Information on EC 2.4.99.19 - undecaprenyl-diphosphooligosaccharide-protein glycotransferase and Organism(s) Campylobacter lari and UniProt Accession B9KDD4

for references in articles please use BRENDA:EC2.4.99.19
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IUBMB Comments
A bacterial enzyme that has been isolated from Campylobacter jejuni and Campylobacter lari . It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
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This record set is specific for:
Campylobacter lari
UNIPROT: B9KDD4
Word Map
The taxonomic range for the selected organisms is: Campylobacter lari
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
bacterial oligosaccharyltransferase, bacterial OST, N-oligosaccharyltransferase, N-OTase, oligosaccharyl transferase, oligosaccharyltransferase, oligosacharyltransferase, OST, OT, OTase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bacterial oligosaccharyltransferase
297814
-
bacterial OST
297814
-
OTase
297813
-
PglB protein
297814
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
tritrans,heptacis-undecaprenyl-diphosphooligosaccharide:protein-L-asparagine N-beta-D-oligosaccharidotransferase
A bacterial enzyme that has been isolated from Campylobacter jejuni [1] and Campylobacter lari [2]. It forms a glycoprotein by the transfer of a glucosyl-N-acetylgalactosaminyl-N,N'-diacetylbacillosamine (GalNAc2(Glc)GalNAc3diNAcBac) polysaccharide and related oligosaccharides to the side-chain of an L-asparagine residue in the sequence -Asp/Glu-Xaa-Asn-Xaa'-Ser/Thr- (Xaa and Xaa' not Pro) in nascent polypeptide chains. Requires Mn2+ or Mg2+. Occurs on the external face of the plasma membrane. The polyprenol involved is normally tritrans,heptacis-undecaprenol but a decaprenol is used by some species.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
show the reaction diagram
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
show the reaction diagram
additional information
?
-
-
PglBCl is able to transfer Man3GlcNAc2 to extended sites but not to minimal glycosylation sites in engineered or eukaryotic target proteins
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
show the reaction diagram
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
show the reaction diagram
-
-
a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
the physiological cation is Mn2+, but PglB is also active with Mg2+
Mn2+
the physiological cation is Mn2+, but PglB is also active with Mg2+
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
transmembrane protein
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
asparagine-linked glycosylation (N-linked glycosylation) is an essential and highly conserved post-translational protein modification. This modification is essential for specific molecular recognition, protein folding, sorting in the endoplasmic reticulum, cell-cell communication, and stability
additional information
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
functional PglB is partially autoglycosylated at N535 and N556
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PglB in complex with acceptor hexapeptide DQNATF, X-ray diffraction structure determination and analysis at 3.4 A resolution, molecular replacement using the periplasmic domain of Campylobacter jejuni PglB, PDB ID 3AAG, as model
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D154A
the mutation reduces the observed glycosylation yield by over 50% compared to the wild-type enzyme
D56A
the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme
D56A/E319A
the double mutant is inactive
E319A
the mutation reduces the observed glycosylation yield by over 90% compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His10-tagged wild-type and mutant enzymes from Escherichia coli strain SCM6
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene pglB, expression of His10-tagged wild-type and mutant enzymes in Escherichia coli strain SCM6
gene pglB, expressio of the enzyme and the modified substrates in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Valderrama-Rincon, J.D.; Fisher, A.C.; Merritt, J.H.; Fan, Y.Y.; Reading, C.A.; Chhiba, K.; Heiss, C.; Azadi, P.; Aebi, M.; DeLisa, M.P.
An engineered eukaryotic protein glycosylation pathway in Escherichia coli
Nat. Chem. Biol.
8
434-436
2012
Campylobacter jejuni, Campylobacter lari
Manually annotated by BRENDA team
Lizak, C.; Gerber, S.; Numao, S.; Aebi, M.; Locher, K.
X-ray structure of a bacterial oligosaccharyltransferase
Nature
474
350-356
2011
Campylobacter jejuni, Campylobacter lari (B9KDD4), Campylobacter lari
Manually annotated by BRENDA team
Mohanty, S.; Chaudhary, B.P.; Zoetewey, D.
Structural insight into the mechanism of N-linked glycosylation by oligosaccharyltransferase
Biomolecules
10
624
2020
Campylobacter lari (B9KDD4), Campylobacter lari RM2100 (B9KDD4)
Manually annotated by BRENDA team
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