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Information on EC 3.1.3.85 - glucosyl-3-phosphoglycerate phosphatase
for references in articles please use BRENDA:EC3.1.3.85
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EC Tree 3 Hydrolases
3.1 Acting on ester bonds
3.1.3 Phosphoric-monoester hydrolases
3.1.3.85 glucosyl-3-phosphoglycerate phosphatase
IUBMB Comments
The enzyme is involved in biosynthesis of 2-O-(α-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(α-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(α-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(α-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency [1,2]. Divalent metal ions (Mg2+, Mn2+ or Co2+) stimulate activity [1,2].
The expected taxonomic range for this enzyme is: Bacteria, Archaea
- 3.1.3.85
-
glucosylglycerate
- gg
-
methylglucose
- tuberculosis
- lipopolysaccharides
- d-3-phosphoglycerate
- gdp-glucose
-
anti-tuberculosis
-
5.4.2.1
-
glucosyltransferase
- marina
-
mycolic
- burtonii
-
mannosyl-3-phosphoglycerate
-
methanococcoides
Reaction Schemes
showSynonyms
glucosyl-3-phosphoglycerate phosphatase, mtbgpgp, gpgp protein, rv2419c, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GpgP
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O = 2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
glucosylglycerate biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucosyl-3-phospho-D-glycerate phosphohydrolase
The enzyme is involved in biosynthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate via the two-step pathway in which EC 2.4.1.266 (glucosyl-3-phosphoglycerate synthase) catalyses the conversion of GDP-glucose and 3-phospho-D-glycerate into 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase. In vivo the enzyme catalyses the dephosphorylation of 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate with lower efficiency [1,2]. Divalent metal ions (Mg2+, Mn2+ or Co2+) stimulate activity [1,2].
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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-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucosyl)-D-glycerate + phosphate
A9QXB5
Substrates: in Persephonella marina two pathways for synthesis of glucosylglycerate are present: 1. the single-step pathway in with glucosylglycerate synthase (Ggs) catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate in one-step from ADP-glucose and D-glycerate, and 2. the two-step pathway in which glucosyl-3-phosphoglycerate synthase (GpgS) catalyzes the conversion of NDP-glucose and D-3-phosphoglycerate into glucosyl-3-phosphoglycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
Products: -
Products: -
?
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-mannopyranosyl)-D-glycerate + phosphate
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
Substrates: -
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
-
Substrates: synthesis of the solute glucosylglycerate proceeds via a two-step pathway involving glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP)
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
-
Substrates: the Vmax/Km-value for 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate is about 2fold higher than the value for 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: -
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: -
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
A9QXB5
Substrates: the Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is 6-7fold higher than the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate, depending on assay temperature
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: synthesis of the solute glucosylglycerate proceeds via a two-step pathway involving glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP)
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: the Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is about 2fold higher than the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 30Ā°C and at 50Ā°C. The Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is similar to the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 70Ā°C and at 90Ā°C
Products: -
Products: -
?
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-mannopyranosyl)-D-glycerate + phosphate
-
Substrates: the Vmax/Km-value for 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate is about 2fold higher than the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
Products: -
Products: -
?
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-mannopyranosyl)-D-glycerate + phosphate
A9QXB5
Substrates: the Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is 6-7fold higher than the value for 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate, depending on assay temperature
Products: -
Products: -
?
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-mannopyranosyl)-D-glycerate + phosphate
Substrates: the Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is about 2fold higher than the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 30Ā°C and at 50Ā°C. The Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is similar to the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 70Ā°C and at 90Ā°C
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme has residual mutase activity but it prefers glucosyl-3-phosphoglycerate over 2-phosphoglycerate as a substrate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme has residual mutase activity but it prefers glucosyl-3-phosphoglycerate over 2-phosphoglycerate as a substrate
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme has residual mutase activity but it prefers glucosyl-3-phosphoglycerate over 2-phosphoglycerate as a substrate
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-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucosyl)-D-glycerate + phosphate
A9QXB5
Substrates: in Persephonella marina two pathways for synthesis of glucosylglycerate are present: 1. the single-step pathway in with glucosylglycerate synthase (Ggs) catalyzes the synthesis of 2-O-(alpha-D-glucopyranosyl)-D-glycerate in one-step from ADP-glucose and D-glycerate, and 2. the two-step pathway in which glucosyl-3-phosphoglycerate synthase (GpgS) catalyzes the conversion of NDP-glucose and D-3-phosphoglycerate into glucosyl-3-phosphoglycerate, which is then converted to 2-O-(alpha-D-glucopyranosyl)-D-glycerate by glucosyl-3-phosphoglycerate phosphatase (GpgP)
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
-
Substrates: synthesis of the solute glucosylglycerate proceeds via a two-step pathway involving glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP)
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: -
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: -
Products: -
Products: -
?
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate + H2O
2-O-(alpha-D-glucopyranosyl)-D-glycerate + phosphate
Substrates: synthesis of the solute glucosylglycerate proceeds via a two-step pathway involving glucosyl-3-phosphoglycerate synthase (GpgS) and glucosyl-3-phosphoglycerate phosphatase (GpgP)
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Co2+
K+
-
at 30Ā°C, GpgP retains 37% of its enzyme activity towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate and 12% activity towards 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate in a reaction mixture without cations compared to the activity with 10 mM K+ and Co2+. Potassium chloride, in the concentration range of 10 to 100 mM, stimulates enzyme activity about 40% at 50Ā°C, but only when 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate is the substrate. However, at 30Ā°C, K+ has a stimulatory effect towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate, but not with 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate as the substrate
Mg2+
Mn2+
Ni2+
-
at 50Ā°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. Mg2+ and, to a lesser extent, Ni2+ can replace Co2+
additional information
Co2+
-
at 50Ā°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. However, when 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate is the substrate, 3% activity is detected without cations, and the preferred metal ion with both substrates is Co2+ (10 mM). At 30Ā°C, GpgP retains 37% of its enzyme activity towards 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate and 12% activity towards 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate in a reaction mixture without cations compared to the activity with 10 mM K+ and Co2+
Co2+
A9QXB5
stimulates activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
Mg2+
-
at 50Ā°C, divalent cations are absolutely required for GpgP activity with 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate as the substrate. Mg2+ and, to a lesser extent, Ni2+ can replace Co2+
Mg2+
A9QXB5
0.1 mM is sufficient to promote the dephosphorylation of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate. Maximal activation of dephosphorylation of 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate at 0.1 mM Mg2+. Maximal activation of dephosphorylation of 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 10 mM Mg2+
Mn2+
-
enzyme activity is not detected with Mn2+ when 2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate is used, while Mn2+ had a strong stimulatory effect (85% of the maximal activity with Co2+) with 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate
Mn2+
A9QXB5
stimulates activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
additional information
-
Ca2+, Sr2+, Ba2+, Cu2+, and Zn2+, have no effect on GpgP activity at any concentration
additional information
A9QXB5
K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgP activity at any concentration
additional information
-
K+, Ca2+, Sr2+, Cu2+, Ba2+, and Zn2+, do not stimulate GpgP activity at any concentration
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Tuberculosis
Identification of glucosyl-3-phosphoglycerate phosphatase as a novel drug target against resistant strain of Mycobacterium tuberculosis (XDR1219) by using comparative metabolic pathway approach.
Tuberculosis
Mycobacterium tuberculosis Rv2419c, the missing glucosyl-3-phosphoglycerate phosphatase for the second step in methylglucose lipopolysaccharide biosynthesis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.08
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
pH 7.6, 30Ā°C
0.1
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
pH 7.6, 30Ā°C
0.19
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
A9QXB5
pH 7.0, 70Ā°C
0.21
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
A9QXB5
pH 7.0, 90Ā°C
0.27
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
-
pH 7.6, 50Ā°C
0.36
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
A9QXB5
pH 7.0, 70Ā°C
0.36
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
pH 7.6, 50Ā°C
0.41
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
A9QXB5
pH 7.0, 90Ā°C
0.43
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
A9QXB5
pH 7.0, 85Ā°C
0.53
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
A9QXB5
pH 7.0, 85Ā°C
0.79
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
pH 7.6, 70Ā°C
1.1
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
pH 7.6, 90Ā°C
0.11
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
pH 7.6, 30Ā°C
0.28
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
-
pH 7.6, 50Ā°C
0.37
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
pH 7.6, 50Ā°C
0.83
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
pH 7.6, 70Ā°C
0.9
2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
pH 7.6, 90Ā°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
the Vmax/Km-value for 2-O-(alpha-D-glucopyranisyl)-3-phospho-D-glycerate is about 2fold higher than the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 30Ā°C and at 50Ā°C. The Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is similat to the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 70Ā°C and at 90Ā°C
-
additional information
additional information
-
the Vmax/Km-value for 2-O-(alpha-D-glucopyranisyl)-3-phospho-D-glycerate is about 2fold higher than the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 30Ā°C and at 50Ā°C. The Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is similat to the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate at 70Ā°C and at 90Ā°C
-
additional information
additional information
-
the Vmax/Km-value for 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate is about 2fold higher than the value for 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
-
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
-
substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
6.5
6.5
-
substrate: 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
6.5
A9QXB5
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate as substrate
7
A9QXB5
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate as substrate
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9
-
pH 4.5: about 40% of maximal activity, pH 9.0: about 45% of maximal activity, substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
5.3 - 7.5
A9QXB5
pH 5.3: about 60% of maximal activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate as substrate, pH 8.5: about 35% of maximal activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate as substrate, about 80% of maximal activity with 2-O-(alpha-D-mannosyl)-3-phospho-D-glycerate as substrate
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
-
30Ā°C: about 55% of maximal activity, 70Ā°C: about 50% of maximal activity, substrate: 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
50 - 70
-
50Ā°C: about 60% of maximal activity, 70Ā°C: about 60% of maximal activity, substrate: 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate
60 - 100
A9QXB5
60Ā°C: about 30% of maximal activity with 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate as substrate, about 50% of maximal activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate as substrate, 100Ā°C: about 15% of maximal activity with 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate or 2-O-(alpha-D-mannopyranosyl)-3-phospho-D-glycerate as substrate
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
metabolism
the protein is involved in the biosynthesis of methylglucose lipopolysaccharides which regulate the biosynthesis of mycolic acid
metabolism
-
the protein is involved in the biosynthesis of methylglucose lipopolysaccharides which regulate the biosynthesis of mycolic acid
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GPGP_MYCTO
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
223
0
24174
Swiss-Prot
-
GPGP_MYCTU
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
223
0
24174
Swiss-Prot
-
GPGP_MYCVP
Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 / PYR-1)
225
0
24218
Swiss-Prot
-
GPMPP_METBU
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
272
0
30554
Swiss-Prot
-
GPMPP_PERMH
Persephonella marina (strain DSM 14350 / EX-H1)
269
0
31076
Swiss-Prot
-
A0A385ZRV1_9ACTN
196
0
20574
TrEMBL
-
I4CB67_DESTA
Desulfomonile tiedjei (strain ATCC 49306 / DSM 6799 / DCB-1)
286
0
31104
TrEMBL
-
A0A564S1V8_BIFLI
232
0
26203
TrEMBL
-
A0A3P3ZWN6_MYCHD
Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)
222
0
24303
TrEMBL
-
A0A645A9R8_9ZZZZ
203
0
22372
TrEMBL
other Location (Reliability: 3)
A0A6J5FZL7_9BURK
197
0
21962
TrEMBL
-
A0A6J4M4E9_9ACTN
235
0
25124
TrEMBL
-
A0A564S4I7_BIFLI
281
0
31362
TrEMBL
-
A0A124GZ78_9ACTN
219
0
23770
TrEMBL
-
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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
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structures of apo-, vanadate-bound, and phosphate-bound MtbGpgP are refined to 1.95 A, 2.3 A and 1.77 A, respectively. Enzyme consists of a single domain made up of a central beta-sheet flanked by alpha-helices on either side. The active site is located in a positively charged cleft situated above the central beta-sheet
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E84Q
mutant shows only 40% of catalytic activity compared to wild-type
H159A
mutation almost completely abolishes catalytic activity
L209E
mutation results in monomeric GpgP, rendering the enzyme incapable of dephosphorylation. Mutation almost completely abolishes catalytic activity
N17A
mutation almost completely abolishes catalytic activity
Q23A
mutant shows only 20% of catalytic activity compared to wild-type
R10A
mutation almost completely abolishes catalytic activity
R60A
mutation almost completely abolishes catalytic activity
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the enzyme expression is slightly down-regulated under nitrogen deficient conditions
the transcript abundance of the enzyme gene has no significant changes over those from the control condition during hyper-osmotic conditions
the enzyme expression is slightly down-regulated under nitrogen deficient conditions
-
the enzyme expression is slightly down-regulated under nitrogen deficient conditions
-
the transcript abundance of the enzyme gene has no significant changes over those from the control condition during hyper-osmotic conditions
-
the transcript abundance of the enzyme gene has no significant changes over those from the control condition during hyper-osmotic conditions
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Costa, J.; Empadinhas, N.; da Costa, M.S.
Glucosylglycerate biosynthesis in the deepest lineage of the bacteria: characterization of the thermophilic proteins GpgS and GpgP from Persephonella marina
J. Bacteriol.
189
1648-1654
2007
Persephonella marina (A9QXB5), Persephonella marina
brenda
Costa, J.; Empadinhas, N.; Goncalves, L.; Lamosa, P.; Santos, H.; da Costa, M.S.
Characterization of the biosynthetic pathway of glucosylglycerate in the archaeon Methanococcoides burtonii
J. Bacteriol.
188
1022-1030
2006
Methanococcoides burtonii, Thermus thermophilus (Q84B23), Thermus thermophilus
brenda
Zheng, Q.; Jiang, D.; Zhang, W.; Zhang, Q.; Zhao, Q.; Jin, J.; Li, X.; Yang, H.; Bartlam, M.; Shaw, N.; Zhou, W.; Rao, Z.
Mechanism of dephosphorylation of glucosyl-3-phosphoglycerate by a histidine phosphatase
J. Biol. Chem.
289
21242-21251
2014
Mycobacterium tuberculosis (P9WIC6), Mycobacterium tuberculosis
brenda
Uddin, R.; Zahra, N.; Azam, S.
Identification of glucosyl-3-phosphoglycerate phosphatase as a novel drug target against resistant strain of Mycobacterium tuberculosis (XDR1219) by using comparative metabolic pathway approach
Comput. Biol. Chem.
79
91-102
2019
Mycobacterium tuberculosis (P9WIC7), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIC7)
brenda
Ferreira, C.; Soares, A.R.; Lamosa, P.; Santos, M.A.; da Costa, M.S.
Comparison of the compatible solute pool of two slightly halophilic planctomycetes species, Gimesia maris and Rubinisphaera brasiliensis
Extremophiles
20
811-820
2016
Gimesia maris, Rubinisphaera brasiliensis
brenda
EXTERNAL LI