Species | Exiguobacterium sp003467445 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Exiguobacterales; Exiguobacteraceae; Exiguobacterium; Exiguobacterium sp003467445 | |||||||||||
CAZyme ID | MGYG000000264_01658 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 97907; End: 100078 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03801 | GT4_PimA-like | 2.14e-21 | 374 | 713 | 22 | 364 | 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. |
cd03811 | GT4_GT28_WabH-like | 2.13e-14 | 440 | 645 | 85 | 286 | family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core. |
COG0438 | RfaB | 1.66e-11 | 453 | 713 | 123 | 373 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
COG0438 | RfaB | 1.18e-10 | 7 | 383 | 2 | 374 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd03801 | GT4_PimA-like | 3.89e-10 | 148 | 383 | 131 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
ACQ69993.1 | 0.0 | 1 | 723 | 1 | 727 |
QPI68332.1 | 0.0 | 1 | 723 | 1 | 727 |
QUE87297.1 | 0.0 | 6 | 717 | 5 | 714 |
ACK92434.1 | 1.08e-219 | 4 | 714 | 3 | 710 |
AJH89385.1 | 1.23e-218 | 4 | 714 | 3 | 710 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000055 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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