| Activities in Family | CMP-NeuAc: α-galactoside-a-(2,6)-sialyltransferase (EC 2.4.3.-); |
|---|---|
| Mechanism | Inverting |
| Note | Created after Romanow et al., J. Biol. Chem., 289:33945-33957 [PMID=25342753] who have shown that the C-terminal domains of bi-functional capsule polymerases from Neisseria meningitidis W and Y function as a-2,6-sialyltransferases that utilize CMP-beta-Neu5Ac as the sugar donor to build the alternating capsular polysaccharides [->6)-a-D-Gal-(1->4)-a-Neu5Ac-(2->)]n and [->6)-a-D-Glc-(1->4)-a-Neu5Ac-(2->)]n, respectively. |
| Statistics | GenBank accession (137); Uniprot accession (2); |
| Bacteria | |||||||
| Protein Name | EC# | Reference | Organism | GenBank | Uniprot | PDB/3D | |
| bifunctional alternating UDP-Gal: α-1,4-galactosyltransferase / CMP-Neu5Ac: α-2,6-sialyltransferase (SiaD-W-135) | 2.4.3.- | Neisseria meningitidis W135 | CAA74303.1 | O33390 | |||
| bifunctional alternating UDP-Glc: α-glucosyltransferase / CMP-Neu5Ac α-sialyltransferase (SiaD-Y) | 2.4.3.- | Neisseria meningitidis Y:2A:P1.2,5 | CAA74302.1 | O33391 | |||
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