| Species | Coprobacter secundus | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Coprobacteraceae; Coprobacter; Coprobacter secundus | |||||||||||
| CAZyme ID | MGYG000001512_01991 | |||||||||||
| CAZy Family | GT10 | |||||||||||
| CAZyme Description | Alpha-(1,3)-fucosyltransferase FucT | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 1292381; End: 1293325 Strand: - | |||||||||||
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT10 | 99 | 246 | 2.5e-47 | 0.4322766570605187 |
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| pfam18025 | FucT_N | 2.67e-48 | 6 | 97 | 1 | 92 | Alpha-(1,3)-fucosyltransferase FucT N-terminal domain. This is the N-terminal domain of the alpha chain found in Helicobacter pylori Fucosyltransferase protein which is involved in the production of Lewis x trisaccharide, a major component of lipopolysaccharide. The N-terminal domain contains the catalyst base, Glu-95 which is equivalent to the Asp-100 of other members of the glycosyltransferases-B family. The domain contains the pocket where LacNAc binds. The domain is composed of 2-10 heptad repeats and a conserved N-terminal alpha-beta-alpha motif which has little sequence similarity to the conserved N-terminal motif in other glycosyltransferases. |
| pfam00852 | Glyco_transf_10 | 1.32e-25 | 115 | 280 | 1 | 159 | Glycosyltransferase family 10 (fucosyltransferase) C-term. This is the C-terminal domain of a family of fucosyltransferases. This enzyme transfers fucose from GDP-Fucose to GlcNAc in an alpha1,3 linkage. This family is known as glycosyltransferase family 10. The C-terminal domain is the likely binding-region for ADP (manuscript in publication). |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| BCI63450.1 | 2.24e-238 | 1 | 314 | 1 | 314 |
| QCT79965.1 | 1.79e-120 | 1 | 294 | 1 | 294 |
| CAH09151.1 | 2.69e-120 | 1 | 294 | 13 | 306 |
| QCQ38686.1 | 5.41e-120 | 1 | 294 | 13 | 306 |
| QCQ56021.1 | 1.80e-118 | 1 | 293 | 1 | 294 |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2NZW_A | 4.51e-54 | 18 | 287 | 43 | 354 | CrystalStructure of alpha1,3-Fucosyltransferase [Helicobacter pylori],2NZW_B Crystal Structure of alpha1,3-Fucosyltransferase [Helicobacter pylori],2NZW_C Crystal Structure of alpha1,3-Fucosyltransferase [Helicobacter pylori],2NZX_A Crystal Structure of alpha1,3-Fucosyltransferase with GDP [Helicobacter pylori],2NZX_B Crystal Structure of alpha1,3-Fucosyltransferase with GDP [Helicobacter pylori],2NZX_C Crystal Structure of alpha1,3-Fucosyltransferase with GDP [Helicobacter pylori],2NZY_A Crystal Structure of alpha1,3-Fucosyltransferase with GDP-fucose [Helicobacter pylori],2NZY_B Crystal Structure of alpha1,3-Fucosyltransferase with GDP-fucose [Helicobacter pylori],2NZY_C Crystal Structure of alpha1,3-Fucosyltransferase with GDP-fucose [Helicobacter pylori] |
| 5ZOI_A | 3.04e-52 | 18 | 287 | 43 | 354 | CrystalStructure of alpha1,3-Fucosyltransferase [Helicobacter pylori],5ZOI_B Crystal Structure of alpha1,3-Fucosyltransferase [Helicobacter pylori] |
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| O30511 | 2.71e-52 | 18 | 287 | 43 | 354 | Alpha-(1,3)-fucosyltransferase FucT OS=Helicobacter pylori OX=210 GN=fucT PE=1 SV=1 |
| Q5UQ63 | 5.54e-26 | 115 | 248 | 423 | 566 | Putative fucosyltransferase R654 OS=Acanthamoeba polyphaga mimivirus OX=212035 GN=MIMI_R654 PE=3 SV=1 |
| Q8BHC9 | 1.54e-13 | 65 | 246 | 162 | 348 | Alpha-(1,3)-fucosyltransferase 11 OS=Mus musculus OX=10090 GN=Fut11 PE=1 SV=1 |
| Q68FV3 | 2.08e-13 | 65 | 246 | 167 | 353 | Alpha-(1,3)-fucosyltransferase 11 OS=Rattus norvegicus OX=10116 GN=Fut11 PE=2 SV=1 |
| Q70AG8 | 2.10e-13 | 105 | 246 | 202 | 359 | Alpha-(1,3)-fucosyltransferase 11 OS=Takifugu rubripes OX=31033 GN=fut11 PE=2 SV=1 |
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000044 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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