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Information on EC 2.4.1.265 - dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase
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EC Tree
2.4.1.265 dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferaseIUBMB Comments
The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
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Synonyms
halg8, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALG8
dolichyl-P-Glc:Glc1 Man9GlcNAc2-PP-dolichyl alpha1,3-glucosyltransferase
-
dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl alpha1,3-glucosyltransferase
-
dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
dolichyl beta-D-glucosyl phosphate + alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol = alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphosphodolichol + dolichyl phosphate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
dolichyl beta-D-glucosyl phosphate: D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-mannosyltransferase
The successive addition of three glucose residues by EC 2.4.1.267 (dolichyl-P-Glc:Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase), EC 2.4.1.265 and EC 2.4.1.256 (dolichyl-P-Glc:Glc2Man9GlcNAc2-PP-dolichol alpha-1,2-glucosyltransferase) represents the final stage of the lipid-linked oligosaccharide assembly.
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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
dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
-
-
-
?
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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-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate
-
-
-
?
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Congenital Disorders of Glycosylation
A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation.
Congenital, Hereditary, and Neonatal Diseases and Abnormalities
A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
ALG8 deficiency (CDG Ih), leads to protein N-glycosylation defects caused by malfunction of Dol-P-Glc:Glc1-Man9-GlcNAc2-P-P-Dol glucosyltransferase resulting in inefficient addition of the second glucose residue onto lipid-linked oligosaccharides. The lipid-linked oligosaccharide profile of the patient shows the accumulation of incomplete precursor structures corresponding to GlcNAc2Man9 and GlcNAc2-Man9Glc1. Two ALG8 mutations in heterozygous form are detected in the patient. The first mutation (c.139A>C), is combined with a c.1090C>T mutation. The index mutation, which is translated into the missense mutation p.T47P, is inherited from the father. The c.1090C>T mutation resulting in a premature stop codon (p.R364X) is found in heterozygous form in the mother, whereas it is not found in 150 healthy controls. The prognosis of patients with ALG8 deficiency is unfavourable. The majority of affected children have early onset of the disease with heterogeneous symptoms including multiple organ dysfunction, coagulopathy and protein-losing enteropathy
malfunction
CDG type Ih is caused by a deficiency of the dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl alpha1,3-glucosyltransferase. The defect leads to an accumulation of Dol-PP-Glc-NAc2Man9 and Dol-PP-GlcNAc2Man9Glc1 in the endoplasmic reticulum of patients fibroblasts that can be detected by analyzing the lipid-linked oligosaccharyl intermediates. Two mildly affected siblings with CDG-Ih caused by two novel mutations are described. While one mutation (c.1434delC) causes a frame shift resulting in a premature termination codon (p.485X), the point mutation of the other allele (c.845C>T, p.A282V) causes an amino acid replacement in a highly conserved region of the hALG8 gene. The two siblings show similar symptoms, including pseudo-gynecomastia, epicanthus, muscular hypotonia, mental retardation and ataxia, expanding the genetic and clinical spectrum of CDG-Ih
malfunction
cells carrying the alg8-1 mutation accumulate Glc1Man9GlcNAc2-lipid both in vivo and in vitro
malfunction
congenital disorder of glycosylation type Ih (CDG-Ih) is caused by a defect in the dolichyl-P-Glc:Glc1 Man9GlcNAc2-PP-dolichyl alpha1,3-glucosyltransferase (ALG8). Accumulation of the lipid-linked oligosaccharyl intermediates Dol-PP-GlcNAc2Man9 and Dol-PP-GlcNAc2Man9Glc1 in patients' fibroblasts. Mutation analysis of the ALG8 gene identifies in both families a compound heterozygosity for a splice site mutation and a missense mutation (family 1: c.96-2A>G and p.T47P; family 2: c.672+4A>G and p.G275D). The functional effect of the ALG8 splice mutations is analysed on mRNA and the effect of the missense mutations is assayed in ALG8 deficient yeast strains. The molecular and clinical features of three patients from two families with an ALG8 deficiency are described. All three patients show severe, life-threatening multi organ failure and die within their first months of life
malfunction
patient with inefficient addition of the second glucose residue onto lipid-linked oligosaccharide. The patient possesses only 1020% normal amounts of mRNA encoding the enzyme, dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase (hALG8p), which catalyzes this reaction. Sequencing of hALG8 genomic DNA reveals exon 4 to contain a base deletion in one allele and a base insertion in the other. Both mutations give rise to premature stop codons predicted to generate severely truncated proteins. Because the translation inhibitor emetine is shown to stabilize the hALG8 mRNA from the patient to normal levels, it is likely that both transcripts undergo nonsensemediated mRNA decay. As the cells from the patient are successfully complemented with wild type hALG8 cDNA, it is concluded that these mutations are the underlying cause of this new CDG I subtype that we propose be called CDG Ih
malfunction
the ALG8 protein is a hydrophobic protein that is not essential for the vegetative growth of yeast. The lack of this protein results in underglycosylation of secreted proteins
physiological function
-
deletion of algK, a protein essential for alginate secretion, in an alginate-overproducing strain, PDO300, interferes with the polymerization of alginate, suggesting that in the absence of AlgK, the polymerase and copolymerase subunits, Alg8 and Alg44, are destabilized. Deletion of Alg8 resulted in the absence of AlgK, AlgX, and Alg44 from the envelope fraction and leads to a complete loss of production of alginate
physiological function
-
generation of a marker-free isogenic double-gene-knockout mutant lacking Alg8 and 44. This mutant lost the mucoid phenotype and production of alginate. A direct interaction exists between the membrane-anchored glycosyltransferase Alg8 and the copolymerase Alg44 proteins
physiological function
-
generation of a marker-free isogenic double-gene-knockout mutant lacking Alg8 and 44. This mutant lost the mucoid phenotype and production of alginate. A direct interaction exists between the membrane-anchored glycosyltransferase Alg8 and the copolymerase Alg44 proteins
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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). ALG8_MOUSE
526
10
59535
Swiss-Prot
Secretory Pathway (Reliability: 2)
ALG8_NEUCR
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
505
11
57417
Swiss-Prot
Secretory Pathway (Reliability: 2)
ALG8_SCHPO
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
501
10
57606
Swiss-Prot
Secretory Pathway (Reliability: 3)
ALG8_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
577
12
67385
Swiss-Prot
other Location (Reliability: 2)
ALG8_ARATH
506
12
58222
Swiss-Prot
Secretory Pathway (Reliability: 5)
ALG8_ASHGO
Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
570
9
64926
Swiss-Prot
other Location (Reliability: 3)
ALG8_ASPOR
Aspergillus oryzae (strain ATCC 42149 / RIB 40)
504
11
57787
Swiss-Prot
Secretory Pathway (Reliability: 3)
ALG8_BOVIN
526
10
59964
Swiss-Prot
Secretory Pathway (Reliability: 2)
ALG8_CAEEL
766
13
86870
Swiss-Prot
Secretory Pathway (Reliability: 1)
ALG8_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
587
12
67910
Swiss-Prot
other Location (Reliability: 5)
ALG8_CANGA
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65)
550
12
64425
Swiss-Prot
Secretory Pathway (Reliability: 3)
ALG8_CHAGB
Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970)
474
11
53203
Swiss-Prot
Secretory Pathway (Reliability: 3)
ALG8_COCIM
Coccidioides immitis (strain RS)
501
9
57019
Swiss-Prot
Secretory Pathway (Reliability: 2)
ALG8_DEBHA
Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968)
559
12
65129
Swiss-Prot
other Location (Reliability: 4)
ALG8_DICDI
625
12
72999
Swiss-Prot
other Location (Reliability: 2)
ALG8_DROME
511
13
57945
Swiss-Prot
Secretory Pathway (Reliability: 1)
ALG8_EMENI
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)
509
10
58455
Swiss-Prot
Secretory Pathway (Reliability: 3)
ALG8_GIBZE
Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1)
501
12
56916
Swiss-Prot
Secretory Pathway (Reliability: 2)
ALG8_HUMAN
526
10
60088
Swiss-Prot
Secretory Pathway (Reliability: 2)
ALG8_KLULA
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37)
561
12
64574
Swiss-Prot
Mitochondrion (Reliability: 5)
A0A6A6JQ35_9PLEO
1526
10
173307
TrEMBL
Secretory Pathway (Reliability: 2)
A0A2P6TJW7_CHLSO
942
5
103164
TrEMBL
Secretory Pathway (Reliability: 5)
A0A8H4N9Z2_9PEZI
1585
10
180142
TrEMBL
Secretory Pathway (Reliability: 4)
A0A6A6RSE4_9PLEO
1551
9
176920
TrEMBL
Secretory Pathway (Reliability: 2)
A0A1E3QTV4_9ASCO
971
10
111306
TrEMBL
other Location (Reliability: 3)
F0VNP4_NEOCL
Neospora caninum (strain Liverpool)
885
12
97831
TrEMBL
other Location (Reliability: 2)
A0A6A5WQW3_9PLEO
1593
10
179887
TrEMBL
Secretory Pathway (Reliability: 3)
A0A835Y1H5_9CHLO
1297
9
132456
TrEMBL
Secretory Pathway (Reliability: 5)
A0A086MBJ1_TOXGO
896
12
98881
TrEMBL
other Location (Reliability: 3)
A0A151H8T7_TOXGO
896
12
98881
TrEMBL
other Location (Reliability: 3)
A0A6A5KEF6_9PLEO
1553
9
176594
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6A5SMN9_9PLEO
1515
9
172831
TrEMBL
Secretory Pathway (Reliability: 2)
A0A3M7MLP7_9EURO
1416
9
159083
TrEMBL
Mitochondrion (Reliability: 3)
A0A2W1ENT7_9PLEO
1484
8
167914
TrEMBL
Secretory Pathway (Reliability: 3)
E5A158_LEPMJ
Leptosphaeria maculans (strain JN3 / isolate v23.1.3 / race Av1-4-5-6-7-8)
1763
10
199803
TrEMBL
Secretory Pathway (Reliability: 2)
C5LR05_PERM5
Perkinsus marinus (strain ATCC 50983 / TXsc)
876
8
98341
TrEMBL
other Location (Reliability: 4)
A0A2U1PWT1_ARTAN
879
9
98827
TrEMBL
other Location (Reliability: 2)
A0A0F7V8X1_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
914
12
100749
TrEMBL
other Location (Reliability: 3)
A0A8H3UK99_VENIN
856
8
95523
TrEMBL
Secretory Pathway (Reliability: 2)
A0A7J6JXZ8_TOXGO
896
12
98865
TrEMBL
other Location (Reliability: 3)
A0A6A6A4Q8_9PLEO
1681
11
191321
TrEMBL
Secretory Pathway (Reliability: 3)
A0A177V6F1_9BASI
955
10
100394
TrEMBL
Mitochondrion (Reliability: 1)
S7ULF0_TOXGG
Toxoplasma gondii (strain ATCC 50853 / GT1)
896
12
98865
TrEMBL
other Location (Reliability: 3)
A0A177UL57_9BASI
948
5
100292
TrEMBL
Mitochondrion (Reliability: 2)
A0A086LHZ2_TOXGO
896
12
98760
TrEMBL
other Location (Reliability: 3)
A0A1I7VUP9_LOALO
1064
9
122086
TrEMBL
other Location (Reliability: 5)
A0A6A5Z0P2_9PLEO
1525
8
174065
TrEMBL
Secretory Pathway (Reliability: 2)
A0A6A7BCY0_9PLEO
1574
10
178842
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H6X0M1_9AGAR
1170
10
131948
TrEMBL
Mitochondrion (Reliability: 3)
A0A086QBR3_TOXGO
896
12
98879
TrEMBL
other Location (Reliability: 3)
R9PDA5_PSEHS
Pseudozyma hubeiensis (strain SY62)
851
6
92719
TrEMBL
Mitochondrion (Reliability: 5)
A0A812DNB9_SEPPH
423
14
51818
TrEMBL
Secretory Pathway (Reliability: 1)
A0A1W0W8F2_HYPDU
909
9
101974
TrEMBL
Mitochondrion (Reliability: 3)
A0A2T9Z2K1_9FUNG
1223
7
137856
TrEMBL
other Location (Reliability: 4)
A0A1Y1ZKB5_9PLEO
1532
8
174922
TrEMBL
Secretory Pathway (Reliability: 1)
S8ER60_TOXGM
Toxoplasma gondii (strain ATCC 50611 / Me49)
896
12
98833
TrEMBL
other Location (Reliability: 3)
A0A7J6FKV0_CANSA
1175
9
133738
TrEMBL
Chloroplast (Reliability: 5)
A0A1Q9D0E8_SYMMI
1453
14
158965
TrEMBL
Secretory Pathway (Reliability: 1)
A0A814PFC2_ADIRI
1121
12
128383
TrEMBL
other Location (Reliability: 4)
A0A2C6LES2_9APIC
1055
7
116833
TrEMBL
other Location (Reliability: 5)
A0A125YMM1_TOXGV
Toxoplasma gondii (strain ATCC 50861 / VEG)
896
12
98833
TrEMBL
other Location (Reliability: 3)
A0A2G8STZ3_9APHY
910
7
102774
TrEMBL
other Location (Reliability: 3)
A0A813QQK8_ADIRI
909
11
104362
TrEMBL
other Location (Reliability: 4)
A0A8J2A9K9_9DINO
886
8
98040
TrEMBL
other Location (Reliability: 2)
A0A2G8Y0D1_TOXGO
896
12
98853
TrEMBL
other Location (Reliability: 3)
A0A419PJ11_CLOSI
955
7
107439
TrEMBL
Secretory Pathway (Reliability: 5)
A0A2U1IXA9_SMIAN
1314
9
148327
TrEMBL
other Location (Reliability: 4)
A0A835Z7Q6_9STRA
901
11
95468
TrEMBL
other Location (Reliability: 4)
A0A6A6VPL8_9PLEO
1543
12
175387
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H5ZIQ9_COCSA
1612
10
183566
TrEMBL
Secretory Pathway (Reliability: 2)
A0A086R0K8_TOXGO
896
12
98923
TrEMBL
other Location (Reliability: 3)
A0A1M2VRL5_TRAPU
893
7
101130
TrEMBL
other Location (Reliability: 1)
A0A7J6LM50_PERCH
1223
12
136329
TrEMBL
other Location (Reliability: 1)
A0A2A9M7E5_9APIC
881
12
95483
TrEMBL
Secretory Pathway (Reliability: 5)
A0A177TKJ2_9BASI
947
6
100101
TrEMBL
Mitochondrion (Reliability: 2)
A0A0G4LJ92_9PEZI
1474
11
163231
TrEMBL
other Location (Reliability: 2)
A0A139XMW4_TOXGO
896
12
98881
TrEMBL
other Location (Reliability: 3)
A0A4S8JTW3_MUSBA
884
12
97124
TrEMBL
other Location (Reliability: 2)
A0A818YZF8_9BILA
913
12
105258
TrEMBL
Secretory Pathway (Reliability: 2)
A0A8H5GRW3_9AGAR
887
8
100888
TrEMBL
other Location (Reliability: 3)
A0A5D6XU65_9STRA
1071
9
119388
TrEMBL
other Location (Reliability: 5)
C1H737_PARBA
Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01)
1195
12
135455
TrEMBL
Secretory Pathway (Reliability: 2)
A0A0F4ZJM9_9PEZI
1552
8
174485
TrEMBL
Secretory Pathway (Reliability: 3)
A0A7R9A411_9CRUS
975
8
112220
TrEMBL
Mitochondrion (Reliability: 4)
A0A8H3D1Y5_9AGAM
863
15
96280
TrEMBL
Secretory Pathway (Reliability: 5)
A0A813RPZ8_ADIRI
888
13
101767
TrEMBL
other Location (Reliability: 4)
A0A3R7YQL9_TOXGO
896
12
98795
TrEMBL
other Location (Reliability: 3)
A0A6G1KPK7_9PLEO
1536
9
174258
TrEMBL
Secretory Pathway (Reliability: 2)
A0A086KZE8_TOXGO
896
12
98879
TrEMBL
other Location (Reliability: 3)
J4H4D8_9APHY
931
10
105683
TrEMBL
other Location (Reliability: 5)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A282V
CDG type Ih is caused by a deficiency of the dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichyl alpha1,3-glucosyltransferase. The defect leads to an accumulation of Dol-PP-Glc-NAc2Man9 and Dol-PP-GlcNAc2Man9Glc1 in the endoplasmic reticulum of patients fibroblasts that can be detected by analyzing the lipid-linked oligosaccharyl intermediates. Two mildly affected siblings with CDG-Ih caused by two novel mutations are described. While one mutation (c.1434delC) causes a frame shift resulting in a premature termination codon (p.485X), the point mutation of the other allele (c.845C>T, p.A282V) causes an amino acid replacement in a highly conserved region of the hALG8 gene. The two siblings show similar symptoms, including pseudo-gynecomastia, epicanthus, muscular hypotonia, mental retardation and ataxia, expanding the genetic and clinical spectrum of CDG-Ih
R364X
-
two ALG8 mutations in heterozygous form are detected in the patient. The first mutation (c.139A>C), is combined with a c.1090C>T mutation. The index mutation, which is translated into the missense mutation p.T47P, is inherited from the father. The c.1090C>T mutation resulting in a premature stop codon (p.R364X) is found in heterozygous form in the mother, whereas it is not found in 150 healthy controls. The prognosis of patients with ALG8 deficiency is unfavourable. The majority of affected children have early onset of the disease with heterogeneous symptoms including multiple organ dysfunction, coagulopathy and protein-losing enteropathy
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
expression of the genes encoding for alginate-lyase algL and the catalytic subunit of the alginate polymerase complex, dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase alg8, in chemostat cultures of Azotobacter vinelandii ATCC 9046. Increased alginate production of 2.4 g per l and a higher specific alginate production rate of 0.1 g per g and h are obtained at an inlet sucrose concentration of 15 g per l. Carbon recovery of about 100% is obtained at an inlet sucrose concentration of 10 g per l, whereas it is close to 50% at higher inlet sucrose concentrations. An increase in the molecular weight of alginate is linked to higher alg8 gene expression
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Runge, K.W.
Robbins, P.W.: A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues
J. Biol. Chem.
261
15582-15590
1986
Saccharomyces cerevisiae (P40351)
brenda
Chantret, I.; Dancourt, J.; Dupre, T.; Delenda, C.; Bucher, S.; Vuillaumier-Barrot, S.; Ogier de Baulny, H.; Peletan, C.; Danos, O.; Seta, N.; Durand, G.; Oriol, R.; Codogno, P.; Moore, S.E.
A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation
J. Biol. Chem.
278
9962-9971
2003
Homo sapiens (Q9BVK2)
brenda
Vesela, K.; Honzik, T.; Hansikova, H.; Haeuptle, M.A.; Semberova, J.; Stranak, Z.; Hennet, T.; Zeman, J.
A new case of ALG8 deficiency (CDG Ih)
J. Inherit. Metab. Dis.
32
259264
2009
Homo sapiens
brenda
Schollen, E.; Frank, C.G.; Keldermans, L.; Reyntjens, R.; Grubenmann, C.E.; Clayton, P.T.; Winchester, B.G.; Smeitink, J.; Wevers, R.A.; Aebi, M.; Hennet, T.; Matthijs, G.
Clinical and molecular features of three patients with congenital disorders of glycosylation type Ih (CDG-Ih) (ALG8 deficiency)
J. Med. Genet.
41
550-556
2004
Homo sapiens (Q9BVK2)
brenda
Stlting, T.; Omran, H.; Erlekotte, A.; Denecke, J.; Reunert, J.; Marquardt, T.
Novel ALG8 mutations expand the clinical spectrum of congenital disorder of glycosylation type Ih
Mol. Genet. Metab.
98
305-309
2009
Homo sapiens (Q9BVK2), Homo sapiens
brenda
Stagljar, I.; te Heesen, S.; Aebi, M.
New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus
Proc. Natl. Acad. Sci. USA
91
5977-5981
1994
Saccharomyces cerevisiae (P40351)
brenda
Diaz-Barrera, A.; Soto, E.; Altamirano, C.
Alginate production and alg8 gene expression by Azotobacter vinelandii in continuous cultures
J. Ind. Microbiol. Biotechnol.
39
613-621
2012
Azotobacter vinelandii
brenda
Rehman, Z.U.; Wang, Y.; Moradali, M.F.; Hay, I.D.; Rehm, B.H.
Insights into the assembly of the alginate biosynthesis machinery in Pseudomonas aeruginosa
Appl. Environ. Microbiol.
79
3264-3272
2013
Pseudomonas aeruginosa
brenda
Fata Moradali, M.; Donati, I.; Sims, I.; Ghods, S.; Rehm, B.
Alginate polymerization and modification are linked in Pseudomonas aeruginosa
mBio
6
1-17
2015
Pseudomonas aeruginosa, Pseudomonas aeruginosa PDO300
brenda
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