EC Number | Cloned (Comment) | Organism |
---|---|---|
2.4.1.109 | expression in Saccharomyces cerevisiae | Schizosaccharomyces pombe |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.109 | dolichyl phosphate D-mannose + protein | Schizosaccharomyces pombe | O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential | dolichyl phosphate + O-D-mannosylprotein | - |
? | |
2.4.1.109 | dolichyl phosphate D-mannose + protein | Schizosaccharomyces pombe | O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination | dolichyl phosphate + O-D-mannosylprotein | - |
? | |
2.4.1.109 | dolichyl phosphate D-mannose + protein | Schizosaccharomyces pombe | O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells | dolichyl phosphate + O-D-mannosylprotein | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.109 | Schizosaccharomyces pombe | O13898 | - |
- |
2.4.1.109 | Schizosaccharomyces pombe | O42933 | - |
- |
2.4.1.109 | Schizosaccharomyces pombe | Q9C100 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.109 | dolichyl phosphate D-mannose + protein | O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential | Schizosaccharomyces pombe | dolichyl phosphate + O-D-mannosylprotein | - |
? | |
2.4.1.109 | dolichyl phosphate D-mannose + protein | O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. None of the ogm genes is found to be essential. ogm4D mutants differ morphologically from wild type and exhibit defects in sexual agglutination | Schizosaccharomyces pombe | dolichyl phosphate + O-D-mannosylprotein | - |
? | |
2.4.1.109 | dolichyl phosphate D-mannose + protein | O-glycosylation initiated by Ogm proteins plays crucial physiological roles and can serve as a sorting determinant for protein transport of membrane glycoproteins. While none of the ogm genes is found to be essential, ogm1D mutants differ morphologically from wildtype and exhibit defects in sexual agglutination. O-glycosylation of chitinase from Saccharomyces cerevisiae is decreased in ogm1D cells | Schizosaccharomyces pombe | dolichyl phosphate + O-D-mannosylprotein | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.109 | dolichyl-phosphate-mannose--protein mannosyltransferase 1 | - |
Schizosaccharomyces pombe |
2.4.1.109 | dolichyl-phosphate-mannose--protein mannosyltransferase 2 | - |
Schizosaccharomyces pombe |
2.4.1.109 | dolichyl-phosphate-mannose--protein mannosyltransferase 4 | - |
Schizosaccharomyces pombe |
2.4.1.109 | O-glycoside mannosyltransferase | - |
Schizosaccharomyces pombe |
2.4.1.109 | ogm1 | - |
Schizosaccharomyces pombe |
2.4.1.109 | ogm2 | - |
Schizosaccharomyces pombe |
2.4.1.109 | ogm4 | - |
Schizosaccharomyces pombe |