Species | Eubacterium_I sp900557275 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Eubacterium_I; Eubacterium_I sp900557275 | |||||||||||
CAZyme ID | MGYG000004740_01461 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | Putative glycosyltransferase EpsD | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 16985; End: 18178 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03808 | GT4_CapM-like | 7.97e-79 | 3 | 380 | 1 | 353 | capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides. |
cd03801 | GT4_PimA-like | 1.21e-44 | 3 | 385 | 1 | 366 | 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 | 6.04e-38 | 1 | 387 | 1 | 377 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd03819 | GT4_WavL-like | 1.37e-35 | 51 | 355 | 43 | 324 | 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. |
cd03817 | GT4_UGDG-like | 1.50e-35 | 77 | 387 | 74 | 372 | UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AWY98517.1 | 2.10e-131 | 2 | 385 | 3 | 384 |
ACR76500.1 | 2.81e-93 | 1 | 387 | 1 | 364 |
CBK75674.1 | 2.96e-92 | 1 | 385 | 1 | 381 |
ADL03173.1 | 1.12e-87 | 1 | 387 | 1 | 374 |
QRV18651.1 | 1.12e-87 | 1 | 387 | 1 | 374 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6KIH_A | 2.59e-12 | 90 | 390 | 133 | 427 | Sucrose-phosphatesynthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus] |
3C4Q_A | 7.57e-12 | 90 | 392 | 105 | 410 | 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 | 7.83e-12 | 90 | 392 | 125 | 430 | 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] |
7EC2_A | 6.61e-11 | 213 | 340 | 322 | 447 | ChainA, Glycosyl transferase, group 1 family protein [Staphylococcus aureus subsp. aureus USA300],7EC2_B Chain B, Glycosyl transferase, group 1 family protein [Staphylococcus aureus subsp. aureus USA300] |
3OKA_A | 6.45e-09 | 81 | 351 | 80 | 343 | Crystalstructure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum],3OKA_B Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
P71053 | 1.19e-65 | 2 | 384 | 3 | 368 | Putative glycosyltransferase EpsD OS=Bacillus subtilis (strain 168) OX=224308 GN=epsD PE=2 SV=1 |
Q48453 | 5.12e-17 | 79 | 340 | 66 | 313 | Uncharacterized 41.2 kDa protein in cps region OS=Klebsiella pneumoniae OX=573 PE=4 SV=1 |
D2S4K7 | 5.44e-16 | 82 | 390 | 104 | 422 | D-inositol 3-phosphate glycosyltransferase OS=Geodermatophilus obscurus (strain ATCC 25078 / DSM 43160 / JCM 3152 / KCC A-0152 / KCTC 9177 / NBRC 13315 / NRRL B-3577 / G-20) OX=526225 GN=mshA PE=3 SV=1 |
D1BD84 | 6.38e-16 | 90 | 386 | 111 | 416 | D-inositol 3-phosphate glycosyltransferase OS=Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74) OX=446469 GN=mshA PE=3 SV=1 |
C4LLD6 | 9.82e-16 | 79 | 385 | 120 | 432 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717) OX=645127 GN=mshA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000042 | 0.000012 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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