Latest update: September 24, 2018


ProGT10.8 (PglD)

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ProGT ID ProGT10.8 (PglD)
Organism Information
Organism NameCampylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Domain Bacteria
PhylumProteobacteria
ClassificationFamily: Campylobacteraceae
Order: Campylobacterales
Class: Epsilonproteobacteria
Division or phylum: "Proteobacteria"
Taxonomic ID (NCBI)192222
Genome Information
Gene BankAL111168
EMBLAL111168
Gene Information
Gene NamepglD 
NCBI Gene ID905414
NCBI Reference SequenceNC_002163.1.
Protein information
Protein NamePglD 
UniProtKB/ SwissProt IDQ0P9D1
NCBI Ref SeqWP_002852865.1.
UniProtKB Sequence>sp|Q0P9D1|PGLD_CAMJE UDP-N-acetylbacillosamine N-acetyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=pglD PE=1 SV=1 MARTEKIYIYGASGHGLVCEDVAKNMGYKECIFLDDFKGMKFESTLPKYDFFIAIGNNEI RKKIYQKISENGFKIVNLIHKSALISPSAIVEENAGILIMPYVVINAKAKIEKGVILNTS SVIEHECVIGEFSHVSVGAKCAGNVKIGKNCFLGINSCVLPNLSLADDSILGGGATLVKN QDEKGVFVGVPAKRM
EMBL CDSCAL35240.1.
Sequence length195 AA
String192222.Cj1123c.
PDB ID (Structural Information)3BSY, 2NPO, 2VHE, 3BFP, 3BSS, 3BSW, 5T2Y, 5TYH
Glycosylation Information
CAZY FamilyNon-GT
EC Number (BRENDA)2.3.1.203
Experimental ValidationIn vitro and In vivo
Function in Glycosylation pathway1) PglD is an acetyltransferase, catalyzes the final step in the formation of Campylobacter jejuni by N-acetylation of the UDP-4-amino-sugar at the C4 position.
Litrature
Year Of Validation2006 
Reference Olivier, N. B., Chen, M. M., Behr, J. R., & Imperiali, B. (2006). In vitro biosynthesis of UDP-N, N ‘-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry, 45(45), 13659-13669.

Authors Olivier, N. B., Chen, M. M., Behr, J. R., & Imperiali, B.
Research groupsDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Corresponding Author Imperiali, B.
ContactsDepartment of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, Massachusetts 02139, USA.
Reference Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. & Young, N. M. (2008). Structure and active site residues of PglD, an N-acetyltransferase from the bacillosamine synthetic pathway required for N-glycan synthesis in Campylobacter jejuni. Biochemistry, 47(7), 1827-1836.

Authors Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. & Young, N. M.
Research groupsDepartment of Biochemistry, McGill University, Montreal, QC, H3G 1Y6 Canada.
Corresponding Author Burlet-Schiltz, O.
ContactsDepartment of Biochemistry, McGill University, Montreal, QC, H3G 1Y6 Canada.
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 groupsNational Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6.
Corresponding Author Szymanski, C. M.
ContactsNational Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6.