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Information on EC 2.4.99.18 - dolichyl-diphosphooligosaccharide-protein glycotransferase
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2.4.99.18 dolichyl-diphosphooligosaccharide-protein glycotransferaseIUBMB Comments
Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram {polysacc/Dol14}). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine. Occurs on the cytosolic face of the endoplasmic reticulum. The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
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Word Map
- 2.4.99.18
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n-glycosylation
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n-linked
- glycans
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lipid-linked
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sequons
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asparagine-linked
- jejuni
- campylobacter
- dolichol
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ribophorins
- otase
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cotranslational
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bloc
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dolichol-linked
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translocon
- glc3man9glcnac2
- heptasaccharide
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s-layer
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underglycosylation
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preassembled
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mannosyltransferases
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glycoengineering
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hypoglycosylation
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hetero-oligomeric
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single-subunit
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translocon-associated
- man9glcnac2
- lari
- drug development
- biotechnology
- medicine
- n-glycoproteins
-
glycoproteomics
- pilins
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
Synonyms
oligosaccharyltransferase, oligosaccharyl transferase, oligosaccharyltransferase complex, ost3p, wbp1p, ost6p, oligosaccharide transferase, swp1p, tbstt3a, tbstt3b, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
asparagine N-glycosyltransferase
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dolichyldiphosphooligosaccharide-protein oligosaccharyltransferase
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glycosyltransferase, dolichyldiphosphooligosaccharide-protein
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glycosyltransferase, dolichylpyrophosphodiacetylchitobiose-protein
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oligomannosyltransferase
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oligosaccharide transferase
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oligosaccharyltransferase, dolichyldiphosphoryloligosaccharide-protein
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OST
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
dolichyl-diphosphooligosaccharide:protein-L-asparagine N-beta-D-oligopolysaccharidotransferase
Occurs in eukaryotes that form a glycoprotein by the transfer of a glucosyl-mannosyl-glucosamine polysaccharide to the side-chain of an L-asparagine residue in the sequence -Asn-Xaa-Ser- or -Asn-Xaa-Thr- (Xaa not Pro) in nascent polypeptide chains. The basic oligosaccharide is the tetradecasaccharide Glc3Man9GlcNAc2 (for diagram {polysacc/Dol14}). However, smaller oligosaccharides derived from it and oligosaccharides with additional monosaccharide units attached may be involved. See ref [2] for a review of N-glycoproteins in eukaryotes. Man3GlcNAc2 seems to be common for all of the oligosaccharides involved with the terminal N-acetylglucosamine linked to the protein L-asparagine. Occurs on the cytosolic face of the endoplasmic reticulum. The dolichol involved normally has 14-21 isoprenoid units with two trans double-bonds at the omega end, and the rest of the double-bonds in cis form.
CAS REGISTRY NUMBER
COMMENTARY
75302-32-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. The sequence of the lumen-oriented half of the transmembrane domain is important for the function of the Wbp1 protein
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). OSTB_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
430
0
49392
Swiss-Prot
-
PDB
SCOP
CATH
UNIPROT
ORGANISM
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
additional information
-
oligosaccharyl transferase consists of nine different subunits, all of which contain one or more predicted transmembrane segments. In yeast, five of these proteins are encoded by essential genes, Swp1p, Wbp1p, Ost2p, Ost1p and Stt3p
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
oligosaccharyl transferase consists of nine different subunits. Three of the essential gene products, Ost1p, Wbp1p, and Stt3p, are N-linked glycoproteins. The four potential N-glycosylation sites in Ost1p and the two potential N-glycosylation sites in Wbp1p are occupied in the mature proteins. None of the N-glycosylation sites in these two proteins is conserved, and no defect in growth or oligosaccharyl transferase activity is observed when the N-glycosylation sites are mutated to block N-glycosylation in either subunit. Glycan chain of the Stt3p subunit (Man8GlcNAc2) is linked only to Asn539
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
N217Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
N332Q
mutant of subunit Wbp1p, normal growth phenotype, glycosylation change detected
N336Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
N400Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
N535Q
mutant of subunit Stt3p, lethal phenotype, glycosylation change detected
N536Q
mutant of subunit Stt3p, normal growth phenotype, glycosylation change detected
N539Q
mutant of subunit Stt3p, lethal phenotype, glycosylation change detected
N540Q
mutant of subunit Stt3p, normal growth phenotype, glycosylation change detected
N60Q
N99Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
N99Q/N217Q
mutant of subunit Ost1p, normal growth phenotype, glycosylation change detected
T537A
mutant of subunit Stt3p, lethal phenotype, glycosylation change detected
T537A/N539Q
mutant of subunit Stt3p, lethal phenotype, glycosylation change detected
T537S
mutant of subunit Stt3p, normal growth phenotype, glycosylation change detected
T541A
mutant of subunit Stt3p, extremely temperature-sensitive phenotype, glycosylation change detected
T541S
mutant of subunit Stt3p, normal growth phenotype, glycosylation change detected
N60Q
mutant of subunit Stt3p, mutant of subunit Stt3p, normal growth phenotype, no glycosylation change detected
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Li, G.; Yan, Q.; Nita-Lazar, A.; Haltiwanger, R.S.; Lennarz, W.J.
Studies on the N-glycosylation of the subunits of oligosaccharyl transferase in Saccharomyces cerevisiae
J. Biol. Chem.
280
1864-1871
2005
Saccharomyces cerevisiae (P33767), Saccharomyces cerevisiae (P39007), Saccharomyces cerevisiae (P41543), Saccharomyces cerevisiae (P46964), Saccharomyces cerevisiae (P48439), Saccharomyces cerevisiae (Q02795), Saccharomyces cerevisiae (Q03723), Saccharomyces cerevisiae (Q92316), Saccharomyces cerevisiae (Q99380), Saccharomyces cerevisiae
Lennarz, W.J.
Studies on oligosaccharyl transferase in yeast
Acta Biochim. Pol.
54
673-677
2007
Saccharomyces cerevisiae (P33767), Saccharomyces cerevisiae (P41543), Saccharomyces cerevisiae (P46964), Saccharomyces cerevisiae (P48439), Saccharomyces cerevisiae (Q02795), Saccharomyces cerevisiae (Q92316), Saccharomyces cerevisiae (Q99380), Saccharomyces cerevisiae
EXTERNAL LINKS (specific for EC-Number 2.4.99.18)
Transporter Classification Database (TCDB): 9.B.142.3.17, 9.B.142.3.14, 9.B.142.3.4, 9.B.142.3.5, 9.B.142.3.3
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Release 2023.1 (January 2023)
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