Information on EC 6.5.1.5 - RNA 3'-terminal-phosphate cyclase (GTP)

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The expected taxonomic range for this enzyme is: Pyrococcus furiosus

EC NUMBER
COMMENTARY hide
6.5.1.5
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RECOMMENDED NAME
GeneOntology No.
RNA 3'-terminal-phosphate cyclase (GTP)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5'-guanosyl [RNA 3'-phosphate cyclase]-Ntau-phosphono-L-histidine + [RNA]-3'-(3'-phospho-ribonucleoside) = [RNA 3'-phosphate cyclase]-L-histidine + [RNA]-3'-ribonucleoside-3'-(5'-diphosphoguanosine)
show the reaction diagram
(1b)
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GTP + [RNA 3'-phosphate cyclase]-L-histidine = 5'-guanosyl [RNA 3'-phosphate cyclase]-Ntau-phosphono-L-histidine + diphosphate
show the reaction diagram
(1a)
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GTP + [RNA]-3'-(3'-phospho-ribonucleoside) = GMP + diphosphate + [RNA]-3'-(2',3'-cyclophospho)-ribonucleoside
show the reaction diagram
overall reaction
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[RNA]-3'-ribonucleoside-3'-(5'-diphosphoguanosine) = [RNA]-3'-(2',3'-cyclophospho)-ribonucleoside + GMP
show the reaction diagram
(1c)
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SYSTEMATIC NAME
IUBMB Comments
RNA-3'-phosphate:RNA ligase (cyclizing, GMP-forming)
The enzyme, which is specific for GTP, was characterized from the archaeon Pyrococcus furiosus. The enzyme converts the 3'-terminal phosphate of various RNA substrates into the 2',3'-cyclic phosphodiester in a GTP-dependent reaction. Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by GTP, forming a phosphoramide bond between guanylate and a histidine residue. The guanylate group is then transferred to the 3'-phosphate terminus of the substrate, forming the capped structure [RNA]-3'-(5'-diphosphoguanosine). Finally, the enzyme catalyses an attack of the vicinal O-2' on the 3'-phosphorus, which results in formation of cyclic phosphate and release of the guanylate. cf. EC 6.5.1.4, RNA-3'-phosphate cyclase (ATP).
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme may contribute to GTP-dependent RNA ligation activity through the 2'-5' RNA ligase
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GTP + RNA 3'-terminal-phosphate
GMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
GTP + RNA 3'-terminal-phosphate
GMP + diphosphate + RNA terminal-2',3'-cyclic-phosphate
show the reaction diagram
Q8U0N7
the enzyme may contribute to GTP-dependent RNA ligation activity through the 2'-5' RNA ligase
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?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
activation, Mn2+ can substitute for Mg2+
Mn2+
activation, Mn2+ can substitute for Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22 - 95
similar activity in the range 22°C-75°C, much higher activity at 95°C
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
x * 37000, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 37000, SDS-PAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpression of the recombinant C-terminal His-tagged protein in the Escherichia coli strain BL21(DE3)pLysS