Species | Paraclostridium sordellii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Paraclostridium; Paraclostridium sordellii | |||||||||||
CAZyme ID | MGYG000000157_03055 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | hypothetical protein | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 2478; End: 3830 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04950 | GT4_TuaH-like | 1.07e-25 | 183 | 421 | 104 | 340 | teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins. Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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. |
cd03794 | GT4_WbuB-like | 1.41e-12 | 182 | 388 | 102 | 324 | 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 |
---|---|---|---|---|---|
AUN14733.1 | 0.0 | 1 | 450 | 1 | 450 |
CEK38523.1 | 0.0 | 1 | 450 | 1 | 450 |
CEJ74045.1 | 2.25e-317 | 1 | 450 | 1 | 450 |
ANV81165.1 | 2.89e-82 | 89 | 448 | 308 | 662 |
AZT84502.1 | 1.32e-66 | 97 | 448 | 90 | 431 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000051 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
Copyright 2022 © YIN LAB, UNL. All rights reserved. Designed by Jinfang Zheng and Boyang Hu. Maintained by Yanbin Yin.