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

for references in articles please use BRENDA:EC5.4.99.24
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The expected taxonomic range for this enzyme is: Escherichia coli

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EC NUMBER
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5.4.99.24
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RECOMMENDED NAME
GeneOntology No.
23S rRNA pseudouridine955/2504/2580 synthase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
23S rRNA uridine955/uridine2504/uridine2580 = 23S rRNA pseudouridine955/pseudouridine2504/pseudouridine2580
show the reaction diagram
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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.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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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
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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
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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RluC is associates with a pre-50S ribosomal particle
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Manually annotated by BRENDA team
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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analytical ultracentrifugation sedimentation velocity experiments show that RluC(92-319) is monomeric in solution
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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
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crystals of the catalytic domain RluC(92-319) are grown at 20°C using the hanging drop method
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
overexpressed in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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a proteolytically derived fragment of the enzyme consisting of residues 89-319 retains catalytic activity
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Show AA Sequence (352 entries)
Please use the Sequence Search for a specific query.
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LINKS TO OTHER DATABASES (specific for EC-Number 5.4.99.24)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)