1 Proteins
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Medtr1501s0010.1 | A0A072TE38 | PAC:31105882 | Medicago truncatula |
430
 |
| Type: | Family | Name: | Hopanoid biosynthesis associated glycosyltransferase, HpnI |
| Description: | Proteins in this entry contain glycosyl transferase family 2 domains which are responsible, generally, for the transfer of nucleotide-diphosphate sugars to substrates such as polysaccharides and lipids. The Acidithiobacillus ferrooxidans ATCC 23270protein (AFE_0974) is encoded in the same locus as the genes for squalene-hopene cyclase (SHC, ) and other proteins associated with the biosynthesis of hopanoid natural products. Similarly, in Ralstonia eutropha(strain JMP134) (Alcaligenes eutrophus) this protein (Reut_B4902) is encoded adjacent to the genes for HpnAB, IspH and HpnH (), although SHC itself is encoded elsewhere in the genome. Notably, this protein (here named HpnI) and three others form a conserved set (HpnIJKL) which occurs in a subset of all genomes containing the SHC enzyme. This relationship was discerned using the method of partial phylogenetic profiling []. This group includes Zymomonas mobilis, the organism where the initial hopanoid biosynthesis locus was described consisting of the genes HpnA-E and SHC (HpnF) []. Continuing past SHC are found genes for a phosphorylase enzyme (ZMO0873, i.e. HpnG, ) and another radical SAM enzyme (ZMO0874), HpnH. Although discontinuous in Z. mobilis, we continue the gene symbol sequence with HpnIJKL. Hopanoids are known to feature polar glycosyl head groups in many organisms. | Short Name: | Hopen-assoc_HpnI |
| DB identifier | UniProt Accession | Secondary Identifier | Organism Name | Length |
|---|---|---|---|---|
| Medtr1501s0010.1 | A0A072TE38 | PAC:31105882 | Medicago truncatula |
430
|
