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Information on EC 2.4.1.315 - diglucosyl diacylglycerol synthase (1,6-linking) and Organism(s) Staphylococcus aureus and UniProt Accession Q5HH69

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EC Tree
     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.315 diglucosyl diacylglycerol synthase (1,6-linking)
IUBMB Comments
The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose . The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo . The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1'-sn-glycerol) .
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Staphylococcus aureus
UNIPROT: Q5HH69
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Word Map
The taxonomic range for the selected organisms is: Staphylococcus aureus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
mg517, ugt106b1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-diglucosyldiacylglycerol synthase
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processive diacylglycerol beta-glucosyltransferase
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processive diacylglycerol beta-glucosyltransferase
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-glucose:1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol 6-glucosyltransferase
The enzyme is found in several bacterial species. The enzyme from Bacillus subtilis is specific for glucose [1]. The enzyme from Mycoplasma genitalium can incoporate galactose with similar efficiency, but forms mainly 1,2-diacyl-diglucopyranosyl-sn-glycerol in vivo [3]. The enzyme from Staphylococcus aureus can also form glucosyl-glycero-3-phospho-(1'-sn-glycerol) [2].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
GDP-alpha-D-glucose + 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
1,2-diacyl-3-O-[alpha-D-glucopyranosyl-(1->6)-O-alpha-D-glucopyranosyl]-sn-glycerol + UDP
show the reaction diagram
GDP-glucose shows poor activity
-
-
?
UDP-alpha-D-glucose + 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol
1,2-diacyl-3-O-[alpha-D-glucopyranosyl-(1->6)-O-alpha-D-glucopyranosyl]-sn-glycerol + UDP
show the reaction diagram
-
-
-
?
UDP-alpha-D-glucose + glycero-3-phospho-(1'-sn-glycerol)
alpha-D-glucopyranosyl-glycero-3-phospho-(1'-sn-glycerol) + UDP
show the reaction diagram
-
-
-
?
additional information
?
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
localization is independent of phosphoglucomutase PgcA and hence the production of UDP-Glc
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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proteins YpfP and LtaA, involved in glycolipid production, and LtaS, required for lipoteichoic acid backbone synthesis, interact with one another. All three proteins also interact with numerous cell division and peptidoglycan synthesis proteins. Lipoteichoic acid backbone synthesis proceeds in Staphylococcus aureus at the division site in coordination with cell division, while glycolipid synthesis takes place throughout the membrane
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44000
x * 44000, SDS-PAGE, x * 44700, calculated
44700
x * 44000, SDS-PAGE, x * 44700, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 44000, SDS-PAGE, x * 44700, calculated
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Jorasch, P.; Warnecke, D.C.; Lindner, B.; Zahringer, U.; Heinz, E.
Novel processive and nonprocessive glycosyltransferases from Staphylococcus aureus and Arabidopsis thaliana synthesize glycoglycerolipids, glycophospholipids, glycosphingolipids and glycosylsterols
Eur. J. Biochem.
267
3770-3783
2000
Staphylococcus aureus (Q5HH69), Staphylococcus aureus, Staphylococcus aureus COL (Q5HH69)
Manually annotated by BRENDA team
Reichmann, N.T.; Picarra Cassona, C.; Monteiro, J.M.; Bottomley, A.L.; Corrigan, R.M.; Foster, S.J.; Pinho, M.G.; Gruendling, A.
Differential localization of LTA synthesis proteins and their interaction with the cell division machinery in Staphylococcus aureus
Mol. Microbiol.
92
273-286
2014
Staphylococcus aureus, Staphylococcus aureus Newman
Manually annotated by BRENDA team