Species | Ruminococcus_C sp000980705 | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus_C; Ruminococcus_C sp000980705 | |||||||||||
CAZyme ID | MGYG000001021_00613 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
CAZyme Property |
|
|||||||||||
Genome Property |
|
|||||||||||
Gene Location | Start: 53454; End: 54605 Strand: + |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03809 | GT4_MtfB-like | 1.84e-111 | 2 | 373 | 1 | 360 | glycosyltransferases MtfB, WbpX, and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide. |
cd03801 | GT4_PimA-like | 6.16e-59 | 99 | 378 | 95 | 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. |
COG0438 | RfaB | 1.50e-51 | 1 | 383 | 1 | 380 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
cd03800 | GT4_sucrose_synthase | 1.73e-41 | 144 | 373 | 161 | 396 | sucrose-phosphate synthase and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light. |
pfam00534 | Glycos_transf_1 | 4.85e-40 | 203 | 360 | 1 | 158 | 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 |
---|---|---|---|---|---|
QIX91416.1 | 1.83e-115 | 1 | 379 | 1 | 380 |
ASN97928.1 | 8.12e-109 | 1 | 379 | 1 | 380 |
QRP37261.1 | 8.12e-109 | 1 | 379 | 1 | 380 |
QEH66970.1 | 5.35e-81 | 1 | 379 | 1 | 376 |
ADZ85469.1 | 7.48e-78 | 1 | 379 | 1 | 376 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
6KIH_A | 7.14e-20 | 129 | 379 | 177 | 423 | Sucrose-phosphatesynthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_B Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_C Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_D Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_E Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_F Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_G Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_H Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_I Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_J Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_K Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus],6KIH_L Sucrose-phosphate synthase (tll1590) from Thermosynechococcus elongatus [Thermosynechococcus vestitus] |
6TVP_A | 6.84e-17 | 141 | 377 | 148 | 396 | Structureof Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155],6TVP_B Structure of Mycobacterium smegmatis alpha-maltose-1-phosphate synthase GlgM [Mycolicibacterium smegmatis MC2 155] |
2R60_A | 4.51e-11 | 170 | 379 | 221 | 458 | Structureof apo Sucrose Phosphate Synthase (SPS) of Halothermothrix orenii [Halothermothrix orenii],2R66_A Complex Structure of Sucrose Phosphate Synthase (SPS)-F6P of Halothermothrix orenii [Halothermothrix orenii H 168],2R68_A Complex Structure of Sucrose Phosphate Synthase (SPS)-S6P of Halothermothrix orenii [Halothermothrix orenii H 168] |
3L01_A | 6.92e-11 | 164 | 377 | 206 | 427 | ChainA, GlgA glycogen synthase [Pyrococcus abyssi],3L01_B Chain B, GlgA glycogen synthase [Pyrococcus abyssi] |
3FRO_A | 7.11e-11 | 164 | 377 | 206 | 427 | Crystalstructure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi],3FRO_B Crystal structure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi],3FRO_C Crystal structure of Pyrococcus abyssi glycogen synthase with open and closed conformations [Pyrococcus abyssi] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A8LDJ8 | 1.68e-24 | 139 | 380 | 178 | 426 | D-inositol 3-phosphate glycosyltransferase OS=Frankia sp. (strain EAN1pec) OX=298653 GN=mshA PE=3 SV=1 |
D7C367 | 9.47e-24 | 147 | 382 | 202 | 445 | D-inositol 3-phosphate glycosyltransferase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=mshA PE=3 SV=1 |
O34413 | 5.34e-23 | 141 | 378 | 124 | 374 | Putative glycosyltransferase YtcC OS=Bacillus subtilis (strain 168) OX=224308 GN=ytcC PE=3 SV=1 |
D1A4Q3 | 3.03e-20 | 147 | 377 | 171 | 414 | D-inositol 3-phosphate glycosyltransferase OS=Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9) OX=471852 GN=mshA PE=3 SV=1 |
Q4JSW2 | 6.91e-20 | 147 | 379 | 165 | 405 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium jeikeium (strain K411) OX=306537 GN=mshA PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000021 | 0.000017 | 0.000002 | 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.