpolyglutamate synthaseTetrahydrofolate synthaseDihydrofolate synthaseDihydrofolate synthetaseFolyl-polyglutamate synthetaseUncharacterized proteinFolC bifunctional proteinTetrahydrofolylpolyglutamate synthase, putativeFolylpolyglutamate synthetase, putativeFolylpolyglutamate synthaseFolylpolyglutamate synthaseFolylpolyglutamate synthaseDihydrofolate synthetaseMur ligaseBifunctional folylpolyglutamate synthase/dihydrofolate synthaseBifunctional folylpolyglutamate synthase/dihydrofolate synthaseFolylpolyglutamate synthaseFolylpolyglutamate synthase / 7,8-dihydropteroate reductase / dihydropteroate synthaseFolylpolyglutamate synthetaseFolylpolyglutamate synthetaseFolylpolyglutamate synthaseUncharacterized proteinUncharacterized proteinPredicted proteinUncharacterized proteinFolylpolyglutamate synthaseFolylpolyglutamate synthasePutative folylpolyglutamate synthaseFolylpolyglutamate synthase, mitochondrial-like ProteinFolylpolyglutamate synthaseFolylpolyglutamate synthaseFolC bifunctional proteinUncharacterized protein
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FunFam 14: Dihydrofolate synthetase

There are 1 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 TermAnnotationsEvidence
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 F4JYE9
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