| ProGT ID | ProGT16.3 (AglC) |
| Organism Information | |
| Organism Name | Methanococcus voltae PS |
| Domain | Archaebacteria |
| Classification | Phylum : Euryarchaeota Class : Methanococci Orders : Methanococcales Family : Methanococcaceae Genus : Methanococcus Species : voltae Strain : PS |
| Taxonomic ID (NCBI) | 2188 |
| Genome Information | |
| Gene Bank | DQ372941.1 |
| EMBL | DQ372941.1 |
| Gene Information | |
| Gene Name | aglC |
| NCBI Reference Sequence | DQ372941 |
| Protein information | |
| Protein Name | AglC |
| UniProtKB/ SwissProt ID | B3VA59 |
| UniProtKB Sequence | >sp|B3VA59|AGLC_METVO Dolichyl N-acetyl-alpha-D-glucosaminyl phosphate 3-beta-D-2,3-diacetamido-2,3-dideoxy-beta-D-glucuronosyltransferase OS=Methanococcus voltae GN=aglC PE=1 SV=1 MNFISIIIPTFNEEKYITKCLENWFNQDYPKENYEILIFDGKSTDKTLDVIKELQKKHNF ENIKIYTNEKRKQVYAFNEGIKNANGDFFIIFGAHAYPEQDFLKNNIETYQRIKKEEPKL AGVGGIINKISENMSAEIAKVIYSTPLSGGSSFWYAKEGFFSNTVVYGMYDTKMIKESEI LFDTDFITGQDFEFNLHLIKEGFKLYTNPNIVSSYYTRSSVKKFIKQTISYGAAKGLMIR KGYFNILWLFPFGFLFMLLSIIITGLLIFIYIMAILIDTIRLLIKTREPLYIALPILLFL FHCLISYGFFKGLIKGNSTFK |
| EMBL CDS | ACE74695.1. |
| Sequence length | 321 AA |
| Subcellular Location | Membrane (Integral component of membrane) |
| Glycosylation Information | |
| CAZY Family | GT2 |
| EC Number (BRENDA) | 2.4.1.335 |
| Sugar Donor Specificity | UDP-Glc-2,3-diNAcA |
| Acceptor Substrate Specificity | Dol-P-GlcNAc |
| Experimental Validation | In vivo |
| Product | Dol-P-GlcNAc-Glc-2,3-diNAcA |
| Donor Specificity | UDP-Glc-2,3-diNAcA |
| Function in Glycosylation pathway | 1) AglC is Glc-2,3-diNAcA glycosyltransferase, It transfers Glc-2,3-diNAcA to Dol-P-GlcNAc to form a beta-1,3 linkage. |
| Litrature | |
| Year Of Validation | 2009 |
| Reference | Chaban, B., Logan, S.M., Kelly, J.F. and Jarrell, K.F., 2009. AglC and AglK are involved in biosynthesis and attachment of diacetylated glucuronic acid to the N-glycan in Methanococcus voltae. Journal of Bacteriology, 191(1), pp.187-195. |
| Corresponding Author | Department of Microbiology and Immunology, Queens University, Kingston, Ontario, K7L 3N6, Canada. |
| Reference | Larkin, A., Chang, M.M., Whitworth, G.E. and Imperiali, B., 2013. Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis. Nature chemical biology, 9(6), pp.367-373. |
| Corresponding Author | Department of Life Sciences, Ben Gurion University of the Negev, Beersheva, Israel. |