Species | RC9 sp000432515 | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; UBA932; RC9; RC9 sp000432515 | |||||||||||
CAZyme ID | MGYG000004402_00622 | |||||||||||
CAZy Family | GT94 | |||||||||||
CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 56584; End: 57705 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT94 | 108 | 304 | 9.6e-22 | 0.6537102473498233 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03822 | GT4_mannosyltransferase-like | 1.23e-37 | 2 | 361 | 1 | 360 | mannosyltransferases of glycosyltransferase family 4 and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides. |
COG0438 | RfaB | 3.57e-25 | 1 | 373 | 1 | 377 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd03801 | GT4_PimA-like | 7.05e-24 | 2 | 369 | 1 | 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. |
pfam00534 | Glycos_transf_1 | 7.29e-19 | 197 | 351 | 1 | 156 | 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. |
cd03795 | GT4_WfcD-like | 6.82e-16 | 9 | 346 | 9 | 337 | Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. 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 bacteria and eukaryotes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AGY54189.1 | 7.22e-172 | 1 | 373 | 1 | 372 |
ALO15251.1 | 3.13e-137 | 1 | 366 | 1 | 365 |
ASS49078.1 | 3.25e-135 | 1 | 373 | 1 | 373 |
AZQ62941.1 | 2.06e-134 | 1 | 369 | 1 | 368 |
QWG07062.1 | 7.26e-134 | 1 | 369 | 1 | 368 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
D7AW65 | 3.55e-10 | 185 | 366 | 219 | 410 | D-inositol 3-phosphate glycosyltransferase OS=Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509) OX=446468 GN=mshA PE=3 SV=1 |
O32272 | 1.00e-08 | 48 | 313 | 82 | 324 | Putative teichuronic acid biosynthesis glycosyltransferase TuaC OS=Bacillus subtilis (strain 168) OX=224308 GN=tuaC PE=2 SV=1 |
Q47KS6 | 1.12e-08 | 185 | 366 | 225 | 416 | D-inositol 3-phosphate glycosyltransferase OS=Thermobifida fusca (strain YX) OX=269800 GN=mshA PE=3 SV=1 |
D2B9F4 | 1.13e-08 | 188 | 361 | 227 | 410 | D-inositol 3-phosphate glycosyltransferase OS=Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100) OX=479432 GN=mshA PE=3 SV=1 |
Q58577 | 4.97e-08 | 1 | 373 | 4 | 349 | Uncharacterized glycosyltransferase MJ1178 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1178 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000062 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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