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Information on EC 2.4.1.258 - dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P38179
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2.4.1.258 dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferaseIUBMB Comments
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
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Word Map
- 2.4.1.258
-
n-glycosylation
- n-glycans
-
lipid-linked
- oligosaccharide
- glc3man9glcnac2
- glycan
- medicine
-
peptide-n-glycosidase
- synthesis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
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Synonyms
alg3p, atalg3, tbalg3, dol-p-man:man5glcnac2-pp-dol mannosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
dolichyl beta-D-mannosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-mannosyltransferase
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
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
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
GDP-alpha-D-mannose + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
GDP + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
the formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate. Alg3p is not required for elongation of D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
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-
?
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
extension does not occur when the acceptor was added as a free Man5GlcNAc2 oligosaccharide or when GDP-Man is used as mannosyl donor
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-
?
GDP-alpha-D-mannose + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
GDP + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
alg3 Man5GlcNAc2 precursor
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-
?
GDP-alpha-D-mannose + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
GDP + Manalpha(1-2)Manalpha(1-2)Manalpha(1-3)(Manalpha(1-3)Manalpha(1-6))Manbeta(1-4)GlcNAcbeta(1-4)GlcNAc-PP-dolichol
cytosolic alg3 Man5GlcNAc2 precursor
product of the Alg3p step
?
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
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-
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?
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
regulatory role for the Alg3p-dependent alpha1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation. The presence of this Man appears to provide structural information potentiating the downstream action of the endoplasmic reticulum glucosyltransferases Alg6p, Alg8p and Alg10p, glucosidases Gls1p and Gls2p, and the Golgi Och1p outerchain alpha1,6-Man branch-initiating mannosyltransferase
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-
?
additional information
?
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MNN1 encoded enzyme adds at least the penultimate alpha-1,3-linked Man of the terminal Manalpha(1-3)Manalpha(1-3)-disaccharide on O-linked glycans
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-
?
additional information
?
-
MNN1 encoded enzyme adds at least the penultimate alpha-1,3-linked Man of the terminal Manalpha(1-3)Manalpha(1-3)-disaccharide on O-linked glycans
-
-
?
additional information
?
-
-
regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
-
-
?
additional information
?
-
regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
-
-
?
additional information
?
-
involved in oligosaccharide-lipid synthesis
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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
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
the formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate. Alg3p is not required for elongation of D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
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-
?
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
regulatory role for the Alg3p-dependent alpha1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation. The presence of this Man appears to provide structural information potentiating the downstream action of the endoplasmic reticulum glucosyltransferases Alg6p, Alg8p and Alg10p, glucosidases Gls1p and Gls2p, and the Golgi Och1p outerchain alpha1,6-Man branch-initiating mannosyltransferase
-
-
?
additional information
?
-
-
regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
-
-
?
additional information
?
-
regulatory role for the Alg3p-dependent alpha-1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation, it provides structural information that potentiates the Alg6p, Alg8p and Alg10p ER glucosyltransferases and Gls1p and Gls2p trimming glucosidases
-
-
?
additional information
?
-
involved in oligosaccharide-lipid synthesis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
the formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-Dol to Man9Glc-NAc2-PP-Dol on the lumenal side use dolichyl beta-D-mannosyl phosphate
physiological function
malfunction
alg3 yeast accumulates Man5GlcNAc2-P-P-dolichol due to a defective alphal,3-mannosyltransferase required for the next step in oligosaccharide-lipid elongation
malfunction
the alg3 mutant accumulates D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
malfunction
the inactivation of the nonessential ALG3 gene results in the accumulation of lipid-linked Man5GlcNAc2 and protein-bound carbohydrates which are completely Endo H resistant
physiological function
regulatory role for the Alg3p-dependent alpha1,3-linked Man in subsequent oligosaccharide-lipid and glycoprotein glycan maturation. The presence of this Man appears to provide structural information potentiating the downstream action of the endoplasmic reticulum glucosyltransferases Alg6p, Alg8p and Alg10p, glucosidases Gls1p and Gls2p, and the Golgi Och1p outerchain alpha1,6-Man branch-initiating mannosyltransferase
physiological function
-
an the alg3 knockout strain displays decreased site-specific N-glycosylation occupancy preferentially at Asn-Xaa-Ser sequences located in secondary structural elements. Glycosylation sites are not uniformly affected in DELTAalg3 cells, with the subset of sites with lower affinity for oligosaccharyltransferase most strongly affected. 13 specific glycosylation sites are found which are underglycosylated in the DELTAalg3 strain compared to wild type cells. The features of these glycosylation sites suggest that they are the subset of normally modified sites that are more difficult for oligosaccharyltransferase to glycosylate. Under-glycosylated sites in the DELTAalg3 strain are likely to be present in secondary structural elements such as helices or sheets, whereas efficiently glycosylated sites are more likely present in flexible loops
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
alg3 encodes enzyme responsible for the alpha-1,3-Man middle-arm addition, MNN1 encoded enzyme adds at least the penultimate alpha-1,3-linked Man of the terminal Manalpha(1-3)Manalpha(1-3)-disaccharide on O-linked glycans
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cipollo, J.F.; Trimble, R.B.
The accumulation of Man6GlcNAc2-PP-dolichol in the Saccharomyces cerevisiae deltaalg9 mutant reveals a regulatory role for the Alg3p alpha1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing
J. Biol. Chem.
275
4267-4277
2000
Saccharomyces cerevisiae, Saccharomyces cerevisiae (P38179), Saccharomyces cerevisiae A (P38179)
Verostek, M.F.; Atkinson, P.H.; Trimble, R.B.
Structure of Saccharomyces cerevisiae alg3,sec18 mutant oligosaccharides
J. Biol. Chem.
266
5547-5551
1991
Saccharomyces cerevisiae (P38179), Saccharomyces cerevisiae A (P38179)
Sharma, C.B.; Knauer, R.; Lehle, L.
Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase
Biol. Chem.
382
321-328
2001
Saccharomyces cerevisiae (P38179), Saccharomyces cerevisiae
Aebi, M.; Gassenhuber, J.; Domdey, H.; te Heesen, S.
Cloning and characterization of the ALG3 gene of Saccharomyces cerevisiae
Glycobiology
6
439-444
1996
Saccharomyces cerevisiae (P38179)
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