Species | Stenotrophomonas maltophilia_S | |||||||||||
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Lineage | Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia_S | |||||||||||
CAZyme ID | MGYG000003761_02614 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | N-acetyl-alpha-D-glucosaminyl L-malate synthase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1383; End: 2498 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03819 | GT4_WavL-like | 5.27e-52 | 6 | 345 | 1 | 323 | Vibrio cholerae WavL and similar sequences. This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core. |
cd03801 | GT4_PimA-like | 4.30e-34 | 14 | 345 | 12 | 335 | 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 | 5.49e-32 | 6 | 345 | 2 | 330 | 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 | 1.54e-30 | 2 | 371 | 1 | 379 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd04962 | GT4_BshA-like | 1.11e-23 | 81 | 341 | 82 | 333 | N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins. This family is most closely related to the GT1 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, while some of them are also found in Archaea and eukaryotes. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AUI08940.1 | 6.56e-253 | 1 | 371 | 1 | 371 |
QDL29403.1 | 1.54e-251 | 1 | 371 | 1 | 371 |
QGL81819.1 | 1.80e-250 | 1 | 371 | 1 | 371 |
AEM52700.1 | 1.80e-250 | 1 | 371 | 1 | 371 |
QNG79143.1 | 1.80e-250 | 1 | 371 | 1 | 371 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
7MI0_A | 7.82e-36 | 3 | 369 | 20 | 392 | ChainA, Glycosyltransferase [Rickettsia africae ESF-5] |
4XSO_A | 9.79e-07 | 240 | 317 | 246 | 323 | ChainA, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSO_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSP_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSP_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSR_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSR_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSU_A Chain A, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418],4XSU_B Chain B, Alr3699 protein [Nostoc sp. PCC 7120 = FACHB-418] |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.999899 | 0.000155 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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