Latest update: September 24, 2018


ProGT23 (AglB)

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ProGT ID ProGT23 (AglB)
Organism Information
Organism NamePyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Clinical ImplicationNon-pathogenic
DomainArchaebacteria
PhylumEuryarchaeota
ClassificationFamily: Thermococcaceae
Order: Thermococcales
Class: Thermococci or Protoarchaea
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI)186497
Genome Information
Gene BankAE009950
EMBLAE009950
Gene Information
Gene NamePF0156
NCBI Gene ID1467988
Protein information
Protein NameAglB 
UniProtKB/ SwissProt IDQ8U4D2
NCBI Ref SeqNC_003413.1.
UniProtKB Sequence>tr|Q8U4D2|Q8U4D2_PYRFU Oligosaccharyl transferase stt3 subunit related protein OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) GN=PF0156 PE=1 SV=1 MVKTQIKEKKKDEKVTIPLPGKIKTVLAFLVVLAFAAYGFYIRHLTAGKYFSDPDTFYHF EIYKLVLKEGLPRYYPMADAPFGSLIGEPLGLYILPAIFYKIISIFGYNELEAFLLWPPF VGFLSVIGVYLLGRKVLNEWAGMWGAIILSVLTANFSRTFSGNARGDGPFMMLFTFSAVL MLYYLTEENKNKKIIWGTLFVLLAGISTAAWNGSPFGLMVLLGFASFQTIILFIFGKINE LREFIKEYYPAYLGILAISYLLTIPGIGKIGGFVRFAFEVFLGLVFLAIVMLYGGKYLNY SDKKHRFAVVAVIVIAGFAGAYIYVGPKLFTLMGGAYQSTQVYETVQELAKTDWGDVKVY YGVEKPNGIVFFLGLVGAMIVTARYLYKLFKDGRRPHEELFAITFYVMSIYLLWTAARFL FLASYAIALMSGVFAGYVLETVEKMKESIPIKAALGGVIAIMLLLIPLTHGPLLAQSAKS MRTTEIETSGWEDALKWLRENTPEYSTATSWWDYGYWIESSLLGQRRASADGGHARDRDH ILALFLARDGNISEVDFESWELNYFLVYLNDWAKFNAISYLGGAITRREYNGDESGRGAV TTLLPLPRYGEKYVNLYAKVIVDVSNSSVKVTVGDRECDPLMVTFTPSGKTIKGTGTCSD GNAFPYVLHLTPTIGVLAYYKVATANFIKLAFGVPASTIPGFSDKLFSNFEPVYESGNVI VYRFTPFGIYKIEENINGTWKQVYNLTPGKHELKLYISAFGRDIENATLYIYAINNEKII EKIKIAEISHMDYLNEYPIAVNVTLPNATSYRFVLVQKGPIGVLLDAPKVNGEIRSPTNI LREGESGEIELKVGVDKDYTADLYLRATFIYLVRKSGKDNEDYDAAFEPQMDVFFITKIG ENIQLKEGENTVKVRAELPEGVISSYKDELQRKYGDKLIIRGIRVEPVFIAEKEYLMLEV SASAPHH
EMBL CDSAAL80280.1
Sequence length967 AA
Subcellular LocationMembrane (Integral component of membrane)
String186497.PF0156.
Potential Application1) Design of OST mutational variants could be use for the production of homogeneous glycoproteins in engineered mammalian and Escherichia coli cells.
Additional Information1) Pyrococcus furiosus OST contains a newly identified conserved motif DxxK (DK motif), which is located very close to the conserved WWDYG motif in the tertiary structure.
PDB ID 2ZAG 2ZAI
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.99.18.5243.
Mechanism of Glycan TransferEn bloc
Donor TypeLipid linked sugars
Donor SpecificityDolPP-Heptasaccharide
Glycan Information
Glycan transferredHeptasaccharide (one hexouronate and two pentose residues) 
Method of Glycan IndentificationMALDI-QIT-TOF MS
Experimental_strategiesIn vitro 
Acceptor Subtrate Information
Acceptor Substrate name Polypeptide containing N-X-S/T consensus sequence
Litrature
Year Of Validation2007 
Reference Igura, M., Maita, N., Obita, T., Kamishikiryo, J., Maenaka, K., & Kohda, D. (2007). Purification, crystallization and preliminary X?ray diffraction studies of the soluble domain of the oligosaccharyltransferase STT3 subunit from the thermophilic archaeon Pyrococcus furiosus. Acta Crystallographica Section F, 63(9), 798-801.

Authors Igura, M., Maita, N., Obita, T., Kamishikiryo, J., Maenaka, K., & Kohda, D.
Research groupsDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Corresponding Author Kohda, D.
ContactsDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Reference Igura, M., Maita, N., Kamishikiryo, J., Yamada, M., Obita, T., Maenaka, K., & Kohda, D. (2008). Structure?guided identification of a new catalytic motif of oligosaccharyltransferase. The EMBO journal, 27(1), 234-243.

Authors Igura, M., Maita, N., Kamishikiryo, J., Yamada, M., Obita, T., Maenaka, K., & Kohda, D.
Research groupsDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Corresponding Author Kohda, D.
ContactsDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Reference Igura, M., & Kohda, D. (2011). Selective control of oligosaccharide transfer efficiency for the N-glycosylation sequon by a point mutation in oligosaccharyltransferase. Journal of Biological Chemistry, jbc-M110.

Authors Igura, M., & Kohda, D.
Research groupsDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku,Fukuoka 812-8582, Japan
Corresponding Author Kohda, D.
ContactsDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku,Fukuoka 812-8582, Japan