Species | Bacteroides neonati | |||||||||||
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Lineage | Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides neonati | |||||||||||
CAZyme ID | MGYG000001461_01109 | |||||||||||
CAZy Family | GT1 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 546145; End: 547266 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam13528 | Glyco_trans_1_3 | 7.01e-21 | 1 | 322 | 1 | 310 | Glycosyl transferase family 1. |
cd03785 | GT28_MurG | 1.23e-10 | 2 | 337 | 1 | 326 | undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase. MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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. |
COG1819 | YjiC | 5.39e-07 | 1 | 366 | 2 | 391 | UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism]. |
cd01635 | Glycosyltransferase_GTB-type | 4.50e-06 | 74 | 293 | 20 | 215 | glycosyltransferase family 1 and related proteins with GTB topology. 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. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common 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. |
cd03794 | GT4_WbuB-like | 4.73e-05 | 21 | 352 | 23 | 379 | Escherichia coli WbuB and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QUT77029.1 | 5.90e-202 | 1 | 363 | 1 | 363 |
QDM08445.1 | 2.37e-199 | 1 | 373 | 1 | 373 |
ALJ44787.1 | 2.37e-199 | 1 | 373 | 1 | 373 |
QRQ56460.1 | 2.37e-199 | 1 | 373 | 1 | 373 |
QUT82367.1 | 2.37e-199 | 1 | 373 | 1 | 373 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000077 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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