EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
2.4.1.B58 | membrane | multispanning membrane protein | Haloferax volcanii | 16020 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.B58 | dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein | Haloferax volcanii | the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway | dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein | - |
? | |
2.4.1.B58 | dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein | Haloferax volcanii DSM 3757 | the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway | dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.4.1.B58 | Haloferax volcanii | D4GYH0 | - |
- |
2.4.1.B58 | Haloferax volcanii DSM 3757 | D4GYH0 | - |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.4.1.B58 | dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein | the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway | Haloferax volcanii | dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein | - |
? | |
2.4.1.B58 | dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein | cells lacking HVO_1526 do not present peaks corresponding to the pentasaccharide-modified Asn-13-containing peptide. When cells of the deletion strain are transformed to express a polyhistidine-tagged version of HVO_1526, it is observed that the Asn-13-containing S-layer glycoprotein-derived peptide is once again modified by the complete pentasaccharide | Haloferax volcanii | dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein | - |
? | |
2.4.1.B58 | dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein | the enzyme is involved in the assembly a pentasaccharide to selected Asn residues of the S-layer glycoprotein in the archaeal N-glycosylation pathway | Haloferax volcanii DSM 3757 | dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein | - |
? | |
2.4.1.B58 | dolichyl beta-D-mannosyl phosphate + protein-bound glycan comprising the first four subunits of the N-linked pentasaccharide attached to the S-layer glycoprotein | cells lacking HVO_1526 do not present peaks corresponding to the pentasaccharide-modified Asn-13-containing peptide. When cells of the deletion strain are transformed to express a polyhistidine-tagged version of HVO_1526, it is observed that the Asn-13-containing S-layer glycoprotein-derived peptide is once again modified by the complete pentasaccharide | Haloferax volcanii DSM 3757 | dolichyl phosphate + protein-bound glycan comprising the N-linked pentasaccharide attached to the S-layer glycoprotein | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.4.1.B58 | AglS | - |
Haloferax volcanii |
2.4.1.B58 | HVO_1526 | locus name | Haloferax volcanii |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.4.1.B58 | malfunction | cells lacking HVO_1526 do not present peaks corresponding to the pentasaccharide-modified Asn-13-containing peptide. When cells of the deletion strain are transformed to express a polyhistidine-tagged version of HVO_1526, it is observed that the Asn-13-containing S-layer glycoprotein-derived peptide is once again modified by the complete pentasaccharide | Haloferax volcanii |
2.4.1.B58 | physiological function | the enzyme is involved in the archaeal N-glycosylation pathway | Haloferax volcanii |