Latest update: September 24, 2018


ProGT16.2 (AglH)

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ProGT ID ProGT16.2 (AglH)
Organism Information
Organism NameMethanococcus voltae PS
Domain Archaebacteria
Phylum Euryarchaeota
ClassificationFamily: Methanococcaceae
Order: Methanococcales
Class: Methanococci or Methanothermea
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI)2188
Genome Information
Gene BankDQ372941
EMBLDQ372941
Gene Information
Gene NameaglH 
NCBI Reference SequenceDQ372941
Protein information
Protein NameAglH 
Glycosylation Information
Sugar Donor SpecificityUDP-GlcNAc 
Acceptor Substrate SpecificityDolichol-phosphate-disaccharide
Experimental ValidationIn vivo
Donor SpecificityUDP-GlcNAc
Function in Glycosylation pathway1) AglH is a GlcNAc-1-P transferase involved in attachment of a GlcNAc residue to a dolichol lipid carrier in the membrane.
Additional Information1) Mv1751 is a GlcNAc-1-Phosphate transferase able to replaced the essential alg7 gene in S. cerevisiae. 
Litrature
Year Of Validation2008 
Reference Shams-Eldin H, Chaban B, Niehus S, Schwarz RT, Jarrell KF. (2008) Identification of the archaeal alg7 gene homolog (encoding N-acetylglucosamine-1-phosphate transferase) of the N-linked glycosylation system by cross-domain complementation in Saccharomyces cerevisiae. J Bacteriol. 190(6):2217-20. doi: 10.1128/JB.01778-07.

Authors Shams-Eldin H, Chaban B, Niehus S, Schwarz RT, Jarrell KF.
Research groupsInstitute for Virology, AG Parasitologie BMFZ, Philipps-University Marburg, Hans-Meerwein-Str. 2, 35043 Marburg, Germany.
ContactsInstitute for Virology, AG Parasitologie BMFZ, Philipps-University Marburg, Hans-Meerwein-Str. 2, 35043 Marburg, Germany.
Reference Larkin, A., Chang, M. M., Whitworth, G. E., & Imperiali, B. (2013). Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nature chemical biology, 9(6), 367.

Authors Larkin, A., Chang, M. M., Whitworth, G. E., & Imperiali, B.
Research groupsDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA.
Corresponding Author Imperiali, B.
ContactsDepartment of Life Sciences, Ben Gurion University of the Negev, Beersheva, Israel.