×

Network disruptions

We have been experiencing disruptions on our local network which has affected the stability of these web pages. We have been working with IT support team to get this fixed as a matter of urgency and apologise for any inconvenience.

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.
CATH-Gene3D is a Global Biodata Core Resource Learn more...