CATH Classification

Domain Context

CATH Clusters

Superfamily HUPs
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.
Tesmer, J.J., Klem, T.J., Deras, M.L., Davisson, V.J., Smith, J.L.
Nat.Struct.Biol.