Species | Paraprevotella xylaniphila | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Paraprevotella; Paraprevotella xylaniphila | |||||||||||
CAZyme ID | MGYG000001372_00269 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | Glycogen synthase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 36668; End: 38287 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
TIGR04157 | glyco_rSAM_CFB | 5.68e-116 | 3 | 384 | 1 | 392 | glycosyltransferase, GG-Bacteroidales peptide system. Members of this protein family are predicted glycosyltransferases that occur in conserved gene neighborhoods in various members of the Bacteroidales. These neighborhoods feature a radical SAM enzyme predicted to act in peptide modification (family TIGR04148), peptides from family TIGR04149 with a characteristic GG cleavage motif, and several other proteins. |
cd03801 | GT4_PimA-like | 3.89e-47 | 3 | 393 | 1 | 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. |
COG0438 | RfaB | 4.38e-29 | 2 | 393 | 1 | 370 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
pfam13692 | Glyco_trans_1_4 | 2.25e-27 | 219 | 382 | 1 | 138 | Glycosyl transferases group 1. |
cd03798 | GT4_WlbH-like | 1.57e-25 | 172 | 332 | 151 | 316 | Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BAR47688.1 | 2.72e-83 | 1 | 355 | 1 | 369 |
AEW21924.1 | 3.36e-81 | 1 | 355 | 1 | 370 |
BAR50455.1 | 9.36e-81 | 1 | 355 | 1 | 370 |
AKA53449.1 | 4.62e-79 | 1 | 385 | 1 | 392 |
BAD50795.1 | 4.62e-79 | 1 | 385 | 1 | 392 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3C4Q_A | 1.61e-07 | 165 | 327 | 158 | 340 | Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum] |
3C48_A | 1.65e-07 | 165 | 327 | 178 | 360 | Structureof the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q59002 | 2.15e-15 | 174 | 331 | 151 | 322 | Uncharacterized glycosyltransferase MJ1607 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1607 PE=3 SV=1 |
A7TZT2 | 6.31e-10 | 162 | 327 | 184 | 369 | Mannosylfructose-phosphate synthase OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=mfpsA PE=1 SV=1 |
Q4JSW2 | 1.76e-09 | 165 | 382 | 158 | 405 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium jeikeium (strain K411) OX=306537 GN=mshA PE=3 SV=1 |
Q65CC7 | 3.65e-09 | 221 | 386 | 209 | 370 | Alpha-D-kanosaminyltransferase OS=Streptomyces kanamyceticus OX=1967 GN=kanE PE=1 SV=1 |
O05083 | 7.41e-09 | 220 | 382 | 182 | 339 | Uncharacterized glycosyltransferase HI_1698 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1698 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000075 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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