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Information on EC 2.4.2.10 - orotate phosphoribosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P13298

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.2 Pentosyltransferases
                2.4.2.10 orotate phosphoribosyltransferase
IUBMB Comments
The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P13298
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
oprt, orotate phosphoribosyltransferase, oprtase, orotate phosphoribosyl transferase, orotidine monophosphate pyrophosphorylase, omp synthase, orotidine-5'-phosphate pyrophosphorylase, orotic acid phosphoribosyltransferase, orotidylic acid pyrophosphorylase, type i phosphoribosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
OMP synthase
-
-
OPRTase
orotate phosphoribosyl pyrophosphate transferase
-
-
-
-
orotate phosphoribosyltransferase
orotate PRTase
-
-
-
-
orotic acid phosphoribosyltransferase
-
-
-
-
orotidine 5'-monophosphate pyrophosphorylase
-
-
-
-
orotidine 5'-phosphate pyrophosphorylase
-
-
-
-
orotidine monophosphate pyrophosphorylase
-
-
-
-
orotidine phosphoribosyltransferase
-
-
-
-
orotidine-5'-phosphate pyrophosphorylase
-
-
-
-
orotidylate phosphoribosyltransferase
-
-
-
-
orotidylate pyrophosphorylase
-
-
-
-
orotidylic acid phosphorylase
-
-
-
-
orotidylic acid pyrophosphorylase
-
-
-
-
orotidylic phosphorylase
-
-
-
-
orotidylic pyrophosphorylase
-
-
-
-
phosphoribosyltransferase, orotate
-
-
-
-
type I phosphoribosyltransferase
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentosyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
orotidine-5'-phosphate:diphosphate phospho-alpha-D-ribosyl-transferase
The enzyme from higher eukaryotes also catalyses the reaction listed as EC 4.1.1.23, orotidine-5'-phosphate decarboxylase.
CAS REGISTRY NUMBER
COMMENTARY hide
9030-25-5
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
show the reaction diagram
-
-
-
?
5-fluoroorotate + phosphoribose diphosphate
5-fluoroorotidine 5'-phosphate + diphosphate
show the reaction diagram
-
-
-
?
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
show the reaction diagram
orotidine 5-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
additional information
?
-
-
half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to the enzyme supports an alternative variant of the Theorell-Chance mechanism with alternating site catalysis, overview
-
-
?
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
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
orotidine 5'-phosphate + diphosphate
show the reaction diagram
-
-
-
-
r
orotidine 5-phosphate + diphosphate
orotate + 5-phospho-alpha-D-ribose 1-diphosphate
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
Mg2+-dependent activity
Ca2+
-
not activating
Co2+
-
not activating
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5-phospho-alpha-D-ribose 1-diphosphate
-
phosphorolysis, product inhibition, kinetics
anthranilate
-
weak
arabinose 5-phosphate
-
at higher concentrations
Co2+
-
inhibits Mg2+-activation
diphosphate
-
product inhibition, kinetics
EDTA
-
5 mM, complete inhibition
erythrose 4-phosphate
-
at higher concentrations
fructose 1-phosphate
-
at higher concentrations
fructose 6-phosphate
-
at higher concentrations
nicotinate
-
weak
Orotate
-
phosphorolysis, product inhibition, kinetics
orotidylate
phosphate
-
at higher concentrations
ribose 5-phosphate
-
at higher concentrations
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041 - 0.12
5-phospho-alpha-D-ribose 1-diphosphate
0.004 - 0.01
orotidine 5'-phosphate
0.038 - 0.062
5-phospho-alpha-D-ribose 1-diphosphate
0.096 - 0.25
diphosphate
0.027 - 0.035
Orotate
0.008 - 0.0083
orotidine 5'-phosphate
additional information
additional information
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.042
5-phospho-alpha-D-ribose 1-diphosphate
-
-
0.131
diphosphate
-
-
0.063
Orotate
-
-
0.0063 - 0.01
orotydilate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
wild type enzyme
45
-
in the absence of added OMP-decarboxylase, EC 4.1.1.23
65
-
in the presence of added OMP-decarboxylase, EC 4.1.1.23
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20000
-
2 * 20000, SDS-PAGE
39000
-
gel filtration
40000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
x-ray crystallography
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapour diffusion method, the apoenzyme is crystallized in 100 mM Tris-HCl, pH 7.4, 0.2 M magnesium acetate, and 26% (w/v) PEG 6000, crystals of OPRTase in complex with substrates (5.0 mM 5-phospho-alpha-D-ribose 1-diphosphate and 5.0 mM orotate) or product (5.0 mM orotidine 5'-phosphate) are grown in 100 mM sodium acetate, pH 4.6, 0.14 M ammonium acetate, and 38% (w/v) PEG 4000, crystals of the OMP complex are grown from solutions containing 100 mM Tris HCl, pH 7.4, 0.08 M magnesium acetate, and 28% (w/v) PEG 6000
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D131A
severly reduced activity
D131A/D132A
severly reduced activity
D132A
severly reduced activity
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 9.5
-
at least 6 months stable, -20°C
489715
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, pH 7.5-9.5, at least 6 months
-
-76°C, at least 6 months
-
4°C, gradual loss of activity at pH 7.5-9.5
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Co2+), His-tag cleavage (TEV protease), immobilized metal ion affinity chromatography (Co2+)
-
partial, affinity chromatography on Blue-Dextran- or Cibacron Blue F3GA-Sepharose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
mutants are expressed in Escherichia coli strain CS101-4UI
His-tagged protein expressed in Escherichia coli BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Yoshimoto, A.; Amaya, T.; Kobayashi, K.; Tomita, K.
Orotate phosphoribosyltransferase (yeast)
Methods Enzymol.
51
69-74
1978
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Victor, J.; Leo-Mensah, A.; Sloan, D.L.
Divalent metal ion activation of the yeast orotate phosphoribosyltransferase catalyzed reaction
Biochemistry
18
3597-3604
1979
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Reyes, P.; Sandquist, R.B.
Purification of orotate phosphoribosyltransferase and orotidylate decarboxylase by affinity chromatography on Sepharose dye derivatives
Anal. Biochem.
88
522-531
1978
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Victor, J.; Greenberg, L.B.; Sloan, D.L.
Studies of the kinetic mechanism of orotate phosphoribosyltransferase from yeast
J. Biol. Chem.
254
2647-2655
1979
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Witte, J.F.; Tsou, R.; McClard, R.W.
Cloning, overproduction, and purification of native and mutant recombinant yeast orotate phosphoribosyltransferase and the demonstration from magnetization inversion transfer that a proposed oxocarbocation intermediate does not have a kinetic lifetime
Arch. Biochem. Biophys.
361
106-112
1999
Saccharomyces cerevisiae
Manually annotated by BRENDA team
McClard, R.W.; Holets, E.A.; MacKinnon, A.L.; Witte, J.F.
Half-of-sites binding of orotidine 5-phosphate and alpha-D-5-phosphorylribose 1-diphosphate to orotate phosphoribosyltransferase from Saccharomyces cerevisiae supports a novel variant of the Theorell-Chance mechanism with alternating site catalysis
Biochemistry
45
5330-5342
2006
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Gonzalez-Segura, L.; Witte, J.F.; McClard, R.W.; Hurley, T.D.
Ternary complex formation and induced asymmetry in orotate phosphoribosyltransferase
Biochemistry
46
14075-14086
2007
Saccharomyces cerevisiae (P13298), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Hansen, M.; Harris, R.; Barr, E.; Cheng, H.; Girvin, M.; Grubmeyer, C.
Backbone 1H, 13C, 15N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate
Biomol. NMR Assign.
8
103-108
2014
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Subrahmanyeswara Rao, N.; Deshpande, P.
An organism-independent unified model for activity of orotate phosphoribosyltransferases for orotidine monophosphate synthesis
Chem. Eng. Sci.
128
109-118
2015
Saccharomyces cerevisiae, Mycobacterium tuberculosis, Plasmodium falciparum, Salmonella enterica subsp. enterica serovar Typhimurium
-
Manually annotated by BRENDA team