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 | GMP synthase [glutamine-hydrolyzing] |
Enzyme Information
| 6.3.5.2 |
GMP synthase (glutamine-hydrolyzing).
based on mapping to UniProt P04079
ATP + XMP + L-glutamine + H(2)O = AMP + diphosphate + GMP + L-glutamate.
-!- Involved in the de novo biosynthesis of guanosine nucleotides. -!- An N-terminal glutaminase domain binds L-glutamine and generates ammonia, which is transferred by a substrate-protective tunnel to the ATP-pyrophosphatase domain. -!- The enzyme can catalyze the second reaction alone in the presence of ammonia. -!- Formerly EC 6.3.4.1.
|
UniProtKB Entries (1)
| P04079 |
GUAA_ECOLI
Escherichia coli K-12
GMP synthase [glutamine-hydrolyzing]
|
PDB Structure
| PDB | 1GPM |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
Nat.Struct.Biol.
|
