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IUBMB Comments This archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The enzyme is activated by cAMP .
The enzyme appears in viruses and cellular organisms
Synonyms
r15pi, ph0208, r15p isomerase, ribulose 1,5-bisphosphate synthase,
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ribulose 1,5-bisphosphate synthase
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PH0208
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R15P isomerase
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R15Pi
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alpha-D-ribose 1,5-bisphosphate = D-ribulose 1,5-bisphosphate
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alpha-D-ribose 1,5-bisphosphate aldose-ketose-isomerase
This archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes. The enzyme is activated by cAMP [2].
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alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
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r
alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
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alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
the archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes
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alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
the enzyme is involved in archaeal AMP degradation pathway
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alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
the enzyme is specific for the alpha-anomer of D-ribose 1,5-bisphosphate
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alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
the enzyme is specific for the alpha-anomer of D-ribose 1,5-bisphosphate and does not recognize other sugar compounds (ribose 5-phosphate, phosphoribosylpyrophosphate, fructose 1,6-bisphosphate, fructose 6-phosphate, glucose, pyruvate or 3-phosphoglycerate)
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alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
the archaeal enzyme is involved in AMP metabolism and CO2 fixation through type III RubisCO enzymes
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alpha-D-ribose 1,5-bisphosphate
D-ribulose 1,5-bisphosphate
the enzyme is involved in archaeal AMP degradation pathway
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AMP
activity is extremely low with the substrate alpha-D-ribose 1,5-bisphosphate alone but is more than 40fold activated in the presence of AMP
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AMP
presence of AMP provides structural stability to the protein
AMP
elevates the catalytic efficiency of the enzyme. The binding site of AMP in the enzyme is reported
GMP
GMP binds to the AMP binding site and an additional binding site
GMP
elevates the catalytic efficiency of the enzyme to a lower degree than AMP. The binding site of AMP in the enzyme is reported
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0.6
alpha-D-ribose 1,5-bisphosphate
pH 8.3, 85°C
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29.2
alpha-D-ribose 1,5-bisphosphate
pH 8.3, 85°C
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48.7
alpha-D-ribose 1,5-bisphosphate
pH 8.3, 85°C
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29.3
pH 8.0, 85°C, wild-type enzyme
32.3
85°C, pH not specified in the publication
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UniProt
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UniProt
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SwissProt
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SwissProt
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Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Methanotorris igneus (strain DSM 5666 / JCM 11834 / Kol 5)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
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in silico analysis of conserved residues and molecular modeling of structure. Protein PH0208 comprises the residues required for ribose-1,5-bisphosphate activity and the residues reuired for dimerization
wild-type and mutants C135S and D204N, in complex with AMP and with GMP
crystals are obtained in hanging-drop vapor-diffusion method at 20°C within a period of 2-7 days
sitting drop vapor diffusion method at 20°C. Crystal structure of unliganded Tk-R15Pi is solved by means of the single-wavelength anomalous dispersion method using SeMet-substituted enzyme and refined at 2.5 A resolution
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C135S
mutation of catalytic residue, inhibits binding of substrate ribose 1,5-bisphosphate. Mutation does not not alter the binding behavior of AMP to the protein
D204N
mutation of catalytic residue. Mutation does not not alter the binding behavior of AMP to the protein
C135S
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mutation of catalytic residue, inhibits binding of substrate ribose 1,5-bisphosphate. Mutation does not not alter the binding behavior of AMP to the protein
D204N
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mutation of catalytic residue. Mutation does not not alter the binding behavior of AMP to the protein
C133A
inactive mutant enzyme
C133S
inactive mutant enzyme
D202N
inactive mutant enzyme
R227R
mutant enzyme exhibits a decrease in molecular size of the enzyme and significantly decreases the enzymatic activity
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the AMP binding site in PH0208 protein clarifies the role of AMP in providing structural stability to the enzyme. The binding of GMP to the AMP binding site in addition to its own binding site indicates that GMP might also execute a similar function, though with less specificity
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expression in Escherichia coli
expression in Rosetta (DE3) Escherichia coli cells
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increased protein levels of the ribose 1,5-bisphosphate isomerase in the cells cultivated with nucleosides
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Aono, R.; Sato, T.; Yano, A.; Yoshida, S.; Nishitani, Y.; Miki, K.; Imanaka, T.; Atomi, H.
Enzymatic characterization of AMP phosphorylase and ribose-1,5-bisphosphate isomerase functioning in an archaeal AMP metabolic pathway
J. Bacteriol.
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6847-6855
2012
Thermococcus kodakarensis (Q5JFM9), Thermococcus kodakarensis
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Sato, T.; Atomi, H.; Imanaka, T.
Archaeal type III RuBisCOs function in a pathway for AMP metabolism
Science
315
1003-1006
2007
Thermococcus kodakarensis (Q5JFM9)
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Nakamura, A.; Fujihashi, M.; Aono, R.; Sato, T.; Nishiba, Y.; Yoshida, S.; Yano, A.; Atomi, H.; Imanaka, T.; Miki, K.
Dynamic, ligand-dependent conformational change triggers reaction of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1
J. Biol. Chem.
287
20784-20796
2012
Thermococcus kodakarensis (Q5JFM9)
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Gogoi, P.; Srivastava, A.; Jayaprakash, P.; Jeyakanthan, J.; Kanaujia, S.P.
In silico analysis suggests that PH0702 and PH0208 encode for methylthioribose-1-phosphate isomerase and ribose-1,5-bisphosphate isomerase, respectively, rather than aIF2Bbeta and aIF2Bdelta
Gene
575
118-126
2016
Pyrococcus horikoshii (O57947), Pyrococcus horikoshii, Pyrococcus horikoshii DSM 12428 (O57947)
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Gogoi, P.; Kanaujia, S.
A presumed homologue of the regulatory subunits of eIF2B functions as ribose-1,5-bisphosphate isomerase in Pyrococcus horikoshii OT3
Sci. Rep.
8
1891
2018
Pyrococcus horikoshii OT3 (O57947), Pyrococcus horikoshii OT3, Pyrococcus horikoshii (O57947), Pyrococcus horikoshii DSM 12428 (O57947)
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5.3.1.29 ribose 1,5-bisphosphate isomerase
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