Species | Ruminococcus sp900540005 | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Ruminococcus; Ruminococcus sp900540005 | |||||||||||
CAZyme ID | MGYG000001757_01294 | |||||||||||
CAZy Family | GT4 | |||||||||||
CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 22487; End: 23563 Strand: - |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd03809 | GT4_MtfB-like | 6.10e-37 | 51 | 344 | 72 | 358 | 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 | 4.27e-34 | 52 | 351 | 73 | 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 | 2.63e-30 | 44 | 356 | 66 | 380 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
pfam00534 | Glycos_transf_1 | 3.73e-30 | 178 | 333 | 5 | 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. |
cd03798 | GT4_WlbH-like | 5.36e-24 | 127 | 352 | 154 | 375 | Bordetella parapertussis WlbH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QRP37264.1 | 5.37e-136 | 1 | 354 | 1 | 354 |
ASN97925.1 | 5.37e-136 | 1 | 354 | 1 | 354 |
QIX91413.1 | 5.81e-133 | 1 | 354 | 1 | 354 |
QTE73647.1 | 4.15e-123 | 1 | 342 | 1 | 344 |
QTE72662.1 | 4.15e-123 | 1 | 342 | 1 | 344 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5I45_A | 1.12e-10 | 163 | 350 | 13 | 213 | 1.35Angstrom Crystal Structure of C-terminal Domain of Glycosyl Transferase Group 1 Family Protein (LpcC) from Francisella tularensis. [Francisella tularensis subsp. tularensis SCHU S4] |
6ZJ4_AAA | 4.03e-08 | 146 | 329 | 182 | 370 | ChainAAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis],6ZJ7_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis 768-20],6ZJH_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis 768-20],6ZMZ_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis],6ZN1_AAA Chain AAA, Trehalose phosphorylase/synthase [Thermoproteus uzoniensis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
D4GU62 | 8.04e-15 | 63 | 316 | 105 | 355 | Low-salt glycan biosynthesis hexosyltransferase Agl9 OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=agl9 PE=3 SV=1 |
Q47KS6 | 2.41e-09 | 178 | 344 | 241 | 414 | D-inositol 3-phosphate glycosyltransferase OS=Thermobifida fusca (strain YX) OX=269800 GN=mshA PE=3 SV=1 |
D1BD84 | 4.16e-09 | 175 | 348 | 236 | 416 | D-inositol 3-phosphate glycosyltransferase OS=Sanguibacter keddieii (strain ATCC 51767 / DSM 10542 / NCFB 3025 / ST-74) OX=446469 GN=mshA PE=3 SV=1 |
A0QRG8 | 6.53e-09 | 164 | 302 | 191 | 317 | GDP-mannose-dependent alpha-mannosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=mgtA PE=3 SV=1 |
Q4JAK2 | 8.03e-09 | 123 | 342 | 133 | 340 | Archaeal glycosylation protein 16 OS=Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) OX=330779 GN=agl16 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.998336 | 0.001706 | 0.000007 | 0.000003 | 0.000002 | 0.000003 |
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