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Information on EC 3.1.3.70 - mannosyl-3-phosphoglycerate phosphatase
for references in articles please use BRENDA:EC3.1.3.70
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.70 mannosyl-3-phosphoglycerate phosphatase
IUBMB Comments
Requires Mg2+. The enzyme from Pyrococcus horikoshii is specific for α-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 3.1.3.70
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hyperthermophilic
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mannosylglycerate
- pyrococcus
- thermophilus
- horikoshii
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thermus
- archaeon
- d-3-phosphoglycerate
- gdp-mannose
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osmoadaptation
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operon-like
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rhodothermus
- marinus
- dehalococcoides
- c2b
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thermoadaptation
- ethenogenes
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dehalogenase
Reaction Schemes
showSynonyms
mpgp, mannosyl-3-phosphoglycerate phosphatase, mpg phosphatase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
mannosyl-3-phosphoglycerate phosphatase
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MPG phosphatase
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MPGP
phosphatase, mannosyl-3-phosphoglycerate
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-
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additional information
MPGP
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additional information
the enzyme is a member of the haloalkanoic acid dehalogenase superfamily
additional information
the enzyme is a member of the haloalkanoic acid dehalogenase superfamily. It is a metal-dependent haloalcanoic acid dehalogenase-like phosphatase, preserving the catalytic Motifs I-IV of the HAD-core domain, and classified as a Cof-type MPGP based on its C2B cap insertion module
additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
the enzyme is a member of the haloalkanoic acid dehalogenase superfamily
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additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
the enzyme is a member of the haloalkanoic acid dehalogenase superfamily. It is a metal-dependent haloalcanoic acid dehalogenase-like phosphatase, preserving the catalytic Motifs I-IV of the HAD-core domain, and classified as a Cof-type MPGP based on its C2B cap insertion module
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
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2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
in Thermus thermophilus strain HB27 MpgP the phosphoryl-transfer undergoes a concerted DNSN mechanism with assistance of proton transfer from the general acid Asp8, forming a short-lived PO3- intermediate which is attacked by a nucleophilic water molecule, structure-activity relationship analysis, overview
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O = 2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
in Thermus thermophilus strain HB27 MpgP the phosphoryl-transfer undergoes a concerted DNSN mechanism with assistance of proton transfer from the general acid Asp8, forming a short-lived PO3- intermediate which is attacked by a nucleophilic water molecule, structure-activity relationship analysis, overview
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphate bond
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PATHWAY SOURCE
PATHWAYS
MetaCyc
mannosylglycerate biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-mannosyl-3-phosphoglycerate phosphohydrolase
Requires Mg2+. The enzyme from Pyrococcus horikoshii is specific for alpha-D-mannosyl-3-phosphoglycerate and forms part of the pathway for the synthesis of mannosylglycerate.
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CAS REGISTRY NUMBER
COMMENTARY
393512-74-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-(alpha-D-glucosyl)-3-phosphoglycerate + H2O
2-(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: -
Products: -
Products: -
ir
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: the enzyme is involved in synthesis of mannosylglycerate
Products: -
Products: -
?
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: the enzyme is highjly specific for the substrate 2(alpha-D-mannosyl)-3-phosphoglycerate
Products: -
Products: -
?
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: the enzyme is involved in synthesis of mannosylglycerate
Products: -
Products: -
?
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: the enzyme is highjly specific for the substrate 2(alpha-D-mannosyl)-3-phosphoglycerate
Products: -
Products: -
?
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
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Substrates: enzyme is highly specific for D-mannosyl-3-phosphoglycerate
Products: -
Products: -
?
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
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Substrates: enzyme is involved in biosynthesis of alpha-mannosylglycerate
Products: -
Products: -
?
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: high substrate specificity, 2-O-(alpha-D-mannosyl)-3-phosphoglycerate is the only substrate dephosphorylated by the enzyme
Products: -
Products: -
?
2-O-(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2-O-(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: high substrate specificity, 2-O-(alpha-D-mannosyl)-3-phosphoglycerate is the only substrate dephosphorylated by the enzyme
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: the enzyme is involved in synthesis of mannosylglycerate
Products: -
Products: -
?
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
Substrates: the enzyme is involved in synthesis of mannosylglycerate
Products: -
Products: -
?
2(alpha-D-mannosyl)-3-phosphoglycerate + H2O
2(alpha-D-mannosyl)-D-glycerate + phosphate
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Substrates: enzyme is involved in biosynthesis of alpha-mannosylglycerate
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
activity is strictly dependent on divalent cations. Mn2+, Co2+, Mg2+, and to a lesser extent Ni2+ activate the enzyme
Mg2+
Mn2+
activity is strictly dependent on divalent cations. Mn2+, Co2+, Mg2+, and to a lesser extent Ni2+ activate the enzyme
Ni2+
activity is strictly dependent on divalent cations. Mn2+, Co2+, Mg2+, and to a lesser extent Ni2+ activate the enzyme
additional information
Mg2+
barely dependent on Mg2+. In the absence of Mg2+ the enzyme reaches 90% of that in the presence of this divalent cation
Mg2+
activity is strictly dependent on divalent cations. Mn2+, Co2+, Mg2+, and to a lesser extent Ni2+ activate the enzyme
additional information
Ca2+, Sr2+, Ba2+, Cu2+, and Zn2+, have no effect on enzyme activity at any concentration
additional information
-
Ca2+, Sr2+, Ba2+, Cu2+, and Zn2+, have no effect on enzyme activity at any concentration
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.2 - 7.5
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pH 4.2: 60% of maximal actuvity, pH 7.5: about 45% of maximal activity
5 - 7.5
pH 6.0: about 50% of maximal activity, pH 8.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 103
30°C: about 15% of maximal activity, 103°C: about 70% of maximal activity
70 - 100
70°C: about 55% of maximal activity, 100°C: about 70% of maximal activity
70 - 108
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70°C: about 45% of maximal activity, 108°C: about 20% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
metabolism
mannosyl-3-phosphoglycerate phosphatase is the enzyme involved in the second step of the two-step mannosyl-3-phosphoglycerate biosynthetic pathway, most commonly found in (hyper)thermophilic microorganisms
metabolism
the synthesis of MG via mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase, the so-called two-step pathway, is the most prevalent route among these organisms. The phosphorylated intermediate mannosyl-3-phosphoglycerate is synthesized by the first enzyme and is subsequently dephosphorylated by the second
metabolism
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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the synthesis of MG via mannosyl-3-phosphoglycerate synthase and mannosyl-3-phosphoglycerate phosphatase, the so-called two-step pathway, is the most prevalent route among these organisms. The phosphorylated intermediate mannosyl-3-phosphoglycerate is synthesized by the first enzyme and is subsequently dephosphorylated by the second
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metabolism
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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mannosyl-3-phosphoglycerate phosphatase is the enzyme involved in the second step of the two-step mannosyl-3-phosphoglycerate biosynthetic pathway, most commonly found in (hyper)thermophilic microorganisms
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physiological function
mannosyl-3-phosphoglycerate phosphatase is a key mediator in the physiological response to thermal and osmotic stresses, catalyzing the hydrolysis of mannosyl-3-phosphoglycerate into the final product, alpha-mannosylglycerate
physiological function
the enzyme is involved in synthesis of mannosylglycerate
physiological function
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
mannosyl-3-phosphoglycerate phosphatase is a key mediator in the physiological response to thermal and osmotic stresses, catalyzing the hydrolysis of mannosyl-3-phosphoglycerate into the final product, alpha-mannosylglycerate
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physiological function
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the enzyme is involved in synthesis of mannosylglycerate
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additional information
two distinct enzyme conformations, open and closed, are catalytically relevant: the apo-MpgP is prevalently found in the open state, while the holo-MpgP, in complex with the reaction products, is found in the closed state. Enzyme activation entails a structural rearrangement of Motifs I and IV with concomitant binding of the co-catalytic Mg2+ ion. The closure motion of the C2B domain is subsequently triggered by the anchoring of the phosphoryl group to the co-catalytic metal center, and by Arg167 fixing the mannosyl moiety inside the catalytic pocket
additional information
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two distinct enzyme conformations, open and closed, are catalytically relevant: the apo-MpgP is prevalently found in the open state, while the holo-MpgP, in complex with the reaction products, is found in the closed state. Enzyme activation entails a structural rearrangement of Motifs I and IV with concomitant binding of the co-catalytic Mg2+ ion. The closure motion of the C2B domain is subsequently triggered by the anchoring of the phosphoryl group to the co-catalytic metal center, and by Arg167 fixing the mannosyl moiety inside the catalytic pocket
additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
two distinct enzyme conformations, open and closed, are catalytically relevant: the apo-MpgP is prevalently found in the open state, while the holo-MpgP, in complex with the reaction products, is found in the closed state. Enzyme activation entails a structural rearrangement of Motifs I and IV with concomitant binding of the co-catalytic Mg2+ ion. The closure motion of the C2B domain is subsequently triggered by the anchoring of the phosphoryl group to the co-catalytic metal center, and by Arg167 fixing the mannosyl moiety inside the catalytic pocket
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Show AA Sequence and Transmembrane Helices (1425 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
additional information
dimer
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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2 * 28200, recombinant enzyme, SDS-PAGE
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additional information
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
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detailed structure analysis, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo enzyme form lacking magnesium ions using the multiple-wavelength anomalous diffraction method and magnesium-bound holo enzyme form using the molecular-replacement method, with 16-20% (w/v) PEG 3350, 0.2 M ammonium chloride and 0.1 M MES-NaOH pH 6.0
purified recombinant enzyme in apo-form and in complex with substrates, substrate analogues and inhibitors, sitting drop vapor diffusion technique, 10 mg/ml protein in 20 mM MES-NaOH pH 6.3, 760 mM NaCl, 5 mM DTT, 1 mM EDTA, 5 mM Mg2+ and Na/KPO4, is mixed with crystallization solution containing 0.02 M of each of the carboxylic acids, i.e. Na-formate, NH4-acetate, Na3-citrate, NaK-L-tartrate and Na-oxamate, 0.1 M MES/imidazole, pH 6.5, in a 1:1 molar ratio, and a 30% v/v precipitant mixture containing 20% v/v ethylene glycol and 10% v/v PEG 8000, 20°C, 5 days, X-ray diffraction structure determination and analysis, molecular replacement
purified recombinant enzyme, sitting drop vapour diffusion technique, 10 mg/ml in 20 mM MES-NaOH, pH 6.35, 5 mM DTT, 1 mM EDTA, 5 mM MgCl2, and 760 mM NaCl, mixed with crystallization solution containing 0.02 M of each of the carboxylic acids, i.e. Na-formate, NH4-acetate, Na3-citrate, NaK-L-tartrate and Na-oxamate, 0.1 M MES/imidazole, pH 6.5, in a 1:1 molar ratio forming 0.002 ml drops, and a 30% v/v precipitant mixture containing 20% v/v ethylene glycol and 10% v/v PEG 8000, 20°C, 5 days, X-ray diffraction structure determination and analysis at 1.90 A resolution
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, HiTrap Ni2+-chelating column chromatography, Source 15Q column chromatography, and Superdex 75 gel filtration
recombinant enzyme from Escherichia coli strain BL21 (DE3) by anion exchange and cation exchange chromatography
recombinant enzyme from Escherichia coli strain BL21 (DE3) by cation exchange chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli strain BL21 (DE3)
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Empadinhas, N.; Marugg, J.D.; Borges, N.; Santos, H.; Da Costa, M.S.
Pathway for the synthesis of mannosylglycerate in the hyperthermophilic archaeon Pyrococcus horikoshii. Biochemical and genetic characterization of key enzymes
J. Biol. Chem.
276
43580-43588
2001
Pyrococcus horikoshii
brenda
Neves, C.; da Costa, M.S.; Santos, H.
Compatible solutes of the hyperthermophile Palaeococcus ferrophilus: osmoadaptation and thermoadaptation in the order Thermococcales
Appl. Environ. Microbiol.
71
8091-8098
2005
Palaeococcus ferrophilus (Q2VPS0), Palaeococcus ferrophilus, Palaeococcus ferrophilus DSM 13482T (Q2VPS0)
brenda
Kawamura, T.; Watanabe, N.; Tanaka, I.
Structure of mannosyl-3-phosphoglycerate phosphatase from Pyrococcus horikoshii
Acta Crystallogr. Sect. D
64
1267-1276
2008
Pyrococcus horikoshii (O58690), Pyrococcus horikoshii
brenda
Goncalves, S.; Esteves, A.M.; Borges, N.; Santos, H.; Matias, P.M.
Crystallization and preliminary X-ray analysis of mannosyl-3-phosphoglycerate phosphatase from Thermus thermophilus HB27
Acta Crystallogr. Sect. F
67
390-396
2011
Thermus thermophilus (Q72K29), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72K29)
brenda
Goncalves, S.; Esteves, A.M.; Santos, H.; Borges, N.; Matias, P.M.
The three-dimensional structure of mannosyl-3-phosphoglycerate phosphatase from Thermus thermophilus HB27: a new member of the haloalkanoic acid dehalogenase superfamily
Biochemistry
50
9551-9567
2011
Thermus thermophilus (Q72K29), Thermus thermophilus, Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039 (Q72K29)
brenda
Empadinhas, N.; Albuquerque, L.; Henne, A.; Santos, H.; Da Costa, M.
The bacterium Thermus thermophilus, like hyperthermophilic archaea, uses a two-step pathway for the synthesis of mannosylglycerate
Appl. Environ. Microbiol.
69
3272-3279
2003
Thermus thermophilus (Q84B23), Thermus thermophilus, Thermus thermophilus DSM 7039 (Q84B23)
brenda
EXTERNAL LINKS (specific for EC-Number 3.1.3.70)
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