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 P0A6T5
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)
P0A6T5 |
GCH1_ECOLI
Escherichia coli K-12
GTP cyclohydrolase 1
|
PDB Structure
PDB | 1FBX |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Zinc plays a key role in human and bacterial GTP cyclohydrolase I.
Proc.Natl.Acad.Sci.USA
|