EzCatDB: D00263

DB codeD00263
CATH domainDomain 13.30.70.660
Domain 23.30.70.580Catalytic domain
E.C.5.4.99.12
CSA1dj0


Enzyme Name
Swiss-protKEGG

P07649
Protein nametRNA pseudouridine synthase AtRNA-pseudouridine synthase I
tRNA-uridine isomerase
tRNA pseudouridylate synthase I
transfer ribonucleate pseudouridine synthetase
pseudouridine synthase
transfer RNA pseudouridine synthetase
SynonymsEC 5.4.99.12
tRNA-uridine isomerase I
tRNA pseudouridylate synthase I
PSU-I


Swiss-prot:Accession NumberP07649
Entry nameTRUA_ECOLI
ActivitytRNA uridine = tRNA pseudouridine.
SubunitHomodimer.
Subcellular location
Cofactor


SubstratesProducts
KEGG-idC00868C02764
CompoundtRNA uridinetRNA pseudouridine
Typeamide group,nucleic acidsamide group,nucleic acids
1dj0A01UnboundUnbound
1dj0B01UnboundUnbound
1dj0A02UnboundUnbound
1dj0B02UnboundUnbound

Active-site residues
resource
Swiss-prot;P07649
pdbCatalytic residues
1dj0A01
1dj0B01
1dj0A02ASP 60
1dj0B02ASP 60

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[3]Scheme 2, p.349-3504
[5]Fig.3, p.131076
[9]Fig.1, p.235
[10]Fig.2, p.321-3226

references
[1]
PubMed ID9358157
JournalNucleic Acids Res
Year1997
Volume25
Pages4493-9
AuthorsBecker HF, Motorin Y, Planta RJ, Grosjean H
TitleThe yeast gene YNL292w encodes a pseudouridine synthase (Pus4) catalyzing the formation of psi55 in both mitochondrial and cytoplasmic tRNAs.
[2]
PubMed ID9585540
JournalBiochemistry
Year1998
Volume37
Pages7268-76
AuthorsArluison V, Hountondji C, Robert B, Grosjean H
TitleTransfer RNA-pseudouridine synthetase Pus1 of Saccharomyces cerevisiae contains one atom of zinc essential for its native conformation and tRNA recognition.
[3]
CommentsACTIVE SITE
Medline ID98087694
PubMed ID9425056
JournalBiochemistry
Year1998
Volume37
Pages344-51
AuthorsHuang L, Pookanjanatavip M, Gu X, Santi DV
TitleA conserved aspartate of tRNA pseudouridine synthase is essential for activity and a probable nucleophilic catalyst.
Related Swiss-protP07649
[4]
PubMed ID10089432
JournalActa Crystallogr D Biol Crystallogr
Year1999
Volume55
Pages302-4
AuthorsCorollo D, Blair-Johnson M, Conrad J, Fiedler T, Sun D, Wang L, Ofengand J, Fenna R
TitleCrystallization and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli.
[5]
PubMed ID10529181
JournalBiochemistry
Year1999
Volume38
Pages13106-11
AuthorsRamamurthy V, Swann SL, Spedaliere CJ, Mueller EG
TitleRole of cysteine residues in pseudouridine synthases of different families.
[6]
PubMed ID10428788
JournalJ Biol Chem
Year1999
Volume274
Pages22225-30
AuthorsRamamurthy V, Swann SL, Paulson JL, Spedaliere CJ, Mueller EG
TitleCritical aspartic acid residues in pseudouridine synthases.
[7]
PubMed ID10022901
JournalMol Cell Biol
Year1999
Volume19
Pages2142-54
AuthorsMassenet S, Motorin Y, Lafontaine DL, Hurt EC, Grosjean H, Branlant C
TitlePseudouridine mapping in the Saccharomyces cerevisiae spliceosomal U small nuclear RNAs (snRNAs) reveals that pseudouridine synthase pus1p exhibits a dual substrate specificity for U2 snRNA and tRNA.
[8]
PubMed ID10924141
JournalBiochemistry
Year2000
Volume39
Pages9459-65
AuthorsSpedaliere CJ, Hamilton CS, Mueller EG
TitleFunctional importance of motif I of pseudouridine synthases: mutagenesis of aligned lysine and proline residues.
[9]
CommentsX-ray crystallography
PubMed ID10625422
JournalNat Struct Biol
Year2000
Volume7
Pages23-7
AuthorsFoster PG, Huang L, Santi DV, Stroud RM
TitleThe structural basis for tRNA recognition and pseudouridine formation by pseudouridine synthase I.
Related PDB1dj0
[10]
PubMed ID11976723
JournalNat Struct Biol
Year2002
Volume9
Pages320-2
AuthorsMueller EG
TitleChips off the old block.
[11]
PubMed ID11953756
JournalNat Struct Biol
Year2002
Volume9
Pages353-8
AuthorsSivaraman J, Sauve V, Larocque R, Stura EA, Schrag JD, Cygler M, Matte A
TitleStructure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP.
[12]
PubMed ID12515383
JournalRNA
Year2002
Volume8
Pages1502-14
AuthorsFatica A, Dlakic M, Tollervey D
TitleNaf1 p is a box H/ACA snoRNP assembly factor.


createdupdated
2004-03-252009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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