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CAZyme Information: MGYG000004798_02062
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Basic Information |
Genomic context |
Full Sequence |
Enzyme annotations |
CAZy signature domains |
CDD domains |
CAZyme hits |
PDB hits |
Swiss-Prot hits |
SignalP and Lipop annotations |
TMHMM annotations
Basic Information help
| Species | Enterococcus_B hirae | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae; Enterococcus_B; Enterococcus_B hirae | |||||||||||
| CAZyme ID | MGYG000004798_02062 | |||||||||||
| 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: 155802; End: 156875 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03801 | GT4_PimA-like | 5.95e-49 | 22 | 348 | 43 | 363 | 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. |
| cd03798 | GT4_WlbH-like | 1.53e-48 | 2 | 312 | 1 | 336 | 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. |
| COG0438 | RfaB | 2.21e-47 | 4 | 357 | 20 | 381 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| cd03808 | GT4_CapM-like | 3.72e-41 | 82 | 346 | 92 | 357 | capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides. |
| pfam00534 | Glycos_transf_1 | 2.95e-40 | 174 | 330 | 2 | 155 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ASV80994.1 | 6.60e-255 | 1 | 357 | 1 | 357 |
| AND71509.1 | 6.78e-248 | 1 | 357 | 1 | 357 |
| QKX65287.1 | 6.03e-198 | 1 | 357 | 1 | 356 |
| QNT64264.1 | 3.93e-144 | 1 | 350 | 1 | 348 |
| AVH75060.1 | 3.93e-144 | 1 | 350 | 1 | 348 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6KIH_A | 1.87e-18 | 104 | 319 | 170 | 390 | 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] |
| 5D00_A | 2.47e-17 | 69 | 310 | 91 | 332 | Crystalstructure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168] |
| 2JJM_A | 2.23e-16 | 69 | 304 | 101 | 336 | CrystalStructure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_B Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_C Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_D Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_E Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_F Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_G Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_H Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_I Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_J Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_K Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames],2JJM_L Crystal Structure of a family GT4 glycosyltransferase from Bacillus anthracis ORF BA1558. [Bacillus anthracis str. Ames] |
| 3MBO_A | 2.48e-16 | 69 | 304 | 121 | 356 | CrystalStructure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_B Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_C Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_D Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_E Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_F Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_G Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis],3MBO_H Crystal Structure of the Glycosyltransferase BaBshA bound with UDP and L-malate [Bacillus anthracis] |
| 6N1X_A | 3.56e-12 | 69 | 304 | 90 | 325 | ChainA, Glycosyltransferase [Staphylococcus aureus subsp. aureus CN1] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P42982 | 1.33e-16 | 69 | 310 | 89 | 330 | N-acetyl-alpha-D-glucosaminyl L-malate synthase OS=Bacillus subtilis (strain 168) OX=224308 GN=bshA PE=1 SV=2 |
| Q81ST7 | 1.13e-15 | 69 | 304 | 88 | 323 | N-acetyl-alpha-D-glucosaminyl L-malate synthase OS=Bacillus anthracis OX=1392 GN=bshA PE=1 SV=1 |
| C3PK12 | 1.40e-15 | 96 | 299 | 138 | 352 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 / CN-1) OX=548476 GN=mshA PE=3 SV=1 |
| Q8S4F6 | 1.84e-15 | 117 | 338 | 243 | 464 | Sulfoquinovosyl transferase SQD2 OS=Arabidopsis thaliana OX=3702 GN=SQD2 PE=1 SV=1 |
| C7QKE8 | 2.61e-15 | 66 | 312 | 107 | 374 | D-inositol 3-phosphate glycosyltransferase 2 OS=Catenulispora acidiphila (strain DSM 44928 / JCM 14897 / NBRC 102108 / NRRL B-24433 / ID139908) OX=479433 GN=mshA2 PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
|---|---|---|---|---|---|
| 1.000036 | 0.000005 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |