Protein Variants | Comment | Organism |
---|---|---|
E318A | mutation has no effect on activity | Saccharomyces cerevisiae |
E356A | mutation has no effect on activity | Saccharomyces cerevisiae |
E405/H406A | double mutant no longer supports growth, the loss of activity is not caused by a failure of Alg11 expression | Saccharomyces cerevisiae |
E405A | mutation causes an underglycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
E405A/E413 | double mutant no longer supports growth, the loss of activity is not caused by a failure of Alg11 expression | Saccharomyces cerevisiae |
E413A | mutation has no effect | Saccharomyces cerevisiae |
F407A | mutation is not detrimental for growth, impairment of glycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
G84A | mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
G84P | mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
G85A | mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
G85P | mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
G87A | mutation has no effect on growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
G87P | mutation reduces growth and glycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
H406A | mutation is not detrimental for growth, impairment of glycosylation of the vacuolar model glycoproteincarboxypeptidase Y | Saccharomyces cerevisiae |
K302A | mutation has no effect on activity | Saccharomyces cerevisiae |
K319A | mutation causes loss of Alg11 activity | Saccharomyces cerevisiae |
K322A | mutation has no effect on activity | Saccharomyces cerevisiae |
K343A | mutation has no effect on activity | Saccharomyces cerevisiae |
V412A | mutation is not detrimental for growth | Saccharomyces cerevisiae |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
membrane | - |
Saccharomyces cerevisiae | 16020 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
63140 | - |
calculated from sequence | Saccharomyces cerevisiae |
63143 | - |
x * 63143, calculated from sequence | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | Saccharomyces cerevisiae | the biosynthesis of asparagine-linked glycans occurs in an evolutionarily conserved manner with the assembly of the unique lipid-linked oligosaccharide precursor Glc3Man9GlcNAc2-PPDo at the endoplasmic reticulum. The enzyme catalyzes the transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol and subsequently to Man4GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the endoplasmic reticulum before flipping to the luminal side | 2 GDP + 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 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P53954 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | - |
Saccharomyces cerevisiae | 2 GDP + 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 | - |
? | |
2 GDP-alpha-D-mannose + D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol | the biosynthesis of asparagine-linked glycans occurs in an evolutionarily conserved manner with the assembly of the unique lipid-linked oligosaccharide precursor Glc3Man9GlcNAc2-PPDo at the endoplasmic reticulum. The enzyme catalyzes the transfer of two alpha1,2-linked mannose residues from GDP-mannose to Man3GlcNAc2-PP-Dol and subsequently to Man4GlcNAc2-PP-Dol forming the Man5GlcNAc2-PP-Dol intermediate at the cytosolic side of the endoplasmic reticulum before flipping to the luminal side | Saccharomyces cerevisiae | 2 GDP + 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 | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 63143, calculated from sequence | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
Alg11 | - |
Saccharomyces cerevisiae |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
26 | - |
assay at | Saccharomyces cerevisiae |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | - |
assay at | Saccharomyces cerevisiae |
General Information | Comment | Organism |
---|---|---|
malfunction | compared with wild-type cells, DELTAalg11 grows poorly and osmotic stabilization by KCl only slightly improved growth. Deletion of ALG11 causes a temperature-sensitive lethality between 32°C and 36°C | Saccharomyces cerevisiae |