ProGT10.2 (PglA)

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ProGT ID ProGT10.2 (PglA)
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 NamepglA 
NCBI Gene ID905416
NCBI Reference SequenceNC_002163.1.
Protein information
Protein NamePglA 
UniProtKB/ SwissProt IDQ0P9C9
NCBI Ref SeqWP_002852885.1.
UniProtKB Sequence>sp|Q0P9C9|PGLA_CAMJE N,N'-diacetylbacillosaminyl-diphospho-undecaprenol alpha-1,3-N-acetylgalactosaminyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) GN=pglA PE=1 SV=1 MRIGFLSHAGASIYHFRMPIIKALKDRKDEVFVIVPQDEYTQKLRDLGLKVIVYEFSRAS LNPFVVLKNFFYLAKVLKNLNLDFIQSAAHKSNTFGILAAKWAKIPYRFALVEGLGSFYI DQGFKANLVRFVINSLYKLSFKFAHQFIFVNESNAEFMRNLGLKENKICVIKSVGINLKK FFPIYVESEKKELFWKNLNIDKKPIVLMIARALWHKGVKEFYESATMLKDKANFVLVGGR DENPSCASLEFLNSGAVHYLGARSDIVELLQNCDIFVLPSYKEGFPVSVLEAKACGKAIV VSDCEGCVEAISNAYDGLWAKTKNAKDLSEKISLLLEDEKLRLNLAKNAAQDALQYDENI IAQRYLKLYDRVIKNV
EMBL CDSCAL35242.1.
Sequence length376 AA
String192222.Cj1125c.
Glycosylation Information
CAZY FamilyGT4
EC Number (BRENDA)2.4.1.290
Sugar Donor SpecificityUDP-GalNAc 
Acceptor Substrate SpecificityUndPP-diNAcBac
Experimental ValidationIn vivo and In vitro
ProductUndPP-diNAcBac-GalNAc
Donor SpecificityUDP-GalNAc
Function in Glycosylation pathway1) PglA is a GalNAc transferase and adds the first GalNAc residues to the Campylobacter jejuni glycan.
Additional Information1) PglA is very specific enzyme other than Und-PP-Bac, it also accepts Und-PP-6-hydroxybacillosamine and Und-PP-GlcNAc to lesser extents.  
Litrature
Year Of Validation2005 
Reference Glover, K.J., Weerapana, E. and 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), pp.14255-14259.

Corresponding AuthorDepartments of Chemistry and Biology, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139