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Information on EC 2.7.8.6 - undecaprenyl-phosphate galactose phosphotransferase
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EC Tree
2.7.8.6 undecaprenyl-phosphate galactose phosphotransferaseSpecify your search results
Word Map
- 2.7.8.6
-
misfolded
-
glycans
-
man1b1
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er-associated
-
geobacillus
-
retrograde
-
rnai-mediated
-
s-layer
-
n-linked
-
alpha-1
-
2-mannosidase
-
reticulum-associated
- stearothermophilus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
udp-gal:phosphoryl-polyprenol gal-1-phosphate transferase, undecaprenyl-phosphate galactose phosphotransferase, udp-hexnac:polyprenol-p galnac-1-p transferase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
galactosephosphotransferase, poly(isoprenol) phosphate
-
-
-
-
galactosyl-P-P-undecaprenol synthetase
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-
-
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poly(isoprenol)-phosphate galactosephosphotransferase
-
-
-
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poly(isoprenyl)phosphate galactosephosphatetransferase
-
-
-
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UDP-Gal polyprenol-P transferase
UDP-Gal: phosphoryl-polyprenol Gal-1-phosphate transferase
UDP-Gal:phosphoryl-polyprenol Gal-1-phosphate transferase
UDP-HexNAc:polyprenol-P GalNAc-1-P transferase
undecaprenyl phosphate galactosyl-1-phosphate transferase
-
-
-
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WbaP
WbaPCT
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only the WbaP C-terminus (WbaPCT), from phenylalanine-258 (F258) to tyrosine-476 (Y476), is required for transferase activity
WecP
WsaP
UDP-Gal: phosphoryl-polyprenol Gal-1-phosphate transferase
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UDP-Gal: phosphoryl-polyprenol Gal-1-phosphate transferase
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UDP-Gal:phosphoryl-polyprenol Gal-1-phosphate transferase
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-
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WsaP
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the enzyme transfers in vitro a galactose-1-phosphate from UDP-galactose to endogenous phosphoryl-polyprenol
WsaP
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the enzyme transfers in vitro a galactose-1-phosphate from UDP-galactose to endogenous phosphoryl-polyprenol
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-galactose + undecaprenyl phosphate = UMP + alpha-D-galactosyl-diphosphoundecaprenol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
substituted phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
, , , , , , , ,
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SYSTEMATIC NAME
IUBMB Comments
UDP-galactose:undecaprenyl-phosphate galactose phosphotransferase
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CAS REGISTRY NUMBER
COMMENTARY
37278-29-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + undecaprenyl phosphate
UMP + alpha-D-galactosyl-diphosphoundecaprenol
UDP-D-galactose + antigen carrier lipid-phosphate
UMP + galactose-diphosphate antigen carrier lipid
Salmonella newington
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-
polyisoprenoid structure linked to sugars by a diphosphate bridge
?
UDP-D-N-acetylhexosamine + undecaprenyl phosphate
UMP + N-acetyl hexosaminyl-diphosphoundecaprenol
UDP-N-acetyl-D-galactosamine + undecaprenyl phosphate
UMP + N-acetyl-D-galactosaminyl-diphosphoundecaprenol
UDP-alpha-D-galactose + undecaprenyl phosphate
UMP + alpha-D-galactosyl-diphosphoundecaprenol
-
-
-
-
?
UDP-alpha-D-galactose + undecaprenyl phosphate
UMP + alpha-D-galactosyl-diphosphoundecaprenol
-
-
-
-
?
UDP-alpha-D-galactose + undecaprenyl phosphate
UMP + alpha-D-galactosyl-diphosphoundecaprenol
-
-
-
-
?
UDP-alpha-D-galactose + undecaprenyl phosphate
UMP + alpha-D-galactosyl-diphosphoundecaprenol
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specific activity with C55-undecaprenyl phosphate
-
-
?
UDP-D-galactose + phosphoryl-polyprenol
galactosyl-diphospho-polyprenol + CMP
glycosyltransferase activity within C-terminus of WsaP, in vitro assay: 1 h, 37°C, pH 8.5, 1 mM EDTA, 10 mM MgCl2, membrane fraction
analyses by thin-layer chromatography
-
?
UDP-D-galactose + phosphoryl-polyprenol
galactosyl-diphospho-polyprenol + CMP
glycosyltransferase activity within C-terminus of WsaP, in vitro assay: 1 h, 37°C, pH 8.5, 1 mM EDTA, 10 mM MgCl2, membrane fraction
analyses by thin-layer chromatography
-
?
UDP-D-N-acetylhexosamine + undecaprenyl phosphate
UMP + N-acetyl hexosaminyl-diphosphoundecaprenol
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-
-
-
?
UDP-D-N-acetylhexosamine + undecaprenyl phosphate
UMP + N-acetyl hexosaminyl-diphosphoundecaprenol
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-
-
-
?
UDP-galactose + phosphoryl-polyprenol
UMP + alpha-D-galactosyl-diphosphopolyprenol
-
-
-
?
UDP-galactose + phosphoryl-polyprenol
UMP + alpha-D-galactosyl-diphosphopolyprenol
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-
-
?
UDP-N-acetyl-D-galactosamine + undecaprenyl phosphate
UMP + N-acetyl-D-galactosaminyl-diphosphoundecaprenol
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-
-
-
?
UDP-N-acetyl-D-galactosamine + undecaprenyl phosphate
UMP + N-acetyl-D-galactosaminyl-diphosphoundecaprenol
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-
-
-
?
UDPgalactose + phospholipid
UMP + galactose-1-diphospho-lipid
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r
UDPgalactose + phospholipid
UMP + galactose-1-diphospho-lipid
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equilibrium constant 0.5
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r
additional information
?
-
-
the enzyme is unable to transfer N-acetyl-D-glucosamine from UDP-N-acetylglucosamine to undecaprenyl phosphate
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-
?
additional information
?
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the enzyme is unable to transfer N-acetyl-D-glucosamine from UDP-N-acetylglucosamine to undecaprenyl phosphate
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-
?
additional information
?
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initiation step in S-layer glycoprotein glycan biosynthesis
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-
?
additional information
?
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initiation step in S-layer glycoprotein glycan biosynthesis
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-
?
additional information
?
-
-
K30 antigen biosynthesis by full-length enzyme and N-terminal truncated version, membrane fraction
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-
?
additional information
?
-
K30 antigen biosynthesis by full-length enzyme and N-terminal truncated version, membrane fraction
-
-
?
additional information
?
-
-
initiation step in S-layer glycoprotein glycan biosynthesis
-
-
?
additional information
?
-
initiation step in S-layer glycoprotein glycan biosynthesis
-
-
?
additional information
?
-
-
K30 antigen biosynthesis by full-length enzyme and N-terminal truncated version, membrane fraction
-
-
?
additional information
?
-
K30 antigen biosynthesis by full-length enzyme and N-terminal truncated version, membrane fraction
-
-
?
additional information
?
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minimal activity is detected with the shorter polyisoprenyl phosphates like C10-P, C15-P, C20-P and C35-P at 0.28, 0.91, 1 and 1.8% of C55-undecaprenyl phosphate activity, respectively. C50-phosphate, however, results in 49.53% activity of C55-phosphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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initiation step in S-layer glycoprotein glycan biosynthesis
-
-
?
additional information
?
-
initiation step in S-layer glycoprotein glycan biosynthesis
-
-
?
additional information
?
-
-
initiation step in S-layer glycoprotein glycan biosynthesis
-
-
?
additional information
?
-
initiation step in S-layer glycoprotein glycan biosynthesis
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
-
without adding MgCl2, no activity can be detected. Activity is optimal at 25 mM
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dUMP
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0.13 mM: 48% inhibition, 0.37 mM: 78% inhibition, 1 mM: 87% inhibition
KCl
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KCl inhibits the enzyme domain activity, particularly at concentrations higher than 200 mM salt that result in more than 50% inhibition
NaCl
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NaCl inhibits the enzyme domain activity, particularly at concentrations higher than 200 mM salt that result in more than 50% inhibition
UDP
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0.12 mM: no inhibition, 1 mM: 40% inhibition
UMP
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0.04 mM: 56% inhibition, 0.1 mM: 76% inhibition, 0.4 mM: 93% inhibition
UTP
-
0.11 mM: 5% inhibition, 1 mM: 49% inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00055
UDP-alpha-D-galactose
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in 50 mM Tris-HCl (pH 8.5), 25 mM MgCl2, 1% (w/v) CHAPS, at 37°C
0.0785
undecaprenyl phosphate
-
in 50 mM Tris-HCl (pH 8.5), 25 mM MgCl2, 1% (w/v) CHAPS, at 37°C
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
membrane fraction, differential centrifugation, Western blot
brenda
-
membrane fraction, differential centrifugation, Western blot
-
brenda
Show AA Sequence and Transmembrane Helices (2022 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36500
theoretical and apparent for hexa-His-tagged C-terminal part (aa168-417), SDS-PAGE
41800
hexa-His-tagged full-length enzyme, SDS-PAGE/Western blot
56800
72870
theoretical for full-length with N-terminal horseradish peroxide-thioredoxin-tag and C-terminal hexa-His-tag, apparent weight slightly less in SDS-PAGE
56800
theoretical for hexa-His-tagged full-length enzyme
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, stable for at least 1 month
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from Escherichia coli BL21(DE3) Star and TOP10 membrane preparations, nickel affinity chromatography (batch method), in presence of 0.1 mM lauryldimethylamine N-oxide
Ni2+-bound chelating Sepharose column chromatography, and gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli TOP10 and BL21(DE3) Star cells, and in Salmonella enterica serovar Typhimurium
from genomic DNA, (i) in pET28a for inducible expression of entire coding sequence or C-terminal part with N-terminal hexa-His-tag and subcellular localisation in Escherichia coli BL21(DE3) Star, (ii) in pBAD-DEST49: for inducible expression with N-terminal horseradish peroxide-thioredoxin-tag and C-terminal hexa-His-tag in Escherichia coli TOP10, (iii) in pBluescript II SK(+): for complementation studies with full-length WsaP, C-terminal part (aa168-417), N-terminal part (aa1-314) or a mutant lacking the transmembrane domains (aa311-471) in Escherichia coli strain CWG466 and Salmonella enterica strain MSS2
the His6-tagged catalytic domain is expressed in Escherichia coli BL21(DE3) and C43(DE3) cells
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wright, A.; Dankert, M.; Fennessy, P.; Robbins, P.W.
Characterization of a polyisoprenoid compound functional in O-antigen biosynthesis
Proc. Natl. Acad. Sci. USA
57
1798-1803
1967
Salmonella newington
brenda
Osborn, M.J.; Tze-Yuen,R.
Biosynthesis of bacterial lipopolysaccharide. VII. Enzymatic formation of the first intermediate in biosynthesis of the O-antigen of Salmonella typhimurium
J. Biol. Chem.
243
5145-5152
1968
Citrobacter sp., Salmonella enterica subsp. enterica serovar Typhimurium, Citrobacter sp. 139
brenda
Steiner, K.; Novotny, R.; Patel, K.; Vinogradov, E.; Whitfield, C.; Valvano, M.A.; Messner, P.; Schaeffer, C.
Functional characterization of the initiation enzyme of S-layer glycoprotein glycan biosynthesis in Geobacillus stearothermophilus NRS 2004/3a
J. Bacteriol.
189
2590-2598
2007
Geobacillus stearothermophilus, Geobacillus stearothermophilus (Q7BG44), Geobacillus stearothermophilus NRS 2004/3a, Geobacillus stearothermophilus NRS 2004/3a (Q7BG44)
brenda
Patel, K.; Furlong, S.; Valvano, M.
Functional analysis of the C-terminal domain of the WbaP protein that mediates initiation of O antigen synthesis in Salmonella enterica
Glycobiology
20
1389-1401
2010
Salmonella enterica
brenda
Patel, K.; Ciepichal, E.; Swiezewska, E.; Valvano, M.
The C-terminal domain of the Salmonella enterica WbaP (UDP-galactose:Und-P galactose-1-phosphate transferase) is sufficient for catalytic activity and specificity for undecaprenyl monophosphate
Glycobiology
22
116-122
2012
Salmonella enterica
brenda
Merino, S.; Jimenez, N.; Molero, R.; Bouamama, L.; Regu, M.; Tomas, J.M.
A UDP-HexNAc:polyprenol-P GalNAc-1-P transferase (WecP) representing a new subgroup of the enzyme family
J. Bacteriol.
193
1943-1952
2011
Aeromonas hydrophila, Aeromonas hydrophila AH-3
brenda
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