Species | Staphylococcus xylosus_B | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Staphylococcales; Staphylococcaceae; Staphylococcus; Staphylococcus xylosus_B | |||||||||||
CAZyme ID | MGYG000000011_00061 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | Putative glycosyltransferase TagX | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 57801; End: 58859 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 4 | 163 | 7.4e-32 | 0.9294117647058824 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam00535 | Glycos_transf_2 | 4.98e-30 | 4 | 131 | 1 | 130 | Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. |
cd00761 | Glyco_tranf_GTA_type | 6.70e-30 | 5 | 136 | 1 | 127 | Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities. |
PRK10073 | PRK10073 | 7.35e-23 | 2 | 93 | 7 | 100 | putative glycosyl transferase; Provisional |
cd04179 | DPM_DPG-synthase_like | 2.11e-20 | 5 | 114 | 1 | 114 | DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily. |
COG0463 | WcaA | 1.77e-19 | 1 | 100 | 3 | 105 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AID43487.1 | 2.44e-243 | 1 | 352 | 1 | 352 |
CEF19589.1 | 2.44e-243 | 1 | 352 | 1 | 352 |
QDW89901.1 | 1.41e-242 | 1 | 352 | 1 | 352 |
ARD73746.1 | 2.33e-241 | 1 | 352 | 1 | 352 |
AID00710.1 | 2.33e-241 | 1 | 352 | 1 | 352 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5HEA_A | 6.58e-15 | 3 | 224 | 7 | 240 | CgTstructure in hexamer [Streptococcus parasanguinis FW213],5HEA_B CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEA_C CgT structure in hexamer [Streptococcus parasanguinis FW213],5HEC_A CgT structure in dimer [Streptococcus parasanguinis FW213],5HEC_B CgT structure in dimer [Streptococcus parasanguinis FW213] |
3L7I_A | 3.26e-13 | 2 | 116 | 3 | 118 | Structureof the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_B Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_C Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A],3L7I_D Structure of the Wall Teichoic Acid Polymerase TagF [Staphylococcus epidermidis RP62A] |
3L7J_A | 3.26e-13 | 2 | 116 | 3 | 118 | ChainA, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7J_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_A Chain A, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7K_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_A Chain A, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7L_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A] |
3L7M_A | 3.26e-13 | 2 | 116 | 3 | 118 | ChainA, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_B Chain B, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_C Chain C, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A],3L7M_D Chain D, Teichoic acid biosynthesis protein F [Staphylococcus epidermidis RP62A] |
6P61_A | 4.33e-12 | 3 | 224 | 15 | 225 | Structureof a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_B Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_C Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197],6P61_D Structure of a Glycosyltransferase from Leptospira borgpetersenii serovar Hardjo-bovis (strain JB197) [Leptospira borgpetersenii serovar Hardjo-bovis str. JB197] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8NXS4 | 2.00e-66 | 1 | 348 | 1 | 353 | Putative glycosyltransferase TagX OS=Staphylococcus aureus (strain MW2) OX=196620 GN=tagX PE=3 SV=1 |
Q6GJ30 | 2.00e-66 | 1 | 348 | 1 | 353 | Putative glycosyltransferase TagX OS=Staphylococcus aureus (strain MRSA252) OX=282458 GN=tagX PE=3 SV=1 |
Q6GBJ0 | 2.00e-66 | 1 | 348 | 1 | 353 | Putative glycosyltransferase TagX OS=Staphylococcus aureus (strain MSSA476) OX=282459 GN=tagX PE=3 SV=1 |
Q99VX6 | 2.82e-66 | 1 | 348 | 1 | 353 | Putative glycosyltransferase TagX OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=tagX PE=3 SV=2 |
Q7A711 | 2.82e-66 | 1 | 348 | 1 | 353 | Putative glycosyltransferase TagX OS=Staphylococcus aureus (strain N315) OX=158879 GN=tagX PE=1 SV=2 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000030 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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