ProGT53 (AglB)
ProGT ID | ProGT53 (AglB) |
Organism Information | |
Organism Name | Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126) |
Domain | Archaebacteria |
Phylum | Euryarchaeota |
Classification | Family: Archaeoglobaceae Order: Archaeoglobales Class: Archaeoglobi Division or phylum: "Euryarchaeota" |
Taxonomic ID (NCBI) | 224325 |
Genome Information | |
Gene Bank | AE000782 |
EMBL | AE000782 |
Gene Information | |
Gene Name | aglB (AF_0380) |
NCBI Gene ID | 24793919 |
NCBI Reference Sequence | AAB90856.1 |
Protein information | |
Protein Name | AglB |
UniProtKB/ SwissProt ID | O29867 |
NCBI Ref Seq | WP_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 CDS | AAB90856.1 |
Sequence length | 868 AA |
Subcellular Location | Membrane (Integral component of membrane) |
String | 224325.AF0380 |
Additional Information | 1) 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 Type | N- (Asn) linked |
CAZY Family | GT66 |
EC Number (BRENDA) | 2.4.99.18 414 |
Mechanism of Glycan Transfer | En bloc |
Glycan Information | |
Method of Glycan Indentification | LC-ESI-MS, NMR |
Experimental_strategies | In vitro |
Acceptor Subtrate Information | |
Acceptor Substrate name | NH2-Ala-Ala-Tyr-Asn-Val-Thr-Lys-Arg-(Lys-TAMRA) |
Litrature | |
Year Of Validation | 2012 |
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 groups | Division of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan |
Corresponding Author | Kohda, D., |
Contacts | Division 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 groups | Division of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan |
Corresponding Author | Kohda, D. |
Contacts | Division 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 groups | Division of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan |
Corresponding Author | Kohda, D. |
Contacts | Division 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 groups | Division of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan |
Corresponding Author | Kohda, D. |
Contacts | Division 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 groups | Division of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan |
Corresponding Author | Kohda, D. |
Contacts | Division of Structural Biology, Kyushu University, Maidashi 3-1-1, Fukuoka 812-8582, Japan |