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Information on EC 5.4.99.22 - 23S rRNA pseudouridine2605 synthase and Organism(s) Escherichia coli and UniProt Accession P37765

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EC Tree
     5 Isomerases
         5.4 Intramolecular transferases
             5.4.99 Transferring other groups
                5.4.99.22 23S rRNA pseudouridine2605 synthase
IUBMB Comments
Pseudouridine synthase RluB converts uridine2605 of 23S rRNA to pseudouridine.
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This record set is specific for:
Escherichia coli
UNIPROT: P37765
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
23S rRNA uridine2605
=
23S rRNA pseudouridine2605
Synonyms
RluB, YciL, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SYSTEMATIC NAME
IUBMB Comments
23S rRNA-uridine2605 uracil mutase
Pseudouridine synthase RluB converts uridine2605 of 23S rRNA to pseudouridine.
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 SUBSTRATE
NATURAL 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
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
RluB is associated with a particle the migrates slightly slower than the 50S ribosomal subunit, suggesting that it acts during 50S subunit maturation
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
RluB is associated with a particle that migrates slightly slower than the 50S ribosomal subunit, suggesting that it acts during 50S subunit maturation
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D110N
inactive mutant enzyme
D110T
inactive mutant enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using Ni-NTA chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a His-tagged fusion protein
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jiang, M.; Sullivan, S.M.; Walker, A.K.; Strahler, J.R.; Andrews, P.C.; Maddock, J.R.
Identification of novel Escherichia coli ribosome-associated proteins using isobaric tags and multidimensional protein identification techniques
J. Bacteriol.
189
3434-3444
2007
Escherichia coli (P37765)
Manually annotated by BRENDA team
Del Campo, M.; Kaya, Y.; Ofengand, J.
Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli
RNA
7
1603-1615
2001
Escherichia coli (P37765)
Manually annotated by BRENDA team
Czudnochowski, N.; Ashley, G.W.; Santi, D.V.; Alian, A.; Finer-Moore, J.; Stroud, R.M.
The mechanism of pseudouridine synthases from a covalent complex with RNA, and alternate specificity for U2605 versus U2604 between close homologs
Nucleic Acids Res.
42
2037-2048
2014
Escherichia coli (P37765)
Manually annotated by BRENDA team