Species | Ruminococcus_D bicirculans | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_D; Ruminococcus_D bicirculans | |||||||||||
CAZyme ID | MGYG000002321_00614 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | Glycosyltransferase Gtf1 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 672222; End: 673256 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
COG0438 | RfaB | 1.12e-20 | 63 | 338 | 87 | 368 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd03801 | GT4_PimA-like | 6.94e-17 | 96 | 340 | 112 | 361 | 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. |
cd04949 | GT4_GtfA-like | 5.89e-14 | 123 | 338 | 115 | 326 | accessory Sec system glycosyltransferase GtfA and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general 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 in bacteria. |
pfam13692 | Glyco_trans_1_4 | 1.09e-13 | 168 | 308 | 1 | 133 | Glycosyl transferases group 1. |
pfam00534 | Glycos_transf_1 | 5.97e-11 | 167 | 316 | 1 | 147 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
CCO04323.1 | 2.39e-255 | 1 | 344 | 1 | 344 |
QUF81615.1 | 1.09e-203 | 1 | 343 | 1 | 343 |
AXH51535.1 | 1.27e-132 | 1 | 344 | 3 | 345 |
AQW22832.1 | 4.63e-132 | 1 | 344 | 1 | 343 |
QBE94676.1 | 4.87e-127 | 1 | 344 | 1 | 342 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5E9T_A | 4.34e-08 | 123 | 310 | 273 | 464 | Crystalstructure of GtfA/B complex [Streptococcus gordonii],5E9T_C Crystal structure of GtfA/B complex [Streptococcus gordonii],5E9U_A Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_C Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_E Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_G Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9AET5 | 4.30e-08 | 123 | 310 | 273 | 464 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit OS=Streptococcus gordonii OX=1302 GN=gtfA PE=1 SV=2 |
Q3S2Y2 | 1.79e-07 | 121 | 332 | 270 | 479 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit OS=Streptococcus agalactiae OX=1311 GN=gtfA PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000063 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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