Species | Streptococcus agalactiae | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus agalactiae | |||||||||||
CAZyme ID | MGYG000002349_01626 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 76058; End: 77269 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG1819 | YjiC | 4.30e-11 | 1 | 401 | 1 | 402 | UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]. |
cd03784 | GT1_Gtf-like | 3.50e-05 | 3 | 394 | 2 | 404 | 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. |
COG0707 | MurG | 7.93e-05 | 240 | 396 | 184 | 357 | UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]. |
pfam00201 | UDPGT | 0.003 | 303 | 399 | 345 | 442 | UDP-glucoronosyl and UDP-glucosyl transferase. |
cd03785 | GT28_MurG | 0.005 | 238 | 358 | 179 | 318 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ARC45545.1 | 3.68e-298 | 1 | 403 | 1 | 403 |
AIX04458.1 | 3.68e-298 | 1 | 403 | 1 | 403 |
AIK73379.1 | 3.68e-298 | 1 | 403 | 1 | 403 |
AIK71254.1 | 3.68e-298 | 1 | 403 | 1 | 403 |
CAD46298.1 | 3.68e-298 | 1 | 403 | 1 | 403 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000042 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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