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Information on EC 4.2.1.70 - pseudouridylate synthase and Organism(s) Escherichia coli and UniProt Accession P33025

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.70 pseudouridylate synthase
IUBMB Comments
The reaction it readily reversible. While the enzymes from Tetrahymena pyriformis and Agrobacterium tumefaciens produce pseudouridine 5'-phosphate the enzyme from Escherichia coli functions as a pseudouridine-5'-phosphate glycosidase in vivo .
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This record set is specific for:
Escherichia coli
UNIPROT: P33025
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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
Synonyms
pseudouridine synthase, p35 protein, pseudouridine synthase i, pseudouridylate synthase, psi55 synthase, pseudouridylate synthetase, pseudouridine-5'-phosphate glycosidase, trna pseudouridine 55 synthase, orp protein, psi55 trna pseudouridine synthase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pseudouridine-5'-phosphate glycosidase
-
16S pseudouridine 516 synthase
-
-
-
-
16S pseudouridylate 516 synthase
-
-
-
-
5-ribosyluracil 5'-phosphate synthetase
-
-
-
-
Depressed growth-RATE protein DEG1
-
-
-
-
ORP protein
-
-
-
-
Osmoprotectant regulator of PLC
-
-
-
-
P35 protein
-
-
-
-
pseudouridine monophosphate synthetase
-
-
-
-
pseudouridine synthase
pseudouridine synthase I
-
-
-
-
Pseudouridylate synthase
-
-
-
-
pseudouridylate synthetase
-
-
-
-
pseudouridylate synthetase I
-
-
-
-
pseudouridylate synthetase II
-
-
-
-
pseudouridylic acid synthetase
-
-
-
-
PSI55 synthase
-
-
-
-
psiMP synthetase
-
-
-
-
psisynthetase
-
-
-
-
psiUMP synthetase
-
-
-
-
PSUI
-
-
-
-
synthase, pseudouridylate
-
-
-
-
tRNA pseudouridine 55 synthase
-
-
-
-
uracil hydrolyase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
elimination
-
of H2O, C-O bond cleavage
addition
-
of H2O
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
uracil hydro-lyase (adding D-ribose 5-phosphate; pseudouridine-5'-phosphate-forming)
The reaction it readily reversible. While the enzymes from Tetrahymena pyriformis and Agrobacterium tumefaciens produce pseudouridine 5'-phosphate the enzyme from Escherichia coli functions as a pseudouridine-5'-phosphate glycosidase in vivo [5].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-35-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
uracil + D-ribose 5-phosphate
pseudouridine 5'-phosphate + H2O
show the reaction diagram
pseudouridine 5' phosphate + H2O
?
show the reaction diagram
pseudouridine 5'-phosphate + H2O
uracil + D-ribose 5-phosphate
show the reaction diagram
uracil + D-ribose 5-phosphate
pseudouridine 5'-phosphate + H2O
show the reaction diagram
additional information
?
-
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
uracil + D-ribose 5-phosphate
pseudouridine 5'-phosphate + H2O
show the reaction diagram
the enzyme is involved in the metabolism of pseudouridine in uropathogenic Escherichia coli
-
-
r
pseudouridine 5' phosphate + H2O
?
show the reaction diagram
uracil + D-ribose 5-phosphate
pseudouridine 5'-phosphate + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
high activity
Fe2+
high activity
Mn2+
high activity
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-(Tetrahydro-2-furanyl)-5-fluorouracil
-
i.e. ftorafur
5-fluorouracil
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06
pseudouridine 5'-phosphate
pH 7.1, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
assay at, both reaction directions
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at, both reaction directions
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
molecular evolution of the bacterial pseudouridine-5-phosphate glycosidase protein family
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
31000
-
pseudouridine synthase I, calculation from genomic sequence
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
pseudouridine synthase RluC fragment
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by affinity chromatography
Ni2+ Sepharose column chromatography and Superdex 75 gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression as His-tagged enzyme in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
RluC, expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Breitman, T.R.
Pseudouridylate synthetase of Escherichia coli: correlation of its activity with utilization of pseudouridine for growth
J. Bacteriol.
103
263-264
1970
Escherichia coli
Manually annotated by BRENDA team
Salomon, L.R.; Breitman, T.R.
Pseudouridylate synthetase of Escherichia coli: a catabolite-repressible enzyme
J. Bacteriol.
107
535-542
1971
Escherichia coli
Manually annotated by BRENDA team
Remsen, J.F.; Matsushita, T.; Chirikjian, J.G.; Davis, F.F.
Enzymatic synthesis of deoxypseudouridylic acid an a study of certain of its properties
Biochim. Biophys. Acta
281
481-487
1972
Agrobacterium tumefaciens, Escherichia coli, Tetrahymena pyriformis, Agrobacterium tumefaciens ATCC 15955
Manually annotated by BRENDA team
Bruni, C.B.; Colantuoni, V.; Sbordone, L.; Cortese, R.; Blasi, F.
Biochemical and regulatory properties of Escherichia coli K-12 hisT mutants
J. Bacteriol.
130
4-10
1977
Escherichia coli
Manually annotated by BRENDA team
Frendewey, D.A.; Kladianos, D.M.; Moore, V.G.; Kaiser, I.I.
Loss of tRNA 5-methyluridine methyltransferase and pseudouridine synthetase activities in 5-fluorouracil and 1-(tetrahydro-2-furanyl)-5-fluorouracil (ftorafur)-treated Escherichia coli
Biochim. Biophys. Acta
697
31-40
1982
Escherichia coli
Manually annotated by BRENDA team
Marvel, C.C.; Arps, P.J.; Rubin, B.C.; Kammen, H.O.; Penhoet, E.E.; Winkler, M.E.
HisT is part of a multigene operon in Escherichia coli K-12
J. Bacteriol.
161
60-71
1985
Escherichia coli
Manually annotated by BRENDA team
Searles, L.L.; Jones, J.W.; Fournier, M.J.; Grambow, N.; Tyler, B.; Calvo, J.M.
Escherichia coli B/r leuK mutant lacking pseudouridine synthase I
J. Bacteriol.
166
341-345
1986
Escherichia coli, Escherichia coli EB146 (leuK16)
Manually annotated by BRENDA team
Arps, P.J.; Winkler, M.E.
An unusual genetic link between vitamin B6 biosynthesis and tRNA pseudouridine modification in Escherichia coli K-12
J. Bacteriol.
169
1071-1079
1987
Escherichia coli
Manually annotated by BRENDA team
Arps, P.J.; Winkler, M.E.
Structural analysis of the Escherichia coli K-12 hisT operon by using a kanamycin resistance cassette
J. Bacteriol.
169
1061-1070
1987
Escherichia coli
Manually annotated by BRENDA team
Corollo, D.; Blair-Johnson, M.; Conrad, J.; Friedler, T.; Sun, D.; Wang, L.; Ofengand, J.; Fenna, R.
Crystallisation and characterization of a fragment of pseudouridine synthase RluC from Escherichia coli
Acta Crystallogr. Sect. D
55
302-304
1999
Escherichia coli
-
Manually annotated by BRENDA team
Chen, J.; Patton, J.R.
Cloning and characterization of a mammalian pseudouridine synthase
RNA
5
409-419
1999
Escherichia coli, Mus musculus
Manually annotated by BRENDA team
Foster, P.G.; Huang, L.; Santi, D.; Stroud, R.
The structural basis of tRNA recognition and pseudouridine formation by pseudouridine synthase I
Nat. Struct. Biol.
7
23-27
2000
Escherichia coli
Manually annotated by BRENDA team
Wouters, J.; Tricot, C.; Durbecq, V.; Roovers, M.; Stalon, V.; Droogmans, L.
Preliminary X-ray crystallographic analysis of tRNA pseudouridine 55 synthase from the thermophilic eubacterium Thermotoga maritima
Acta Crystallogr. Sect. D
59
152-154
2003
Escherichia coli, Escherichia coli TruB, Thermotoga maritima, Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
Manually annotated by BRENDA team
Del Campo, M.; Ofengand, J.; Malhotra, A.
Purification and crystallization of Escherichia coli pseudouridine synthase RluD
Acta Crystallogr. Sect. D
59
1871-1873
2003
Escherichia coli, Escherichia coli RluD
Manually annotated by BRENDA team
Ericsson, U.B.; Andersson, M.E.; Engvall, B.; Nordlund, P.; Hallberg, B.M.
Expression, purification, crystallization and preliminary diffraction studies of the tRNA pseudouridine synthase TruD from Escherichia coli
Acta Crystallogr. Sect. D
60
775-776
2004
Escherichia coli
Manually annotated by BRENDA team
Hoang, C.; Ferre-D'Amare, A.R.
Cocrystal structure of a tRNA psi55 pseudouridine synthase: nucleotide flipping by an RNA-modifying enzyme
Cell
107
929-939
2001
Escherichia coli, Escherichia coli TruB
Manually annotated by BRENDA team
Kaya, Y.; Del Campo, M.; Ofengand, J.; Malhotra, A.
Crystal structure of TruD, a novel pseudouridine synthase with a new protein fold
J. Biol. Chem.
279
18107-18110
2004
Escherichia coli
Manually annotated by BRENDA team
Sivaraman, J.; Iannuzzi, P.; Cygler, M.; Matte, A.
Crystal structure of the RluD pseudouridine synthase catalytic module, an enzyme that modifies 23S rRNA and is essential for normal cell growth of Escherichia coli
J. Mol. Biol.
335
87-101
2004
Escherichia coli, Escherichia coli RluD
Manually annotated by BRENDA team
Sivaraman, J.; Sauve, V.; Larocque, R.; Stura, E.A.; Schrag, J.D.; Cygler, M.; Matte, A.
Structure of the 16S rRNA pseudouridine synthase RsuA bound to uracil and UMP
Nat. Struct. Biol.
9
353-358
2002
Escherichia coli, Escherichia coli RsuA
Manually annotated by BRENDA team
Pan, H.; Agarwalla, S.; Moustakas, D.T.; Finer-Moore, J.; Stroud, R.M.
Structure of tRNA pseudouridine synthase TruB and its RNA complex: RNA recognition through a combination of rigid docking and induced fit
Proc. Natl. Acad. Sci. USA
100
12648-12653
2003
Escherichia coli, Thermotoga maritima, Thermotoga maritima TruB, Escherichia coli TruB
Manually annotated by BRENDA team
Gu, X.; Liu, Y.; Santi, D.V.
The mechanism of pseudouridine synthase I as deduced from its interaction with 5-fluorouracil-tRNA
Proc. Natl. Acad. Sci. USA
96
14270-14275
1999
Escherichia coli
Manually annotated by BRENDA team
Preumont, A.; Snoussi, K.; Stroobant, V.; Collet, J.F.; Van Schaftingen, E.
Molecular identification of pseudouridine-metabolizing enzymes
J. Biol. Chem.
283
25238-25246
2008
Escherichia coli (P33025), Escherichia coli, Thermotoga maritima
Manually annotated by BRENDA team
Wright, J.R.; Keffer-Wilkes, L.C.; Dobing, S.R.; Kothe, U.
Pre-steady-state kinetic analysis of the three Escherichia coli pseudouridine synthases TruB, TruA, and RluA reveals uniformly slow catalysis
RNA
17
2074-2084
2011
Escherichia coli
Manually annotated by BRENDA team
Thapa, K.; Oja, T.; Metsae-Ketelae, M.
Molecular evolution of the bacterial pseudouridine-5-phosphate glycosidase protein family
FEBS J.
281
4439-4449
2014
Escherichia coli (P33025), Escherichia coli, Escherichia coli K12 (P33025)
Manually annotated by BRENDA team