Information on EC 5.4.99.24 - 23S rRNA pseudouridine955/2504/2580 synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
5.4.99.24
-
RECOMMENDED NAME
GeneOntology No.
23S rRNA pseudouridine955/2504/2580 synthase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
23S rRNA uridine955/uridine2504/uridine2580 = 23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
23S rRNA-uridine955/2504/2580 uracil mutase
The enzyme converts uridines at position 955, 2504 and 2580 of 23S rRNA to pseudouridines.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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 uridine955/uridine2504/uridine2580
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
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 uridine955/uridine2504/uridine2580
23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
show the reaction diagram
-
-
-
-
?
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
RluC is associates with a pre-50S ribosomal particle
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
analytical ultracentrifugation sedimentation velocity experiments show that RluC(92-319) is monomeric in solution
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity. Crystals of this fragment, grown by precipitation with sodium acetate at pH 8.0, belong to space group P321, with unit-cell dimensions a = b = 97.1, c = 86.3 A and have two molecules in the crystallographic asymmetric unit. Crystals diffract X-rays to at least 2.3 A resolution and appear suitable for crystal structure determination
-
crystals of the catalytic domain RluC(92-319) are grown at 20°C using the hanging drop method
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity
Show AA Sequence (275 entries)
Please use the Sequence Search for a specific query.