CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.60 | 4-Layer Sandwich |
|
3.60.20 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
|
3.60.20.10 | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1 |
| Functional Family | Glutamine--fructose-6-phosphate aminotransferase [isomerizing] |
Enzyme Information
| 2.6.1.16 |
Glutamine--fructose-6-phosphate transaminase (isomerizing).
based on mapping to UniProt P17169
L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate.
-!- Although the overall reaction is that of a transferase, the mechanism involves the formation of ketimine between fructose 6-phosphate and a 6-amino group from a lysine residue at the active site, which is subsequently displaced by ammonia (transamidination). -!- Formerly EC 5.3.1.19.
|
UniProtKB Entries (1)
| P17169 |
GLMS_ECOLI
Escherichia coli K-12
Glutamine--fructose-6-phosphate aminotransferase [isomerizing]
|
PDB Structure
| PDB | 1XFG |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Substrate Binding is Required for Assembly of the Active Conformation of the Catalytic Site in Ntn Amidotransferases: Evidence from the 1.8 Angstrom Crystal Structure of the Glutaminase Domain of Glucosamine 6-Phosphate Synthase
Structure
|
