| ProGT ID | ProGT15.2 (AglE) |
| Organism Information | |
| Organism Name | Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 /DS2) |
| Domain | Archaebacteria |
| Classification | Phylum : Euryarchaeota Class : Halobacteria Orders : Haloferacales Family : Haloreacaceae Genus : Haloferax Species : volcanii Strain : strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 /DS2 |
| Taxonomic ID (NCBI) | 309800 |
| Genome Information | |
| Gene Bank | CP001956.1 |
| EMBL | CP001956.1 |
| Gene Information | |
| Gene Name | aglE |
| NCBI Reference Sequence | NZ_AOHU01000097.1. |
| Protein information | |
| Protein Name | AglE |
| UniProtKB/ SwissProt ID | D4GYG6 |
| UniProtKB Sequence | >sp|D4GYG6|AGLQ_HALVD Archaeal glycosylation protein Q OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) GN=aglQ PE=1 SV=1 MTSLSDILASSAEAGLSLQRSDGSMPAGHNGPYHDPETPVRNTSHWLVTFLKAHELTDEN RFRQAASDAVSYLLSEEARPHGHTFEHRQNDTKDRCNGLMGQAWSLEALALAARALDNER AAAVAADVFLSHPFCDKLKLWQRVDTDGTILGFDRTFNHQLWFAASGGLVAHTAPQEVSQ RVRDFLDSLPSTIDLYENGLIRHPLRPSMDLSELAESVTHDVHRSMVRNHLLHYLRPPRS KRRLRNKAEGYHSFNLYALAILAREFPSHSVWSTDLLSDILEYTLSEEFREATTDNKFSH PYNPPGFEVPAAMETFSVGSYKEREMWVNEQIQHSFDPNTSLLTRGTDDKQTHAARLYEA TRLDDYEIYLD |
| EMBL CDS | CAW30728.1. |
| Sequence length | 371 AA |
| Subcellular Location | Cytoplasm |
| String | 309800.HVO_1523 |
| Glycosylation Information | |
| CAZY Family | GT2 |
| EC Number (BRENDA) | 2.4.1.- |
| Experimental Validation | In vivo |
| Function in Glycosylation pathway | 1) It is a glycosyltransferase. |
| Additional Information | 1) Deletion in aglE gene show reduction in 190-Da sugar (hexuronic acid) at position four to the N-linked pentasaccharide. |
| Litrature | |
| Year Of Validation | 2008 |
| Reference | Abu-Qarn, M., Yurist-Doutsch, S., Giordano, A., Trauner, A., Morris, H.R., Hitchen, P., Medalia, O., Dell, A. and Eichler, J., 2007. Haloferax volcanii AglB and AglD are involved in N-glycosylation of the S-layer glycoprotein and proper assembly of the surface layer. Journal of molecular biology, 374(5), pp.1224-1236. |
| Corresponding Author | Department of Life Sciences, Ben Gurion University of the Negev, Beersheva, Israel. |