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CAZyme Information: MGYG000004645_01508
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; QALW01; UMGS1322; | |||||||||||
| CAZyme ID | MGYG000004645_01508 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | hypothetical protein | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 11047; End: 12279 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03801 | GT4_PimA-like | 6.11e-07 | 55 | 408 | 11 | 365 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AGF59168.1 | 1.90e-127 | 6 | 397 | 14 | 404 |
| QMW77448.1 | 4.07e-110 | 34 | 377 | 579 | 925 |
| QIB58016.1 | 4.07e-110 | 34 | 377 | 579 | 925 |
| QBE99399.1 | 5.07e-110 | 34 | 377 | 573 | 919 |
| QJU15227.1 | 5.07e-110 | 34 | 377 | 573 | 919 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2X0E_A | 1.38e-107 | 8 | 377 | 16 | 380 | 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 | 4.42e-106 | 8 | 377 | 16 | 380 | APOstructure of WsaF [Geobacillus stearothermophilus],2X0D_B APO structure of WsaF [Geobacillus stearothermophilus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| Q50864 | 2.24e-17 | 29 | 381 | 899 | 1227 | O-antigen biosynthesis protein RfbC OS=Myxococcus xanthus OX=34 GN=rfbC PE=4 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000075 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |