| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; | |||||||||||
| CAZyme ID | MGYG000004239_00234 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 69284; End: 70489 Strand: + | |||||||||||
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03794 | GT4_WbuB-like | 1.57e-70 | 19 | 396 | 19 | 391 | Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase. |
| PRK10307 | PRK10307 | 6.42e-21 | 101 | 387 | 109 | 393 | colanic acid biosynthesis glycosyltransferase WcaI. |
| cd03801 | GT4_PimA-like | 1.80e-19 | 22 | 400 | 22 | 366 | 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. |
| cd03817 | GT4_UGDG-like | 1.27e-11 | 161 | 397 | 142 | 371 | UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol. |
| pfam13579 | Glyco_trans_4_4 | 5.96e-07 | 22 | 198 | 9 | 157 | Glycosyl transferase 4-like domain. |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AIY06294.1 | 5.92e-121 | 1 | 399 | 1 | 399 |
| QQS99762.1 | 1.31e-120 | 1 | 400 | 1 | 403 |
| QEL71359.1 | 3.91e-117 | 1 | 399 | 1 | 402 |
| QEL76637.1 | 3.91e-117 | 1 | 399 | 1 | 402 |
| ASL68027.1 | 3.91e-117 | 1 | 399 | 1 | 402 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q8KIU8 | 1.66e-17 | 68 | 386 | 67 | 378 | Probable glycosyltransferase WbjE OS=Pseudomonas aeruginosa OX=287 GN=wbjE PE=3 SV=2 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000079 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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