| ProGT ID | ProGT10.1 (PglH) |
| Organism Information | |
| Organism Name | Campylobacter jejuni 11168H |
| Domain | Bacteria |
| Phylum | Proteobacteria |
| Classification | Family: Campylobacteraceae Order: Campylobacterales Class: Epsilonproteobacteria Division or phylum: "Proteobacteria" |
| Taxonomic ID (NCBI) | 192222 |
| Genome Information | |
| Gene Bank | AL111168 |
| EMBL | AL111168 |
| Gene Information | |
| Gene Name | pglHÂ |
| NCBI Gene ID | 905420 |
| NCBI Reference Sequence | NC_002163.1. |
| Protein information | |
| Protein Name | PglHÂ |
| UniProtKB/ SwissProt ID | Q0P9C5 |
| NCBI Ref Seq | YP_002344522.1 |
| UniProtKB Sequence | >sp|Q0P9C5|PGLH_CAMJE GalNAc-alpha-(1->4)-GalNAc-alpha-(1->3)-diNAcBac-PP-undecaprenol alpha-1,4-N-acetyl-D-galactosaminyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=pglH PE=1 SV=1 MMKISFIIATLNSGGAERALVTLANALCKEHEVSIIKFHAGESFYKLENEVKVTSLEQFR FDTLYHKIASRFKKFFALRKALKESKSDVFISFLDTTNIACIAAKIGLKTPLIISEHSNE AYLKPKIWRFLRRVSYPFCDALSVLGSSDKVYYERFVKRVKLLLNPCHFSDEISFDSSFE KENLVLFIGRLDHNKNPVMFLKAIAHLDKNLQENYKFVIAGDGQLRQELEYKVKSLGIKV DFLGRVENVKALYEKAKVLCLCSFVEGLPTVLIESLYFEVCRISSSYYNGAKDLIKDNHD GLLVGCDDEIALAKKLELVLNDENFRKELVNNAKQRCKDFEISHIKEEWLKLIAEVKNA |
| EMBL CDS | CAL35246.1. |
| Sequence length | 359 AA |
| String | 192222.Cj1129c. |
| Glycosylation Information | |
| CAZY Family | GT4 |
| EC Number (BRENDA) | 2.4.1.292 |
| Sugar Donor Specificity | UDP-GalNAc |
| Acceptor Substrate Specificity | UndPP-diNAcBac-GalNAc |
| Experimental Validation | In vitro |
| Product | UndPP-diNAcBac-GalNAc-GalNAc-GalNAc-GalNAc |
| Donor Specificity | UDP-GalNAc |
| Function in Glycosylation pathway | 1) It has a GalNAc alpha-1-4 glycosyltransferase activity and it transfers the three terminal GalNAc residues to the Campylobacter jejuni glycan. |
| Litrature | |
| Year Of Validation | 2004Â |
| Reference | Karlyshev, A. V., Everest, P., Linton, D., Cawthraw, S., Newell, D. G., & Wren, B. W. (2004). The Campylobacter jejuni general glycosylation system is important for attachment to human epithelial cells and in the colonization of chicks. Microbiology, 150(6), 1957-1964. |
| Authors | Karlyshev, A. V., Everest, P., Linton, D., Cawthraw, S., Newell, D. G., & Wren, B. W. |
| Research groups | London School of Hygiene and Tropical Medicine, University of London, Keppel Street, London EC1A 7HT, UK. |
| Corresponding Author | Wren, B. W. |
| Contacts | London School of Hygiene and Tropical Medicine, University of London, Keppel Street, London EC1A 7HT, UK. |
| Reference | Glover, K. J., Weerapana, E., & Imperiali, B. (2005). In vitro assembly of the undecaprenylpyrophosphate-linked heptasaccharide for prokaryotic N-linked glycosylation. Proceedings of the National Academy of Sciences, 102(40), 14255-14259. |
| Authors | Glover, K. J., Weerapana, E., & Imperiali, B. |
| Research groups | Departments of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139. |
| Corresponding Author | Szymanski, C. M. |
| Contacts | Departments of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139 |
| Reference | Reid, C. W., Stupak, J., Chen, M. M., Imperiali, B., Li, J., & Szymanski, C. M. (2008). Affinity-capture tandem mass spectrometric characterization of polyprenyl-linked oligosaccharides: tool to study protein N-glycosylation pathways. Analytical chemistry, 80(14), 5468-5475. |
| Authors | Reid, C. W., Stupak, J., Chen, M. M., Imperiali, B., Li, J., & Szymanski, C. M. |
| Research groups | National Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6. |
| Corresponding Author | Szymanski, C. M. |
| Contacts | National Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6. |