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Information on EC 2.4.1.213 - glucosylglycerol-phosphate synthase
for references in articles please use BRENDA:EC2.4.1.213
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.213 glucosylglycerol-phosphate synthase
IUBMB Comments
Acts with EC 3.1.3.69 (glucosylglycerol phosphatase) to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.4.1.213
- synechocystis
- cyanobacterium
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acclimation
- trehalose
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osmolyte
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freshwater
- rhizophila
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redirect
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stenotrophomonas
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osmoprotectant
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salt-regulated
Synonyms
glucosylglycerol-phosphate synthase, gg-phosphate synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GG-phosphate synthase
GGPPS
GGPS
Glucosyl-glycerol-phosphate synthase
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glucosylglycerol-phosphate synthase/phosphatase
GG-phosphate synthase
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GGPS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ADP-alpha-D-glucose + sn-glycerol 3-phosphate = 2-(alpha-D-glucopyranosyl)-sn-glycerol 3-phosphate + ADP
acts with EC 3.1.3.69: glucosylglycerol phosphatase to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
MetaCyc
glucosylglycerol biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
ADP-alpha-D-glucose:sn-glycerol-3-phosphate 2-alpha-D-glucopyranosyltransferase
Acts with EC 3.1.3.69 (glucosylglycerol phosphatase) to form glucosylglycerol, an osmolyte that endows cyanobacteria with resistance to salt.
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CAS REGISTRY NUMBER
COMMENTARY
161515-13-5
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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
ADP-alpha-D-glucose + sn-glycerol 3-phosphate
2-(alpha-D-glucopyranosyl)-sn-glycerol 3-phosphate + ADP
Substrates: -
Products: -
Products: -
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ADP-glucose + sn-glycerol 3-phosphate
2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP
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Substrates: -
Products: -
Products: -
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ADP-glucose + sn-glycerol 3-phosphate
2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP
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Substrates: -
Products: -
Products: -
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ADP-glucose + sn-glycerol 3-phosphate
2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP
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Substrates: -
Products: -
Products: -
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ADP-glucose + sn-glycerol 3-phosphate
2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP
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Substrates: reaction of second order
Products: -
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UDP-glucose + sn-glycerol 3-phosphate
2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + UDP
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Substrates: the combined enzyme glucosylglycerol-phosphate synthase/phosphatase prefers UDP-glucose compared to ADP-glucose
Products: -
Products: -
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UDP-glucose + sn-glycerol 3-phosphate
2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + UDP
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Substrates: the combined enzyme glucosylglycerol-phosphate synthase/phosphatase prefers UDP-glucose compared to ADP-glucose
Products: -
Products: -
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additional information
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Substrates: the rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol and trehalose under salt stress conditions, overview
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additional information
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Substrates: the rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol and trehalose under salt stress conditions, overview
Products: -
Products: -
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additional information
?
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Substrates: a truncated enzyme version, devoid of the phosphatase part, synthesizes glucosylglycerol-phosphate, in contrast to the full-length wild-type enzyme, that synthesizes glucosylglycerol. The complete GgpPS protein also catalyzes dephosphorylation of glucosylglycerol phosphate, overview
Products: -
Products: -
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additional information
?
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Substrates: a truncated enzyme version, devoid of the phosphatase part, synthesizes glucosylglycerol-phosphate, in contrast to the full-length wild-type enzyme, that synthesizes glucosylglycerol. The complete GgpPS protein also catalyzes dephosphorylation of glucosylglycerol phosphate, overview
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
ADP-alpha-D-glucose + sn-glycerol 3-phosphate
2-(alpha-D-glucopyranosyl)-sn-glycerol 3-phosphate + ADP
Substrates: -
Products: -
Products: -
?
ADP-glucose + sn-glycerol 3-phosphate
2-(beta-D-glucosyl)-sn-glycerol 3-phosphate + ADP
-
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: the rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol and trehalose under salt stress conditions, overview
Products: -
Products: -
?
additional information
?
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Substrates: the rhizobacterium Stenotrophomonas rhizophila accumulates the compatible solutes glucosylglycerol and trehalose under salt stress conditions, overview
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Nucleic acids
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GgpS is inhibited by nucleic acids in a sequence- and length-independent manner in vitro and in vivo, it binds DNA, RNA, and heparin via a salt-dependent electrostatic interaction with the negatively charged backbone of the polyanions. Non-competitive inhibition. The inhibition is completely abolished by 20 mM NaCl
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
gene ggpPS is induced by salt shock
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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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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from freshwater lake Chad in Nigeria, gene ggpS
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brenda
TT-1 and YK-1 strains isolated from freshwater and brackish lakes in Myanmar and Nigeria, gene ggpS
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brenda
several strains isolated from freshwater and brackish lakes in Japan and Russia, gene ggpS
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brenda
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
physiological function
metabolism
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GgpS is the key enzyme of the glucosylglycerol pathway The intermediate is dephosphorylated by the second enzyme of the pathway, the glucosylglycerol-phosphate phosphatase, GgpP
metabolism
the enzyme is synthesized at a basal level under low salt conditions. It is largely inactive and is activated after a salt shock. Since the recombinant enzyme purified from Escherichia coli has NaCl-independent activity, it is concluded that an inhibitor bound to GgpS is removed by NaCl in vivo
physiological function
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the moderately halotolerant cyanobacterium Synechocystis sp. PCC 6803 synthesizes glucosylglycerol as a compatible solute. Mechanism of activity regulation by the nonspecific salt-dependent binding of an enzyme to nucleic acids, overview
physiological function
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the strains possess a GgpS-based osmoprotective mechanism
physiological function
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the strains possess a GgpS-based osmoprotective mechanism
physiological function
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the strains possess a GgpS-based osmoprotective mechanism except for strains from freshwater
physiological function
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the strains possess a GgpS-based osmoprotective mechanism
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Show AA Sequence and Transmembrane Helices (329 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme shows a C-terminal GG-phosphate synthase domain and an N-terminal putative GG-phosphate phosphatase domain
additional information
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the enzyme shows a C-terminal GG-phosphate synthase domain and an N-terminal putative GG-phosphate phosphatase domain
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of a truncated enzyme version devoid of the phosphatase part, which synthesizes glucosylglycerol-phosphate, in contrast to the full-length protein, that synthesizes glucosylglycerol, dephosphorylation of glucosylglycerol phosphate is detected only with the complete GgpPS protein, overview. Expression of the full-length ggpPS gene leads to complementation of the salt-sensitive phenotype of the mutant defective in the phosphatase step showing a severe drop in salt resistance because of the toxic effect of glucosylglycerol phosphate accumulation
additional information
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construction of a truncated enzyme version devoid of the phosphatase part, which synthesizes glucosylglycerol-phosphate, in contrast to the full-length protein, that synthesizes glucosylglycerol, dephosphorylation of glucosylglycerol phosphate is detected only with the complete GgpPS protein, overview. Expression of the full-length ggpPS gene leads to complementation of the salt-sensitive phenotype of the mutant defective in the phosphatase step showing a severe drop in salt resistance because of the toxic effect of glucosylglycerol phosphate accumulation
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and truncated mutant enzymes from Escherichia coli strain LMG194 by nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene ggpPS, DNA and amino acid sequence determination and analysis, expression of His-tagged wild-type and truncated mutant enzymes in Escherichia coli strain LMG194, complementation of the glucosylglycerol-defective mutants of the cyanobacterium Synechocystis sp. strain PCC 6803
gene ggpS, DNA and amino acid sequence determination and analysis, phylogenetic analysis
plasmid-bound expression of ggpS and ggpP from Synechocystis sp. PCC 6803 enables synthesis of alpha-D-glucosylglycerol exclusively in osmotically stressed cells of Corynebacterium glutamicum (pEKEx2-ggpSP), which is probably due to the unique intrinsic control mechanism of GG-phosphate synthase activity in response to intracellular ion concentrations
gene ggpS, DNA and amino acid sequence determination and analysis, phylogenetic analysis
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gene ggpS, DNA and amino acid sequence determination and analysis, phylogenetic analysis
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gene ggpS, DNA and amino acid sequence determination and analysis, phylogenetic analysis
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ggpS mRNA shows a salt-dependent accumulation that roughly follows the kinetics of the intracellular salt ion concentrations in response to salt shocks. The induction of ggpS expression involves several regulatory components in Synechocystis
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hagemann, M.; Erdmann, N.
Activation and pathway of glucosylglycerol biosynthesis in the cyanobacterium Synechocystis sp. PCC 6803
Microbiology
140
1427-1431
1994
Synechocystis sp.
-
brenda
Marin, K.; Zuther, E.; Kerstan, T.; Kunert, A.; Hagemann, M.
The ggpS gene from Synechocystis sp. strain PCC 6803 encoding glucosylglycerol-phosphate synthase is involved in osmolyte synthesis
J. Bacteriol.
180
4843-4849
1998
Synechocystis sp.
brenda
Schoor, A.; Hagemann, M.; Erdmann, N.
Glucosylglycerol-phosphate synthase: target for ion-mediated regulation of osmolyte synthesis in the cyanobacterium Synechocystis sp. strain PCC 6803
Arch. Microbiol.
171
101-106
1999
Synechocystis sp.
brenda
Hagemann, M.; Effmert, U.; Kerstan, T.; Schoor, A.; Erdmann, N.
Biochemical characterization of glucosylglycerol-phosphate synthase of Synechocystis sp. strain PCC 6803: Comparison of crude, purified, and recombinant enzymes
Curr. Microbiol.
43
278-283
2001
Synechocystis sp.
brenda
Marin, K.; Huckauf, J.; Fulda, S.; Hagemann, M.
Salt-dependent expression of glucosylglycerol-phosphate synthase, involved in osmolyte synthesis in the cyanobacterium synechocystis sp. strain PCC 6803
J. Bacteriol.
184
2870-2877
2002
Synechocystis sp.
brenda
Hagemann, M.; Ribbeck-Busch, K.; Klaehn, S.; Hasse, D.; Steinbruch, R.; Berg, G.
The plant-associated bacterium Stenotrophomonas rhizophila expresses a new enzyme for the synthesis of the compatible solute glucosylglycerol
J. Bacteriol.
190
5898-5906
2008
Stenotrophomonas rhizophila (Q5GMP2), Stenotrophomonas rhizophila
brenda
Klaehn, S.; Marquardt, D.M.; Rollwitz, I.; Hagemann, M.
Expression of the ggpPS gene for glucosylglycerol biosynthesis from Azotobacter vinelandii improves the salt tolerance of Arabidopsis thaliana
J. Exp. Bot.
60
1679-1689
2009
Azotobacter vinelandii, Azotobacter vinelandii AvOP
brenda
Yoshikawa, T.; Ikeda, Y.; Sakata, T.; Maeda, H.
Cloning and analysis of the ggpS gene from cyanobacteria Arthrospira spp. involved in the synthesis of an osmolyte glucosylglycerol
Biocontrol. Sci.
16
55-61
2011
Arthrospira platensis, Arthrospira platensis NIES-39, Arthrospira sp., Synechocystis sp.
brenda
Novak, J.F.; Stirnberg, M.; Roenneke, B.; Marin, K.
A novel mechanism of osmosensing, a salt-dependent protein-nucleic acid interaction in the cyanobacterium Synechocystis species PCC 6803
J. Biol. Chem.
286
3235-3241
2011
Synechocystis sp.
brenda
Roenneke, B.; Rosenfeldt, N.; Derya, S.M.; Novak, J.F.; Marin, K.; Kraemer, R.; Seibold, G.M.
Production of the compatible solute alpha-D-glucosylglycerol by metabolically engineered Corynebacterium glutamicum
Microb. Cell Fact.
17
94
2018
Synechocystis sp. PCC 6803 (P74258)
brenda
Kirsch, F.; Klaehn, S.; Hagemann, M.
Salt-regulated accumulation of the compatible solutes sucrose and glucosylglycerol in cyanobacteria and its biotechnological potential
Front. Microbiol.
10
2139
2019
Synechocystis sp. PCC 6803 (P74258)
brenda
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