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Protein

Ribosomal large subunit pseudouridine synthase E

Gene

rluE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Responsible for synthesis of pseudouridine from uracil-2457 in 23S ribosomal RNA.1 Publication

Catalytic activityi

23S rRNA uridine(2457) = 23S rRNA pseudouridine(2457).1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei79 – 791Nucleophile1 Publication

GO - Molecular functioni

  • pseudouridine synthase activity Source: EcoCyc
  • RNA binding Source: InterPro

GO - Biological processi

  • enzyme-directed rRNA pseudouridine synthesis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

rRNA processing

Enzyme and pathway databases

BioCyciEcoCyc:G6581-MONOMER.
ECOL316407:JW1121-MONOMER.
MetaCyc:G6581-MONOMER.
BRENDAi5.4.99.20. 2026.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosomal large subunit pseudouridine synthase E (EC:5.4.99.20)
Alternative name(s):
rRNA pseudouridylate synthase E
rRNA-uridine isomerase E
Gene namesi
Name:rluE
Synonyms:ymfC
Ordered Locus Names:b1135, JW1121
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13447. rluE.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 791D → N or T: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 217217Ribosomal large subunit pseudouridine synthase EPRO_0000100001Add
BLAST

Proteomic databases

PaxDbiP75966.
PRIDEiP75966.

Interactioni

Protein-protein interaction databases

BioGridi4263127. 17 interactions.
DIPiDIP-12716N.
IntActiP75966. 8 interactions.
STRINGi511145.b1135.

Structurei

Secondary structure

1
217
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi41 – 466Combined sources
Helixi63 – 653Combined sources
Beta strandi73 – 764Combined sources
Beta strandi83 – 908Combined sources
Helixi92 – 998Combined sources
Beta strandi107 – 1159Combined sources
Helixi119 – 1279Combined sources
Beta strandi140 – 1445Combined sources
Beta strandi165 – 1739Combined sources
Helixi179 – 1868Combined sources
Beta strandi191 – 1999Combined sources
Beta strandi212 – 2143Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLWX-ray1.60A/B1-217[»]
2OMLX-ray1.20A29-217[»]
ProteinModelPortaliP75966.
SMRiP75966. Positions 36-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP75966.

Family & Domainsi

Sequence similaritiesi

Belongs to the pseudouridine synthase RsuA family.Curated

Phylogenomic databases

eggNOGiENOG4108R99. Bacteria.
COG1187. LUCA.
HOGENOMiHOG000044955.
InParanoidiP75966.
KOiK06181.
OMAiTWIELSI.
OrthoDBiEOG6130DV.
PhylomeDBiP75966.

Family and domain databases

InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR000748. PsdUridine_synth_RsuA/RluB/E/F.
IPR018496. PsdUridine_synth_RsuA/RluB_CS.
IPR006145. PsdUridine_synth_RsuA/RluD.
[Graphical view]
PfamiPF00849. PseudoU_synth_2. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
TIGRFAMsiTIGR00093. TIGR00093. 1 hit.
PROSITEiPS01149. PSI_RSU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P75966-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRQFIISENT MQKTSFRNHQ VKRFSSQRST RRKPENQPTR VILFNKPYDV
60 70 80 90 100
LPQFTDEAGR KTLKEFIPVQ GVYAAGRLDR DSEGLLVLTN NGALQARLTQ
110 120 130 140 150
PGKRTGKIYY VQVEGIPTQD ALEALRNGVT LNDGPTLPAG AELVDEPAWL
160 170 180 190 200
WPRNPPIRER KSIPTSWLKI TLYEGRNRQV RRMTAHVGFP TLRLIRYAMG
210
DYSLDNLANG EWREVTD
Length:217
Mass (Da):24,880
Last modified:December 15, 1998 - v2
Checksum:iF7C7A7CEDC5FD3F6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74219.2.
AP009048 Genomic DNA. Translation: BAA35957.1.
PIRiD64858.
RefSeqiNP_415653.4. NC_000913.3.
WP_001248691.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC74219; AAC74219; b1135.
BAA35957; BAA35957; BAA35957.
GeneIDi945701.
KEGGiecj:JW1121.
eco:b1135.
PATRICi32117519. VBIEscCol129921_1182.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00096 Genomic DNA. Translation: AAC74219.2.
AP009048 Genomic DNA. Translation: BAA35957.1.
PIRiD64858.
RefSeqiNP_415653.4. NC_000913.3.
WP_001248691.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLWX-ray1.60A/B1-217[»]
2OMLX-ray1.20A29-217[»]
ProteinModelPortaliP75966.
SMRiP75966. Positions 36-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263127. 17 interactions.
DIPiDIP-12716N.
IntActiP75966. 8 interactions.
STRINGi511145.b1135.

Proteomic databases

PaxDbiP75966.
PRIDEiP75966.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC74219; AAC74219; b1135.
BAA35957; BAA35957; BAA35957.
GeneIDi945701.
KEGGiecj:JW1121.
eco:b1135.
PATRICi32117519. VBIEscCol129921_1182.

Organism-specific databases

EchoBASEiEB3221.
EcoGeneiEG13447. rluE.

Phylogenomic databases

eggNOGiENOG4108R99. Bacteria.
COG1187. LUCA.
HOGENOMiHOG000044955.
InParanoidiP75966.
KOiK06181.
OMAiTWIELSI.
OrthoDBiEOG6130DV.
PhylomeDBiP75966.

Enzyme and pathway databases

BioCyciEcoCyc:G6581-MONOMER.
ECOL316407:JW1121-MONOMER.
MetaCyc:G6581-MONOMER.
BRENDAi5.4.99.20. 2026.

Miscellaneous databases

EvolutionaryTraceiP75966.
PROiP75966.

Family and domain databases

InterProiIPR020103. PsdUridine_synth_cat_dom.
IPR000748. PsdUridine_synth_RsuA/RluB/E/F.
IPR018496. PsdUridine_synth_RsuA/RluB_CS.
IPR006145. PsdUridine_synth_RsuA/RluD.
[Graphical view]
PfamiPF00849. PseudoU_synth_2. 1 hit.
[Graphical view]
SUPFAMiSSF55120. SSF55120. 1 hit.
TIGRFAMsiTIGR00093. TIGR00093. 1 hit.
PROSITEiPS01149. PSI_RSU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Identification and site of action of the remaining four putative pseudouridine synthases in Escherichia coli."
    Del Campo M., Kaya Y., Ofengand J.
    RNA 7:1603-1615(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-79.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "The crystal structure of E. coli rRNA pseudouridine synthase RluE."
    Pan H., Ho J.D., Stroud R.M., Finer-Moore J.
    J. Mol. Biol. 367:1459-1470(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 29-217, ACTIVE SITE.

Entry informationi

Entry nameiRLUE_ECOLI
AccessioniPrimary (citable) accession number: P75966
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: January 20, 2016
This is version 121 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.