EC Number | Organism | UniProt | Comment | Textmining |
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2.4.1.258 | Pyricularia oryzae | M1RXP4 | - |
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EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
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2.4.1.258 | dolichyl beta-D-mannosyl phosphate + 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 | - |
Pyricularia oryzae | D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate | - |
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2.4.1.258 | additional information | Alg3-mediated N-glycosylation of the effector, Secreted LysM Protein1 (Slp1), is essential for its activity. Slp1 has three N-glycosylation sites and simultaneous Alg3-mediated N-glycosylation of each site is required to maintain protein stability and the chitin binding activity of Slp1 | Pyricularia oryzae | ? | - |
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EC Number | General Information | Comment | Organism |
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2.4.1.258 | physiological function | deletion of Alg3 results in the arrest of secondary infection hyphae and a significant reduction in virulence. Alg3 deletion mutants induce massive production of reactive oxygen species in host cells. Alg3-mediated N-glycosylation of the effector, Secreted LysM Protein1 (Slp1), is essential for its activity. Alg3 deletion mutants accumulate reactive oxygen species in a similar manner to Slp1 deletion mutants, which is a key factor responsible for arresting infection hyphae of the mutants | Pyricularia oryzae |