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
Classification Phylum : Proteobacteria
Class : Epsilonproteobacteria
Orders : Campylobacterales
Family : Campylobacteraceae
Genus : Campylobacter
Species : jejuni
Subspecies : jejuni
Strain : ATCC 700819 / NCTC 11168
Taxonomic ID (NCBI)192222
Genome Information
Gene BankAL111168.1
EMBLAL111168.1
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. and Imperiali, B., 2006. In vitro biosynthesis of UDP-N, N ‘-diacetylbacillosamine by enzymes of the Campylobacter jejuni general protein glycosylation system. Biochemistry, 45(45), pp.13659-13669.

Corresponding AuthorDepartment 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. and 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), pp.1827-1836.

Corresponding AuthorBiotechnology Research Institute, National Research Council of Canada.
Reference Rangarajan, E.S., Ruane, K.M., Sulea, T., Watson, D.C., Proteau, A., Leclerc, S., Cygler, M., Matte, A. and 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), pp.1827-1836.

Corresponding AuthorInstitute for Biological Sciences, National Research Council of Canada.
Reference Reid, C.W., Stupak, J., Chen, M.M., Imperiali, B., Li, J. and 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), pp.5468-5475.

Corresponding AuthorNational Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6.
Reference Reid, C.W., Stupak, J., Chen, M.M., Imperiali, B., Li, J. and 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), pp.5468-5475.

Corresponding AuthorNational Research Council, Institute for Biological Sciences, 100 Sussex Drive, Ottawa, ON, Canada, K1A 0R6.