Information on EC 5.4.99.20 - 23S rRNA pseudouridine2457 synthase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.4.99.20
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RECOMMENDED NAME
GeneOntology No.
23S rRNA pseudouridine2457 synthase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
23S rRNA uridine2457 = 23S rRNA pseudouridine2457
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
23S rRNA-uridine2457 uracil mutase
The enzyme modifies uridine2457 in a stem of 23S RNA in Escherichia coli.
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
malfunction
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 uridine2457
23S rRNA pseudouridine2457
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 uridine2457
23S rRNA pseudouridine2457
show the reaction diagram
P75966
pseudouridine synthase RluE modifies U2457 in a stem of 23S RNA in Escherichia coli. This modification is located in the peptidyl transferase center of the ribosome.The stem alone is not a good RluE substrate, suggesting RluE undergoes additional interactions with other regions in the ribosome
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?
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24900
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24900, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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24900, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method, crystal structures of the C-terminal, catalytic domain of Escherichia coli RluE at 1.2 A resolution and of full-length RluE at 1.6 A resolution. The crystals of the full-length enzyme contain two molecules in the asymmetric unit and in both molecules the N-terminal domain is disordered. The higher resolution, truncated RluE structure is used for analysis and for comparison to other pseudouridine synthases
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D79N
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inactive mutant enzyme
D79T
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inactive mutant enzyme