Species | Streptococcus vestibularis | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae; Streptococcus; Streptococcus vestibularis | |||||||||||
CAZyme ID | MGYG000002302_00384 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | Glycosyltransferase Gtf1 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 74178; End: 75689 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
TIGR02918 | TIGR02918 | 0.0 | 1 | 499 | 1 | 500 | accessory Sec system glycosylation protein GtfA. Members of this protein family are found only in Gram-positive bacteria of the Firmicutes lineage, including several species of Staphylococcus, Streptococcus, and Lactobacillus. Members are associated with glycosylation of serine-rich glycoproteins exported by the accessory Sec system. [Protein fate, Protein modification and repair] |
cd04949 | GT4_GtfA-like | 1.21e-117 | 192 | 492 | 36 | 328 | accessory Sec system glycosyltransferase GtfA and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general 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 in bacteria. |
cd03820 | GT4_AmsD-like | 8.60e-32 | 166 | 492 | 46 | 349 | amylovoran biosynthesis glycosyltransferase AmsD and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran. |
COG0438 | RfaB | 4.47e-21 | 184 | 501 | 56 | 379 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd03801 | GT4_PimA-like | 1.00e-20 | 169 | 460 | 40 | 327 | 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 |
---|---|---|---|---|---|
VED86995.1 | 0.0 | 1 | 503 | 1 | 503 |
AMB82194.1 | 0.0 | 1 | 503 | 1 | 503 |
QKH70941.1 | 0.0 | 1 | 503 | 1 | 503 |
AIY20590.1 | 0.0 | 1 | 503 | 1 | 503 |
VED87521.1 | 0.0 | 1 | 503 | 1 | 503 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5E9T_A | 4.95e-203 | 2 | 499 | 2 | 500 | Crystalstructure of GtfA/B complex [Streptococcus gordonii],5E9T_C Crystal structure of GtfA/B complex [Streptococcus gordonii],5E9U_A Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_C Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_E Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii],5E9U_G Crystal structure of GtfA/B complex bound to UDP and GlcNAc [Streptococcus gordonii] |
4PQG_A | 3.81e-197 | 1 | 503 | 9 | 511 | Crystalstructure of the pneumococcal O-GlcNAc transferase GtfA in complex with UDP and GlcNAc [Streptococcus pneumoniae TIGR4],4PQG_B Crystal structure of the pneumococcal O-GlcNAc transferase GtfA in complex with UDP and GlcNAc [Streptococcus pneumoniae TIGR4] |
7EC2_A | 6.12e-36 | 15 | 496 | 15 | 490 | 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] |
4X6L_A | 1.01e-28 | 113 | 495 | 119 | 490 | ChainA, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_C Chain C, TarM [Staphylococcus aureus subsp. aureus 21178],4X6L_D Chain D, TarM [Staphylococcus aureus subsp. aureus 21178],4X7P_A Chain A, TarM [Staphylococcus aureus subsp. aureus 21178],4X7P_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178] |
4X7M_A | 1.01e-28 | 113 | 495 | 119 | 490 | ChainA, TarM [Staphylococcus aureus subsp. aureus 21178],4X7M_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178],4X7R_A Chain A, TarM [Staphylococcus aureus subsp. aureus 21178],4X7R_B Chain B, TarM [Staphylococcus aureus subsp. aureus 21178] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q9AET5 | 1.96e-205 | 1 | 499 | 1 | 500 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit OS=Streptococcus gordonii OX=1302 GN=gtfA PE=1 SV=2 |
A0A0H2URG7 | 1.58e-196 | 1 | 503 | 1 | 503 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=gtfA PE=1 SV=1 |
Q3S2Y2 | 3.52e-196 | 1 | 501 | 1 | 502 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit OS=Streptococcus agalactiae OX=1311 GN=gtfA PE=1 SV=1 |
A1C3L9 | 1.78e-183 | 1 | 501 | 1 | 503 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit OS=Streptococcus parasanguinis OX=1318 GN=gtfA PE=1 SV=1 |
A0A0S4NM89 | 8.20e-148 | 1 | 499 | 1 | 509 | UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit OS=Limosilactobacillus reuteri (strain ATCC 53608) OX=927703 GN=gtfA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000054 | 0.000005 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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