Species | Bacteroides sp900553815 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp900553815 | |||||||||||
CAZyme ID | MGYG000004185_01297 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 86725; End: 87870 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13528 | Glyco_trans_1_3 | 1.78e-20 | 1 | 329 | 1 | 317 | Glycosyl transferase family 1. |
cd03785 | GT28_MurG | 5.15e-06 | 2 | 330 | 1 | 319 | 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. |
COG1819 | YjiC | 1.58e-04 | 1 | 147 | 2 | 136 | UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]. |
cd03784 | GT1_Gtf-like | 0.002 | 281 | 324 | 319 | 362 | 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 |
---|---|---|---|---|---|
QUT36420.1 | 5.53e-198 | 1 | 354 | 1 | 354 |
QQA28359.1 | 5.53e-198 | 1 | 354 | 1 | 354 |
QUT63690.1 | 5.53e-198 | 1 | 354 | 1 | 354 |
QUT67777.1 | 9.12e-197 | 1 | 354 | 1 | 354 |
QMI81438.1 | 1.29e-196 | 1 | 354 | 1 | 354 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000064 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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