ProGT ID | ProGT15.15 (Agl9) |
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 | agl9 |
NCBI Gene ID | 8925606 |
NCBI Reference Sequence | NZ_AOHU01000097.1. |
Protein information | |
Protein Name | Agl9 |
UniProtKB/ SwissProt ID | D4GU62 |
NCBI Ref Seq | WP_004041934.1. |
UniProtKB Sequence | >sp|D4GU62|AGL9_HALVD Low-salt glycan biosynthesis hexosyltransferase Agl9 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) GN=agl9 PE=3 SV=1 MSSDYSNISELIEEEYNNSKSVGIFVSRFDKSEGVGTVVNRHISELNDAGIDVTLFAYEQ VDEIAEKKVVNVSSSLTGNNTLNKLISSMNPLKWLSLSSELKKLDLLIVHQPILCSIAYY AQKIHDIDTIYYNHEVTRPEDKVGTIQRIYGYTLFQIYLHISSRLDQIVSVSKYSQQEYS RRFDRQGMVIHNSIDHEMYNQSVDGSRIREKYDLEDDPLVLFVGRIAKSKGIHRLISVFE DVSKTIPDATLVIVGRPDNQGYYQRVKVLSKSVDQQIIFAGIVPEEDLPAYYSAADLYAT CSIKEGYNLTIAEAEACGTPTIAFDIGAHSEVMNDGVLVPKDNTSLFKEEMVSQLTKQR |
EMBL CDS | ADE05081.1 |
Sequence length | 359 AA |
String | 309800.HVO_2048. |
Glycosylation Information | |
CAZY Family | GT4 |
EC Number (BRENDA) | 2.4.1.- |
Experimental Validation | In vivo |
Function in Glycosylation pathway | 1) It functions as hexosyltransferase. |
Additional Information | 1) Deletion of Agl9 results in loss of the last two sugars of the tetrasaccharide added to the S-layer glycoprotein. |
Litrature | |
Year Of Validation | 2013 |
Reference | Kaminski, L., Guan, Z., Yurist-Doutsch, S. and Eichler, J., 2013. Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity. MBio, 4(6), pp.e00716-13. |
Corresponding Author | Department of Life Sciences, Ben Gurion University of the Negev, Beersheva, Israel. |