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CAZyme Information: MGYG000004167_00457
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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; Bacilli; RF39; UBA660; CAG-884; | |||||||||||
| CAZyme ID | MGYG000004167_00457 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 49740; End: 51014 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| COG0438 | RfaB | 4.68e-28 | 33 | 419 | 21 | 381 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| cd03801 | GT4_PimA-like | 1.27e-27 | 46 | 413 | 36 | 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. |
| pfam00534 | Glycos_transf_1 | 8.97e-23 | 237 | 394 | 15 | 158 | Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. |
| pfam13692 | Glyco_trans_1_4 | 3.90e-20 | 227 | 380 | 5 | 138 | Glycosyl transferases group 1. |
| cd03817 | GT4_UGDG-like | 2.35e-17 | 90 | 396 | 82 | 357 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AOW11195.1 | 1.81e-117 | 1 | 417 | 1 | 418 |
| QNT15357.1 | 3.91e-110 | 1 | 416 | 1 | 412 |
| QEL87780.1 | 1.42e-108 | 1 | 415 | 1 | 418 |
| QGV06202.1 | 4.57e-107 | 1 | 415 | 1 | 418 |
| AXR19908.1 | 4.57e-107 | 1 | 415 | 1 | 418 |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P39859 | 2.22e-06 | 246 | 357 | 203 | 319 | Protein CapJ OS=Staphylococcus aureus OX=1280 GN=capJ 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 |
|---|---|---|---|---|---|
| 1.000080 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |