| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Rikenellaceae; Alistipes; | |||||||||||
| CAZyme ID | MGYG000002674_00077 | |||||||||||
| CAZy Family | GT1 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 37832; End: 38911 Strand: - | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam13528 | Glyco_trans_1_3 | 1.31e-29 | 1 | 335 | 1 | 321 | Glycosyl transferase family 1. |
| COG1819 | YjiC | 1.33e-08 | 1 | 306 | 2 | 335 | UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]. |
| cd03785 | GT28_MurG | 5.63e-06 | 2 | 114 | 1 | 96 | undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. |
| cd03784 | GT1_Gtf-like | 3.32e-04 | 1 | 306 | 1 | 342 | UDP-glycosyltransferases and similar proteins. This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AOH41937.1 | 8.85e-119 | 1 | 357 | 1 | 359 |
| AVV54514.1 | 8.85e-119 | 1 | 357 | 1 | 359 |
| BAR48128.1 | 8.35e-117 | 1 | 357 | 15 | 372 |
| BAR50670.1 | 1.55e-115 | 4 | 357 | 1 | 355 |
| AEW22571.1 | 1.55e-115 | 4 | 357 | 1 | 355 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000074 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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