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CAZyme Information: MGYG000002401_00130
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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 | Propionibacterium freudenreichii | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Propionibacteriales; Propionibacteriaceae; Propionibacterium; Propionibacterium freudenreichii | |||||||||||
| CAZyme ID | MGYG000002401_00130 | |||||||||||
| 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: 162316; End: 163545 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| TIGR03449 | mycothiol_MshA | 2.39e-95 | 7 | 402 | 1 | 405 | D-inositol-3-phosphate glycosyltransferase. Members of this protein family, found exclusively in the Actinobacteria, are MshA, the glycosyltransferase of mycothiol biosynthesis. Mycothiol replaces glutathione in these species. |
| cd03800 | GT4_sucrose_synthase | 9.99e-94 | 6 | 394 | 1 | 398 | 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. |
| cd03801 | GT4_PimA-like | 1.02e-57 | 6 | 397 | 1 | 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 | 2.83e-57 | 17 | 401 | 8 | 379 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| cd03817 | GT4_UGDG-like | 5.28e-45 | 43 | 396 | 31 | 372 | UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins. This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| CBL57732.1 | 3.56e-299 | 1 | 409 | 1 | 409 |
| ARO11245.1 | 3.56e-299 | 1 | 409 | 1 | 409 |
| AWY94893.1 | 3.56e-299 | 1 | 409 | 1 | 409 |
| CEP27644.1 | 3.56e-299 | 1 | 409 | 1 | 409 |
| AJQ91812.1 | 8.38e-298 | 1 | 409 | 1 | 409 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3C48_A | 3.13e-63 | 2 | 404 | 18 | 430 | Structureof the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum],3C48_B Structure of the retaining glycosyltransferase MshA: The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum- APO (OPEN) structure. [Corynebacterium glutamicum] |
| 3C4Q_A | 6.45e-63 | 5 | 404 | 1 | 410 | Structureof the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4Q_B Structure of the retaining glycosyltransferase MshA : The first step in mycothiol biosynthesis. Organism : Corynebacterium glutamicum- Complex with UDP [Corynebacterium glutamicum],3C4V_A Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum],3C4V_B Structure of the retaining glycosyltransferase MshA:The first step in mycothiol biosynthesis. Organism: Corynebacterium glutamicum : Complex with UDP and 1L-INS-1-P. [Corynebacterium glutamicum] |
| 6KIH_A | 1.81e-38 | 7 | 407 | 33 | 432 | 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 | 1.64e-15 | 105 | 401 | 95 | 401 | 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] |
| 6LDQ_A | 7.18e-14 | 7 | 135 | 8 | 138 | Sucrose-phosphatesynthase (tll1590)_27_220_406_426_from Thermosynechococcus elongatus (twinned) [Thermosynechococcus vestitus],6LDQ_B Sucrose-phosphate synthase (tll1590)_27_220_406_426_from Thermosynechococcus elongatus (twinned) [Thermosynechococcus vestitus],6LDQ_C Sucrose-phosphate synthase (tll1590)_27_220_406_426_from Thermosynechococcus elongatus (twinned) [Thermosynechococcus vestitus],6LDQ_D Sucrose-phosphate synthase (tll1590)_27_220_406_426_from Thermosynechococcus elongatus (twinned) [Thermosynechococcus vestitus] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| B2HQV2 | 4.71e-75 | 6 | 408 | 36 | 443 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium marinum (strain ATCC BAA-535 / M) OX=216594 GN=mshA PE=3 SV=1 |
| A0PVZ1 | 3.70e-73 | 6 | 408 | 33 | 440 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium ulcerans (strain Agy99) OX=362242 GN=mshA PE=3 SV=1 |
| B8ZT88 | 8.89e-72 | 10 | 403 | 2 | 400 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium leprae (strain Br4923) OX=561304 GN=mshA PE=3 SV=1 |
| P54138 | 8.89e-72 | 10 | 403 | 2 | 400 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium leprae (strain TN) OX=272631 GN=mshA PE=3 SV=2 |
| A1UAM8 | 1.19e-71 | 6 | 405 | 14 | 414 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium sp. (strain KMS) OX=189918 GN=mshA 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 |
|---|---|---|---|---|---|
| 0.999372 | 0.000659 | 0.000001 | 0.000001 | 0.000000 | 0.000001 |