Species | Pauljensenia sp902373545 | |||||||||||
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Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Actinomycetaceae; Pauljensenia; Pauljensenia sp902373545 | |||||||||||
CAZyme ID | MGYG000001285_00312 | |||||||||||
CAZy Family | GT0 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 5770; End: 7044 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0438 | RfaB | 1.23e-12 | 88 | 423 | 6 | 379 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd03801 | GT4_PimA-like | 7.94e-12 | 87 | 408 | 3 | 355 | phosphatidyl-myo-inositol mannosyltransferase. This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct 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. The members of this family are found mainly in certain bacteria and archaea. |
cd03809 | GT4_MtfB-like | 0.004 | 280 | 413 | 214 | 359 | glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AKU65238.1 | 9.65e-275 | 1 | 423 | 1 | 423 |
QQC44076.1 | 5.57e-274 | 1 | 423 | 1 | 423 |
QYB16392.1 | 1.55e-194 | 14 | 422 | 14 | 422 |
QAY74590.1 | 2.68e-163 | 56 | 424 | 43 | 411 |
SEB00738.1 | 3.64e-153 | 18 | 422 | 2 | 397 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
2X0E_A | 5.66e-07 | 165 | 361 | 134 | 351 | Complexstructure of WsaF with dTDP [Geobacillus stearothermophilus],2X0E_B Complex structure of WsaF with dTDP [Geobacillus stearothermophilus],2X0F_A Structure of WsaF in complex with dTDP-beta-L-Rha [Geobacillus stearothermophilus],2X0F_B Structure of WsaF in complex with dTDP-beta-L-Rha [Geobacillus stearothermophilus] |
2X0D_A | 1.32e-06 | 165 | 361 | 134 | 351 | APOstructure of WsaF [Geobacillus stearothermophilus],2X0D_B APO structure of WsaF [Geobacillus stearothermophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q50864 | 8.72e-26 | 165 | 408 | 992 | 1243 | O-antigen biosynthesis protein RfbC OS=Myxococcus xanthus OX=34 GN=rfbC PE=4 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000041 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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