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Information on EC 2.4.1.132 - GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase and Organism(s) Homo sapiens and UniProt Accession Q9H553
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2.4.1.132 GDP-Man:Man1GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferaseIUBMB Comments
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation of D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
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Word Map
- 2.4.1.132
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alpha-1,2-mannosyltransferase
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lipid-linked
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alpha-1,3-linked
- mannoses
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beta-glcnac
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oligosaccharide-lipids
- mannans
- pharmacology
- medicine
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
Reaction Schemes
Synonyms
alpha-1,3-mannosyltransferase, mannosyltransferase ii, halg2, scalg2, gdp-man:dol-pp-glcnac2man2 alpha-1,3-mannosyltransferase, gdp-man:man1glcnac2-pp-dolichol mannosyltransferase, asparagine-linked glycosylation 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-1,3-mannosyltransferase
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GDP-mannose-oligosaccharide-lipid mannosyltransferase II
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mannosyltransferase II
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mannosyltransferase, guanosine diphosphomannose-oligosaccharide-lipid II
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
GDP-D-mannose:D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol 3-alpha-mannosyltransferase
The biosynthesis of asparagine-linked glycoproteins utilizes a dolichyl diphosphate-linked glycosyl donor, which is assembled by the series of membrane-bound glycosyltransferases that comprise the dolichol pathway. Alg2 mannosyltransferase from Saccharomyces cerevisiae carries out an alpha1,3-mannosylation of D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol, followed by an alpha1,6-mannosylation (cf. EC 2.4.1.257), to form the first branched pentasaccharide intermediate of the dolichol pathway [1,2].
CAS REGISTRY NUMBER
COMMENTARY
81181-76-2
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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
GDP-alpha-D-mannose + beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
GDP + alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol
hALG2
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?
additional information
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hALG2: early steps of dolichol-linked oligosaccharide biosynthesis
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?
additional information
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hALG2: early steps of dolichol-linked oligosaccharide biosynthesis
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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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hALG2: early steps of dolichol-linked oligosaccharide biosynthesis
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additional information
?
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hALG2: early steps of dolichol-linked oligosaccharide biosynthesis
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
ALG2 is a type I transmembrane protein with the active site located in the cytosol
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
ALG2 is an alpha-1,3-mannosyltransferase that catalyses the second and third mannosylation steps in the N-linked glycosylation pathway
physiological function
the enzyme transfers D-mannosyl units to endoplasmic reticulum membrane-bound N-acetylglucosaminyl dolichyl-phosphates
malfunction
deficiency of GDP-Man:Man1GlcNAc2-PP-dolichol mannosyltransferase, is the cause of a congenital disorders of glycosylation designated CDG-Ii. The patients are normal at birth but develop in the 1st year of life a multisystemic disorder with mental retardation, seizures, coloboma of the iris, hypomyelination, hepatomegaly, and coagulation abnormalities. An accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol is observed in skin fibroblasts of the patient. Incubation of patient fibroblast extracts with Man1GlcNAc2-PP-dolichol and GDP-mannose reveals a severely reduced activity of the mannosyltransferase elongating Man1GlcNAc2-PP dolichol
malfunction
enzyme mutations are linked to congenital myasthenic syndrome
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). ALG2_HUMAN
416
0
47092
Swiss-Prot
other Location (Reliability: 3)
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G393T/DELTAG1040
mutation in a patient with a congenital disorders of glycosylation designated CDG-Ii caused by ALG2 deficiency
V68G
naturally occuring mutation, a non-conservative change, a pathogenic mutation causing a rare congenital disorder such as congenital myasthenic syndrome, CMS
additional information
additional information
variant c.214_226delinsAGTCCCCGGC, p.72_75delinsSPR, removes a highly conserved GDWL motif of the glycosyltransferase 4-like domain, and inserts three different amino acids
additional information
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variant c.214_226delinsAGTCCCCGGC, p.72_75delinsSPR, removes a highly conserved GDWL motif of the glycosyltransferase 4-like domain, and inserts three different amino acids
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
hALG2 encodes an alpha-1,3-mannosyltransferase resulting in Manalpha(1-3)ManGlcNAc2-PP-dolichol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
hALG2 is the cause of a new type of congenital disorders of glycosylation designated CDG-Ii
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Thiel, C.; Schwarz, M.; Peng, J.; Grzmil, M.; Hasilik, M.; Braulke, T.; Kohlschuetter, A.; von Figura, K.; Lehle, L.; Koerner, C.
A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis
J. Biol. Chem.
278
22498-22505
2003
Homo sapiens, Homo sapiens (Q9H553), Saccharomyces cerevisiae, Saccharomyces cerevisiae (P43636), Saccharomyces cerevisiae A
Cossins, J.; Belaya, K.; Hicks, D.; Salih, M.A.; Finlayson, S.; Carboni, N.; Liu, W.W.; Maxwell, S.; Zoltowska, K.; Farsani, G.T.; Laval, S.; Seidhamed, M.Z.; Seidhamed, M.Z.; Donnelly, P.; Bentley, D.; McGowan, S.J.; Mueller, J.; Palace, J.; Lochmueller, H.; Beeson, D.
Congenital myasthenic syndromes due to mutations in ALG2 and ALG14
Brain
136
944-956
2013
Homo sapiens (Q9H553), Homo sapiens, Mus musculus (Q9DBE8)
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