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Information on EC 2.4.1.270 - mannosylglucosyl-3-phosphoglycerate synthase
for references in articles please use BRENDA:EC2.4.1.270
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.270 mannosylglucosyl-3-phosphoglycerate synthase
IUBMB Comments
The enzyme is involved in synthesis of 2-[2-O-(α-D-mannopranosyl)-α-D-glucopyranosyl]-D-glycerate. Petrotoga miotherma and Petrotoga mobilis accumulate this compound in response to water stress imposed by salt.
The enzyme appears in viruses and cellular organisms
Reaction Schemes
showSynonyms
mannosylglucosyl-3-phosphoglycerate synthase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MggA
RB5546
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate = GDP + 2-O-[2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl]-3-phospho-D-glycerate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
mannosylglucosylglycerate biosynthesis I
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SYSTEMATIC NAME
IUBMB Comments
GDP-mannose:2-O-(alpha-D-glucosyl)-3-phospho-D-glycerate 2-O-alpha-D-mannosyltransferase
The enzyme is involved in synthesis of 2-[2-O-(alpha-D-mannopranosyl)-alpha-D-glucopyranosyl]-D-glycerate. Petrotoga miotherma and Petrotoga mobilis accumulate this compound in response to water stress imposed by salt.
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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-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ADP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
UDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
UDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ADP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ADP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: -
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ADP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
ADP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: -
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GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of the rare solute mannosylglucosylglycerate are proposed. The first one is a a phosphorylating pathway (with a phosphorylated intermediate) from 3-phosphoglycerate and UDP-glucose to the final solute. The second nonphosphorylating pathway (no phosphorylated intermediates) could represent an alternative route for the synthesis of mannosylglucosylglycerate in Petrotoga mobilis that could lead to the direct conversion of glucosylglycerate and GDP-mannose to mannosylglucosylglycerate. Pathway multiplicity likely reflects a crucial role for mannosylglucosylglycerate in the physiology of Petrotoga mobilis mobilis during stress adaptation
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GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: no activity with UDP-mannose or mannose-1-phosphate as sugar donors, and 3-phospho-D-glycerate, 2-alpha-D-glucosylglycerate, and glucosyl-3-phosphoglycerate as the sugar acceptors
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GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: -
Products: -
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GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: -
Products: -
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UDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
UDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: -
Products: -
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UDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
UDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: -
Products: -
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additional information
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Substrates: enzyme is non-specific for the mannosyl-donor, using GDP-mannose, UDP-mannose and ADP-mannose as substrates with decreasing affinity. From the tested substrates only 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate is used as mannosyl-acceptor. The enzyme is a configuration retaining sugar transferase
Products: -
Products: -
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additional information
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Substrates: enzyme is non-specific for the mannosyl-donor, using GDP-mannose, UDP-mannose and ADP-mannose as substrates with decreasing affinity. From the tested substrates only 2-(O-alpha-D-glucopyranosyl)-3-phospho-D-glycerate is used as mannosyl-acceptor. The enzyme is a configuration retaining sugar transferase
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
GDP-mannose + 2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
GDP + 2-(2-O-(alpha-D-mannopyranosyl)-alpha-D-glucopyranosyl)-3-phospho-D-glycerate
Substrates: the enzyme is involved in the phosphorylating pathway for synthesis of the solute mannosylglucosylglycerate. In Petrotoga mobilis two alternative pathways for the synthesis of the rare solute mannosylglucosylglycerate are proposed. The first one is a a phosphorylating pathway (with a phosphorylated intermediate) from 3-phosphoglycerate and UDP-glucose to the final solute. The second nonphosphorylating pathway (no phosphorylated intermediates) could represent an alternative route for the synthesis of mannosylglucosylglycerate in Petrotoga mobilis that could lead to the direct conversion of glucosylglycerate and GDP-mannose to mannosylglucosylglycerate. Pathway multiplicity likely reflects a crucial role for mannosylglucosylglycerate in the physiology of Petrotoga mobilis mobilis during stress adaptation
Products: -
Products: -
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency
Mn2+
Ca2+
not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency
Co2+
not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency
Mn2+
not strictly dependent on divalent cations, but the presence of 1 mM Mn2+, Ca2+, Mg2+, or Co2+ stimulates its activity in this order of efficiency
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
EDTA
in the presence of 0.1, 2.0, or 5.0 mM EDTA, the enzyme retaines 85, 30, and 23% of its maximal activity, respectively
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.41
2-O-(alpha-D-glucopyranosyl)-3-phospho-D-glycerate
pH 7.5, 25°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 10
pH 6.0: about 50% of maximal activity, pH 10.0: about 75% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60 - 95
60°C: about 50% of maximal activity, 95°C: about 70% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
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.
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). MGGA_PETMO
Petrotoga mobilis (strain DSM 10674 / SJ95)
505
0
59124
Swiss-Prot
other Location (Reliability: 1)
Q7URP0_RHOBA
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
530
0
59732
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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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
expression in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fernandes, C.; Mendes, V.; Costa, J.; Empadinhas, N.; Jorge, C.; Lamosa, P.; Santos, H.; da Costa, M.S.
Two alternative pathways for the synthesis of the rare compatible solute mannosylglucosylglycerate in Petrotoga mobilis
J. Bacteriol.
192
1624-1633
2010
Petrotoga mobilis (A9BHJ0), Petrotoga mobilis
brenda
Cunha, S.; dAvo, A.F.; Mingote, A.; Lamosa, P.; da Costa, M.S.; Costa, J.
Mannosylglucosylglycerate biosynthesis in the deep-branching phylum Planctomycetes: characterization of the uncommon enzymes from Rhodopirellula baltica
Sci. Rep.
3
2378
2013
Rhodopirellula baltica (Q7URP0), Rhodopirellula baltica DSM 10527 (Q7URP0)
brenda
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