Species | Longibaculum sp900538465 | |||||||||||
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Lineage | Bacteria; Firmicutes; Bacilli; Erysipelotrichales; Erysipelatoclostridiaceae; Longibaculum; Longibaculum sp900538465 | |||||||||||
CAZyme ID | MGYG000001635_01862 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | Glycosyltransferase Gtf1 | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 33442; End: 35883 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
pfam04464 | Glyphos_transf | 2.17e-53 | 38 | 397 | 2 | 359 | CDP-Glycerol:Poly(glycerophosphate) glycerophosphotransferase. Wall-associated teichoic acids are a heterogeneous class of phosphate-rich polymers that are covalently linked to the cell wall peptidoglycan of gram-positive bacteria. They consist of a main chain of phosphodiester-linked polyols and/or sugar moieties attached to peptidoglycan via a linkage unit. CDP-glycerol:poly(glycerophosphate) glycerophosphotransferase is responsible for the polymerization of the main chain of the teichoic acid by sequential transfer of glycerol-phosphate units from CDP-glycerol to the linkage unit lipid. |
cd03811 | GT4_GT28_WabH-like | 1.91e-48 | 419 | 790 | 1 | 329 | family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core. |
COG1887 | TagB | 1.12e-30 | 12 | 397 | 1 | 385 | CDP-glycerol glycerophosphotransferase, TagB/SpsB family [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism]. |
cd03801 | GT4_PimA-like | 2.19e-28 | 515 | 813 | 72 | 366 | 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. |
pfam00534 | Glycos_transf_1 | 3.25e-23 | 649 | 801 | 1 | 157 | Glycosyl transferases group 1. Mutations in this domain of PIGA lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
AMK55912.1 | 9.93e-315 | 3 | 813 | 4 | 812 |
QBE99381.1 | 1.11e-182 | 28 | 813 | 24 | 802 |
QJU15211.1 | 5.47e-180 | 7 | 812 | 3 | 801 |
QQQ92281.1 | 6.43e-180 | 7 | 813 | 4 | 797 |
ANU74732.2 | 9.83e-180 | 7 | 813 | 18 | 811 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3L7I_A | 1.60e-33 | 42 | 396 | 354 | 714 | 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 | 1.17e-32 | 42 | 396 | 354 | 714 | 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 | 2.73e-32 | 42 | 396 | 354 | 714 | 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] |
4X6L_A | 1.90e-07 | 556 | 773 | 239 | 443 | 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 | 1.90e-07 | 556 | 773 | 239 | 443 | 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 |
---|---|---|---|---|---|---|
Q8RKI5 | 1.77e-36 | 43 | 394 | 34 | 390 | Teichoic acid poly(glycerol phosphate) polymerase OS=Bacillus spizizenii (strain ATCC 23059 / NRRL B-14472 / W23) OX=655816 GN=tarF PE=1 SV=1 |
Q5HLM5 | 8.44e-33 | 42 | 396 | 354 | 714 | Teichoic acid poly(glycerol phosphate) polymerase OS=Staphylococcus epidermidis (strain ATCC 35984 / RP62A) OX=176279 GN=tagF PE=1 SV=1 |
P13485 | 2.15e-26 | 35 | 397 | 376 | 743 | Teichoic acid poly(glycerol phosphate) polymerase OS=Bacillus subtilis (strain 168) OX=224308 GN=tagF PE=1 SV=1 |
Q2G1C1 | 2.71e-25 | 39 | 397 | 26 | 388 | Teichoic acid glycerol-phosphate transferase OS=Staphylococcus aureus (strain NCTC 8325 / PS 47) OX=93061 GN=tarF PE=1 SV=1 |
Q58459 | 2.57e-19 | 542 | 763 | 105 | 316 | Uncharacterized glycosyltransferase MJ1059 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1059 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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1.000025 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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