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
Classification Phylum : Euryarchaeota
Class : Archaeoglobi
Orders : Archaeoglobales
Family : Archaeoglobaceae
Genus : Archaeoglobus
Species : fulgidus
Strain : ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126
Taxonomic ID (NCBI)224325
Genome Information
Gene BankAE000782.1
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.
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. and 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.

Corresponding AuthorDivision 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. and Kohda, D., 2013. Crystallographic and NMR evidence for flexibility in oligosaccharyltransferases and its catalytic significance. Structure, 21(1), pp.32-41.

Corresponding AuthorDivision 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.

Corresponding AuthorDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Reference Matsumoto, S., Shimada, A., Nyirenda, J., Igura, M., Kawano, Y. and 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), pp.17868-17873.

Corresponding AuthorDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan
Reference Fujinami, D., Nyirenda, J., Matsumoto, S. and Kohda, D., 2015. Structural elucidation of an asparagine-linked oligosaccharide from the hyperthermophilic archaeon, Archaeoglobus fulgidus. Carbohydrate research, 413, pp.55-62.

Corresponding AuthorDivision of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan