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

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Campylobacter lari
UNIPROT: B9KDD4


The taxonomic range for the selected organisms is: Campylobacter lari

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.99.19
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RECOMMENDED NAME
GeneOntology No.
undecaprenyl-diphosphooligosaccharide-protein glycotransferase
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
protein N-glycosylation (bacterial)
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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.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pglB
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the catalytic pocket is located in the right-side cavity of PglB, structure, overview. Glycosylation sequon recognition and amide nitrogen activation are prerequisites for the formation of the N-glycosidic linkage, identification of catalytically important, acidic amino acid residues, aspartates D154 and D156 belonging to a DXD motif, and metal ion interacting D56 and E319, mechanism of N-linked glycosylation, overview. A hallmark of N-linked glycosylation is the requirement of a serine or threonine at the 12 position of the acceptor sequon, enzyme structure-function relationship
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
?
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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 SUBSTRATES
NATURAL PRODUCTS
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
B9KDD4
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
tritrans,heptacis-undecaprenyl diphosphooligosaccharide + [protein]-L-asparagine
tritrans,heptacis-undecaprenyl diphosphate + [protein]-L-asparagine-oligosaccharide
show the reaction diagram
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a glycoprotein with the oligosaccharide chain attached by N-beta-D-glycosyl linkage to protein L-asparagine
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?
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+
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
transmembrane protein
Manually annotated by BRENDA team
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
PglB possesses a transmembrane domain comprising residues 1-432 and a periplasmic domain comprising residues 433-712, two domains have extensive non-covalent interactions, provided mainly by the first external loop of the transmembrane domain that forms two helices parallel to the membrane plane. The central, catalytic enzyme of OST is the STT3 subunit, structure, overview
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
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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ENGINEERING
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