Information on EC 5.4.99.22 - 23S rRNA pseudouridine2605 synthase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
5.4.99.22
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RECOMMENDED NAME
GeneOntology No.
23S rRNA pseudouridine2605 synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
23S rRNA uridine2605 = 23S rRNA pseudouridine2605
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
23S rRNA-uridine2605 uracil mutase
Pseudouridine synthase RluB converts uridine2605 of 23S rRNA to pseudouridine.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
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RluB is associated with a particle that migrates slightly slower than the 50S ribosomal subunit, suggesting that it acts during 50S subunit maturation
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
23S rRNA uridine2605
23S rRNA pseudouridine2605
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
23S rRNA uridine2605
23S rRNA pseudouridine2605
show the reaction diagram
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?
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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RluB is associated with a particle the migrates slightly slower than the 50S ribosomal subunit, suggesting that it acts during 50S subunit maturation
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the 1.3 A structure of RluB in complex with a 21-mer stem-loop substrate, in which U2605 is substituted by 5-fluorouridine. The structure reveals a covalent bond between the phenolic hydroxyl of the conserved active site Tyr140 and C6 of the isomerized 5-fluorouridine
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D110N
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inactive mutant enzyme
D110T
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inactive mutant enzyme
Show AA Sequence (149 entries)
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