ProGT16 (AglB)

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ProGT ID ProGT16 (AglB)
ProGT Pathway
Organism Information
Organism NameMethanococcus voltae PS
Clinical ImplicationNon-pathogenic
DomainArchaebacteria
Classification Phylum : Euryarchaeota
Class : Methanococci
Orders : Methanococcales
Family : Methanococcaceae
Genus : Methanococcus
Species : voltae
Strain : PS
Taxonomic ID (NCBI)523842
Genome Information
Gene Information
Gene NameaglB
NCBI Reference SequenceABD17750
Protein information
Protein NameAglB 
UniProtKB/ SwissProt IDQ2EMT4
UniProtKB Sequence>sp|Q2EMT4|AGLB_METVO Dolichyl-phosphooligosaccharide-protein glycotransferase OS=Methanococcus voltae GN=aglB PE=1 SV=1 MTENNEKVKNSDSANNQSSKNSKFNFNFEDKKVKCAKTILIIIFLAFLSFQMRAQTADMG FTTNEQYLDVFSDDNGRMYLTALDPYYYLRMSENYLENGHTGDTLKNIDGQQVPWDSYKY GPTGARATFNLLSVVTVWVYQVWHAMDSTVTLMNAAFWVPAILSMFLITPIFFTVRRITS SDIGGAVAAILASLSPSIFVKTVAGFSDTPILEILPLLFIVWFIIEAIHYSKEKNYKSLI YGLLATLMLALYPFMWSAWWYGYYIVIAFLVIYAIYKGISYNSIAKYTKSKNNNHKDKIE SEKLEMLNILKISGLFIIGGAVLITALYGVSTTMNALQAPLNYLGLDEVSSQTGWPNVLT TVSELDTASLDEIISSSLGSIHLFAIGLIGIFLSLFRKVLTPVKQISNGLAEKLDIKYAL LLIIWFAVTFLAASKGVRFVALMVPPLSIGVGIFVGFIEQFIKNNLDKKYEYVAYPTIAI IVLYALFTIYRADSADLVRMLLPSNYVPIAEGIMLASLAVLIIYKVAELIAESNKKLVMN KIFMILLAIGLITPTIATIVPFYSVPTYNDGWGESLEWINTQTPNNSVVTCWWDNGHIYT WKTDRMVTFDGSSQNTPRAYWVGRAFSTSNESLANGIFRMLASSGDKAYTTDSVLIKKTG SIKNTVDVLNEILPLTKSDAQKALKNSSYKFTDTEVSEILDATHPKVTNPDYLITYNRMT SIASVWSYFGNWDFNLPAGTSRSEREAGSFQGLQTYATNINDTLIVRSLIQQTAEYNIYT LIEVRNETLTGAMMAVTNDGQMQTQQLNMHKVKLMVNENGKSKMYNSLADPDGQLSLLIK VDKNSIIGTDGSNNPVYSSSSWMATANLEDSVYSKLHFFDGEGLDTIKLEKESLDPTANG VQPGFKVFSVDYGNYSK
EMBL CDSABD17750.1
Sequence length917 AA
Subcellular LocationMembrane (Integral component of membrane)
Function in Native Organism 1) AglB is OSTase transfer the trisaccharide to the S-Layer protein and flagellin.
Additional Information1) M. voltae AglB has relaxed specificity and attaches incomplete glycans on flagellins and S-layer proteins.
2) AglB is a homolog of the eukaryotic (STT3p) and bacterial (PglB) oligosaccharyl transferases and contain conserved region WWDYG in its active site.
3) It has the ability to transfer glycans of similar but different composition, including glycans with either GlcNAc or GalNAc as a linking sugar.
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.1.-
Mechanism of Glycan TransferEn bloc
Acceptor specificity Sequon_1Asn-Xaa-Ser/Thr
Donor TypeDolP-GlcNAc-Glc-2,3-diNAcA
Donor SpecificityLipid linked sugars
Accessory GT IDProGT16.1, ProGT16.2, ProGT16.3, ProGT16.4
Glycan Information
Glycan transferredTrisaccharide (ManNAc(6Thr)A-beta1,4-Glc-2,3-diNAcA-beta1,3-GlcNAc) 
Method of Glycan IndentificationNano-LC-MS/MS and NMR
Experimental_strategiesIn vitro and In vivo  
Acceptor Subtrate Information
Acceptor Substrate name FlaA
ProGPdb ID ProGP238
Acceptor Substrate name FlaB1
ProGPdb ID ProGP238
Acceptor Substrate name FlaB2
ProGPdb ID ProGP239
Acceptor Substrate name FlaB3
ProGPdb ID ProGP240
Acceptor Substrate name FlaA
ProGPdb ID ProGP241
Acceptor Substrate name S-layer protein
ProGPdb ID ProGP242
Litrature
Year Of Validation2006 
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 AuthorDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA
Reference Chaban, B., Voisin, S., Kelly, J., Logan, S.M. and Jarrell, K.F., 2006. Identification of genes involved in the biosynthesis and attachment of Methanococcus voltae N?linked glycans: insight into N?linked glycosylation pathways in Archaea. Molecular microbiology, 61(1), pp.259-268.

Corresponding AuthorDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
Reference Shams-Eldin, H., Chaban, B., Niehus, S., Schwarz, R.T. and Jarrell, K.F., 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. Journal of Bacteriology, 190(6), pp.2217-2220.

Corresponding AuthorDepartment of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, Canada
Reference Ding, Y., Vrionis, H.A., Schneider, J., Berezuk, A., Khursigara, C.M. and Jarrell, K.F., 2016. Complementation of an aglB mutant of Methanococcus maripaludis with heterologous oligosaccharyltransferases. PloS one, 11(12), p.e0167611.

Corresponding AuthorDepartment of Biomedical and Molecular Sciences, Queen's University, Kingston, Ontario, Canada