Species | UBA7173 sp001701135 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Muribaculaceae; UBA7173; UBA7173 sp001701135 | |||||||||||
CAZyme ID | MGYG000001937_00460 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 151429; End: 152295 Strand: - |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 5 | 109 | 1.5e-26 | 0.6176470588235294 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd00761 | Glyco_tranf_GTA_type | 1.49e-30 | 5 | 121 | 1 | 117 | 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. |
COG0463 | WcaA | 1.65e-25 | 1 | 284 | 3 | 271 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
pfam00535 | Glycos_transf_2 | 1.23e-23 | 4 | 120 | 1 | 113 | 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. |
cd06423 | CESA_like | 3.40e-16 | 8 | 128 | 4 | 122 | CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan. |
cd06433 | GT_2_WfgS_like | 3.43e-16 | 4 | 117 | 1 | 111 | WfgS and WfeV are involved in O-antigen biosynthesis. Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AUI55434.1 | 7.97e-113 | 1 | 288 | 1 | 289 |
APW35110.1 | 1.22e-110 | 1 | 288 | 1 | 292 |
QUB53174.1 | 1.22e-110 | 1 | 288 | 1 | 292 |
AFJ09375.1 | 1.44e-110 | 1 | 288 | 6 | 297 |
BAR95854.1 | 1.44e-110 | 1 | 288 | 6 | 297 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5HEA_A | 2.02e-12 | 2 | 232 | 6 | 239 | 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] |
5TZE_C | 2.78e-09 | 1 | 101 | 1 | 103 | Crystalstructure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZE_E Crystal structure of S. aureus TarS in complex with UDP-GlcNAc [Staphylococcus aureus],5TZI_C Crystal structure of S. aureus TarS 1-349 [Staphylococcus aureus],5TZJ_A Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZJ_C Crystal structure of S. aureus TarS 1-349 in complex with UDP-GlcNAc [Staphylococcus aureus],5TZK_C Crystal structure of S. aureus TarS 1-349 in complex with UDP [Staphylococcus aureus] |
5TZ8_A | 3.69e-09 | 1 | 101 | 1 | 103 | Crystalstructure of S. aureus TarS [Staphylococcus aureus],5TZ8_B Crystal structure of S. aureus TarS [Staphylococcus aureus],5TZ8_C Crystal structure of S. aureus TarS [Staphylococcus aureus] |
3L7I_A | 1.74e-07 | 3 | 106 | 4 | 108 | 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 | 1.74e-07 | 3 | 106 | 4 | 108 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q0P9C6 | 1.38e-10 | 3 | 232 | 4 | 225 | GalNAc(5)-diNAcBac-PP-undecaprenol beta-1,3-glucosyltransferase OS=Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168) OX=192222 GN=pglI PE=1 SV=1 |
A0A0H2UR96 | 1.77e-10 | 2 | 214 | 4 | 224 | Glycosyltransferase GlyG OS=Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) OX=170187 GN=glyG PE=1 SV=1 |
A0A0H3JVA1 | 1.13e-08 | 1 | 172 | 2 | 172 | Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS OS=Staphylococcus aureus (strain MW2) OX=196620 GN=tarS PE=1 SV=1 |
A0A0H3JPC6 | 2.02e-08 | 1 | 101 | 2 | 104 | Poly(ribitol-phosphate) beta-N-acetylglucosaminyltransferase TarS OS=Staphylococcus aureus (strain Mu50 / ATCC 700699) OX=158878 GN=tarS PE=1 SV=1 |
Q9CMP0 | 2.38e-08 | 2 | 133 | 434 | 563 | Chondroitin synthase OS=Pasteurella multocida (strain Pm70) OX=272843 GN=fcbD PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000067 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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