Information on EC 6.3.5.2 - GMP synthase (glutamine-hydrolysing) and Organism(s) Pyrococcus horikoshii and UniProt Accession O59072

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Pyrococcus horikoshii
UNIPROT: O59072


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea


The taxonomic range for the selected organisms is: Pyrococcus horikoshii

EC NUMBER
COMMENTARY hide
6.3.5.2
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RECOMMENDED NAME
GeneOntology No.
GMP synthase (glutamine-hydrolysing)
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amination
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
guanosine ribonucleotides de novo biosynthesis
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purine metabolism
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Purine metabolism
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Drug metabolism - other enzymes
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
xanthosine-5'-phosphate:L-glutamine amido-ligase (AMP-forming)
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 catalyse the second reaction alone in the presence of ammonia.
CAS REGISTRY NUMBER
COMMENTARY hide
37318-71-1
not distinguished from EC 6.3.4.1
9023-55-6
EC 6.3.4.1
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GMP synthase [glutamine-hydrolyzing] subunit B; strain OT3
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
GMPS catalyzes the final step of the de novo synthetic pathway of purine nucleotides
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + xanthosine 5'-phosphate + NH3
AMP + diphosphate + GMP
show the reaction diagram
overall reaction
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?
L-glutamine + H2O
L-glutamate + NH3
show the reaction diagram
GATase half-reaction, structure-activity relationship of the functional subunits, overview
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?
XMP + Mg-ATP2-
adenyl-XMP + diphosphate + Mg2+
show the reaction diagram
ATPPase half-reaction, structure-activity relationship of the functional subunits, overview
adenyl-XMP is the overall reaction intermediate
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
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LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
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LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
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LITERATURE
IMAGE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
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LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
GMPS consists of two functional units that are present as domains or subunits: glutamine amidotransferase, GATase, and 34 kDa ATP pyrophosphatase, ATPPase. Domain structure and interactions, structure-activity relationship of the functional subunits, overview
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATPPase subunit of the two-subunit-type GMPS, sitting drop vapor diffusion at 5°C, mixing of 0.001 ml of protein solution containing 30 mg/ml protein in Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 30% v/v PEG 400, 100 mM Tris-HCl, pH 8.4, and 200 mM MgCl2, equilibration against 0.1 ml of reservoir solution, 3 weeks, X-ray diffraction structure determination and analysis at 1.8 A resolution; crystal structure of the ATPPase subunit of the two-subunit-type GMPS, to 1.79 A resolution. ATPPase consists of a N-domain and a C-domain and exists as a homodimer in the crystal and in solution. The N-domain contains an ATP-binding platform called P-loop, whereas the C-domain contains the xanthosine 5'-monophosphate-binding site and also contributes to homodimerization. The glutamine amidotransferase subunit of the two-subunit-type GMPS alone is inactive, and substrates Mg2+, ATP and XMP of PH-ATPPase except for ammonia are required to stabilize the active complex of ATPPase and GATase subunits
hanging-drop vapor-diffusion method at 5°C, crystal structure is determined at 1.89 A resolution. Its overall structure and active site are the most similar to those of Escherichia coli guanosine 5'-monophosphate synthase and Sulfolobus solfataricus anthranilate synthase, respectively
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
all substrates of PH-ATPPase, Mg2+, ATP and XMP, except for ammonia, are required to stabilize the active complex of PH-ATPPase and PH-GATase subunits
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli; genes ph1346 and ph1347, genetic structure of GMPS, overview. Expressionin Escherichia coli strain BL21(DE3)
expression in Escherichia coli