CATH Classification
| Level | CATH Code | Description | 
|---|---|---|
|   | 1 | Mainly Alpha | 
|   | 1.10 | Orthogonal Bundle | 
|   | 1.10.286 | GTP Cyclohydrolase I; Chain A, domain 1 | 
|   | 1.10.286.10 | GTP cyclohydrolase I, N-terminal domain | 
Domain Context
CATH Clusters
| Superfamily | 1.10.286.10 | 
| Functional Family | GTP cyclohydrolase 1 | 
Enzyme Information
| 3.5.4.16 | GTP cyclohydrolase I. based on mapping to UniProt P22288 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. | 
UniProtKB Entries (1)
| P70552 | GFRP_RAT Rattus norvegicus GTP cyclohydrolase 1 feedback regulatory protein | 
PDB Structure
| PDB | 1IS7 | 
| External Links | |
| Method | X-RAY DIFFRACTION | 
| Organism | Escherichia | 
| Primary Citation | Crystal structure of the stimulatory complex of GTP cyclohydrolase I and its feedback regulatory protein GFRP. Proc.Natl.Acad.Sci.USA | 
