| ProGT ID | ProGT80.9 (AglM) |
| Organism Information | |
| Organism Name | Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) |
| Domain | Archaebacteria |
| Classification | Phylum : Euryarchaeota Class : Halobacteria Orders : Halobacteriales Family : Halobacteriaceae Genus : Halobacterium Species : salinarum Strain : strain ATCC 700922 / JCM 11081 / NRC-1 |
| Taxonomic ID (NCBI) | 64091 |
| Genome Information | |
| Gene Bank | AE004437.1 |
| EMBL | AE004437.1 |
| Gene Information | |
| Gene Name | aglM |
| NCBI Gene ID | 1447756 |
| NCBI Reference Sequence | NC_002607.1. |
| Protein information | |
| Protein Name | AglM |
| UniProtKB/ SwissProt ID | Q9HQQ9 |
| NCBI Ref Seq | WP_010902749.1. |
| UniProtKB Sequence | >tr|Q9HQQ9|Q9HQQ9_HALSA UDP-glucose dehydrogenase OS=Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) GN=udg1 PE=3 SV=1 MDVSIVGSGYVGTTIAACFAELGHTVVNVDVDADVVAAINDGDAPIHEPGLAERIDAHAG TRLRATTDYEAVRDTDVTFLALPTPAREDGSIDTSIMESGAASLGEALAGADDHMVVVKS TVVPGTTEDVVESALVSAGFDDPLLAMNPEFLRMGSAVDDFRHPDKVVFGARRDAAYDQL HAVFEPLLADAGDATVVETGLREAEMIKYANNAFLASKVSLINDLGNICKELGVDAYEVA DAIAEDDRISGRFLRSGVGWGGSCFPKDVAAITAAAKDAGYEPAMLEAAVEVNDRQPERL LSLLDGHVDVAGERVAVLGLSFKPGTDDIRGTRAVPVIDGLQDREADVVAYDPVAAEKMA EQRPEVTYADSAAGALADAVGAVVVTDWDEFAALDDEFDAMAERVVVDGRRVVDPQADLT YDGLTW |
| EMBL CDS | AAG19454.1. |
| Sequence length | 426 AA |
| String | 64091.VNG1048G. |
| Glycosylation Information | |
| CAZY Family | Non-GT |
| Acceptor Substrate Specificity | UDP-Glc |
| Experimental Validation | In vivo |
| Product | UDP-glucuronic acid |
| Function in Glycosylation pathway | 1) It is a UDP-glucose dehydrogenase. |
| Additional Information | 1) aglM gene in Hfx. volcanii can be functionally replaced by their Hbt. Salinarum homolog. 2) It transform UDP-glucose into UDP-glucuronic acid in a NAD(+)-dependent manner. |
| Litrature | |
| Year Of Validation | 2015 |
| Reference | Kandiba, L. and Eichler, J., 2015. Deciphering a pathway of Halobacterium salinarum N?glycosylation. MicrobiologyOpen, 4(1), pp.28-40. |
| Corresponding Author | Department of Life Sciences, Ben Gurion University of the Negev, Beersheva, Israel. |