Latest update: September 24, 2018


ProGT53 (AglB)

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ProGT ID ProGT53 (AglB)
Organism Information
Organism NameArchaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
DomainArchaebacteria
PhylumEuryarchaeota
ClassificationFamily: Archaeoglobaceae
Order: Archaeoglobales
Class: Archaeoglobi
Division or phylum: "Euryarchaeota"
Taxonomic ID (NCBI)224325
Genome Information
Gene BankAE000782
EMBLAE000782
Gene Information
Gene NameaglB (AF_0380)
NCBI Gene ID24793919
NCBI Reference SequenceAAB90856.1
Protein information
Protein NameAglB 
UniProtKB/ SwissProt IDO29867
NCBI Ref SeqWP_010877887.1
UniProtKB Sequence>tr|O29867|O29867_ARCFU Transmembrane oligosaccharyl transferase, putative OS=Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) GN=AF_0380 PE=1 SV=1 MQNAESWFKKYWHLSVLVIAALISVKLRILNPWNSVFTWTVRLGGNDPWYYYRLIENTIH NFPHRIWFDPFTYYPYGSYTHFGPFLVYLGSIAGIIFSATSGESLRAVLAFIPAIGGVLA ILPVYLLTREVFDKRAAVIAAFLIAIVPGQFLQRSILGFNDHHIWEAFWQVSALGTFLLA YNRWKGHDLSHNLTARQMAYPVIAGITIGLYVLSWGAGFIIAPIILAFMFFAFVLAGFVN ADRKNLSLVAVVTFAVSALIYLPFAFNYPGFSTIFYSPFQLLVLLGSAVIAAAFYQIEKW NDVGFFERVGLGRKGMPLAVIVLTALIMGLFFVISPDFARNLLSVVRVVQPKGGALTIAE VYPFFFTHNGEFTLTNAVLHFGALFFFGMAGILYSAYRFLKRRSFPEMALLIWAIAMFIA LWGQNRFAYYFAAVSAVYSALALSVVFDKLHLYRALENAIGARNKLSYFRVAFALLIALA AIYPTYILADAQSSYAGGPNKQWYDALTWMRENTPDGEKYDEYYLQLYPTPQSNKEPFSY PFETYGVISWWDYGHWIEAVAHRMPIANPFQAGIGNKYNNVPGASSFFTAENESYAEFVA EKLNVKYVVSDIEMETGKYYAMAVWAEGDLPLAEKYYGGYFYYSPTGTFGYANSQWDIPL NSIIIPLRIPSELYYSTMEAKLHLFDGSGLSHYRMIYESDYPAEWKSYSSQVNLNNESQV LQTALYEAVMRARYGVSPTMGTQEVLYKYAYTQLYEKKMGIPVKIAPSGYVKIFERVKGA VVTGKVSANVTEVSVNATIKTNQNRTFEYWQTVEVKNGTYTVVLPYSHNSDYPVKPITPY HIKAGNVVKEITIYESQVQNGEIIQLDL
EMBL CDSAAB90856.1
Sequence length868 AA
Subcellular LocationMembrane (Integral component of membrane)
String224325.AF0380
Additional Information1) The Archaeoglobus AglB lacked a beta- barrel-like structure, which had been found in other AglB and PglB structures.
2) AfAglB uses acceptor substrate NH2?Ala-Ala-Tyr-Asn-Val-Thr-Lys-Arg-(Lys-TAMRA) for in vitro assay.
3) Single oligosaccharide chain comprising four Hex and three dHex (2590.1361 Da) were transferred but detailed chemical structure of glycan not known.
PDB ID 3VGP 3VU0 3WAI 3WAJ 3WAK 5GMY
Glycosyltransferase Information
Glycosylation TypeN- (Asn) linked 
CAZY FamilyGT66
EC Number (BRENDA)2.4.99.18 414
Mechanism of Glycan TransferEn bloc
Glycan Information
Method of Glycan IndentificationLC-ESI-MS, NMR
Experimental_strategiesIn vitro 
Acceptor Subtrate Information
Acceptor Substrate name NH2-Ala-Ala-Tyr-Asn-Val-Thr-Lys-Arg-(Lys-TAMRA)
Litrature
Year Of Validation2012 
Reference Matsumoto, S., Igura, M., Nyirenda, J., Matsumoto, M., Yuzawa, S., Noda, N., Inagaki, F. & Kohda, D., (2012). Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 Å resolution. Biochemistry, 51(20), pp.4157-4166.

Authors Matsumoto, S., Igura, M., Nyirenda, J., Matsumoto, M., Yuzawa, S., Noda, N., Inagaki, F. & Kohda, D.,
Research groupsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Corresponding Author Kohda, D.,
ContactsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Reference Nyirenda, J., Matsumoto, S., Saitoh, T., Maita, N., Noda, N. N., Inagaki, F., & Kohda, D. (2013). Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance. Structure, 21(1), 32-41.

Authors Nyirenda, J., Matsumoto, S., Saitoh, T., Maita, N., Noda, N. N., Inagaki, F., & Kohda, D.
Research groupsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Corresponding Author Kohda, D.
ContactsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Reference Matsumoto, S., Shimada, A., & Kohda, D. (2013). Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases. BMC structural biology, 13(1), 11.

Authors Matsumoto, S., Shimada, A., & Kohda, D.
Research groupsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Corresponding Author Kohda, D.
ContactsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Reference Matsumoto, S., Shimada, A., Nyirenda, J., Igura, M., Kawano, Y., & Kohda, D. (2013). Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation. Proceedings of the National Academy of Sciences, 110(44), 17868-17873.

Authors Matsumoto, S., Shimada, A., Nyirenda, J., Igura, M., Kawano, Y., & Kohda, D.
Research groupsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Corresponding Author Kohda, D.
ContactsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Reference Fujinami, D., Matsumoto, M., Noguchi, T., Sonomoto, K., & Kohda, D. (2014). Structural elucidation of an asparagine-linked oligosaccharide from the hyperthermophilic archaeon, Pyrococcus furiosus. Carbohydrate research, 387, 30-36.

Authors Fujinami, D., Matsumoto, M., Noguchi, T., Sonomoto, K., & Kohda, D.
Research groupsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Corresponding Author Kohda, D.
ContactsDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan