CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.880 | Class I glutamine amidotransferase (GATase) domain |
Domain Context
CATH Clusters
| Superfamily | 3.40.50.880 |
| Functional Family | Folate gamma-glutamyl hydrolase |
Enzyme Information
| 3.4.19.9 |
Folate gamma-glutamyl hydrolase.
based on mapping to UniProt Q92820
Tetrahydropteroyl-(gamma-glutamyl)(n) + (n-1) H(2)O = 5,6,7,8- tetrahydrofolate + (n-1) L-glutamate.
-!- The enzyme, which occurs only in animals and plants, can be either endo- and/or exopeptidase. -!- It acts on tetrahydropteroyl polyglutamates and their modified forms, as well as the polyglutamates of the folate breakdown product N-(4-aminobenzoyl)-L-glutamate (pABA-Glu). -!- The initial cleavage may release either monoglutamate or poly-gamma- glutamate of two or more residues, depending on the specific enzyme. -!- For example, GGH1 from the plant Arabidopsis thaliana cleaves pentaglutamates, mainly to di- and triglutamates, whereas GGH2 from the same organism yields mainly monoglutamates. -!- The enzyme is lysosomal (and secreted) in animals and vacuolar in plants. -!- Belongs to peptidase family C26. -!- Formerly EC 3.4.12.10 and EC 3.4.22.12.
|
UniProtKB Entries (1)
| Q92820 |
GGH_HUMAN
Homo sapiens
Gamma-glutamyl hydrolase
|
PDB Structure
| PDB | 1L9X |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate.
J.Biol.Chem.
|
