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CAZyme Information: MGYG000003124_00088
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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 | Rothia mucilaginosa_A | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Micrococcaceae; Rothia; Rothia mucilaginosa_A | |||||||||||
| CAZyme ID | MGYG000003124_00088 | |||||||||||
| 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: 98805; End: 100133 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| TIGR03449 | mycothiol_MshA | 3.95e-91 | 10 | 435 | 1 | 404 | 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 | 3.17e-85 | 14 | 428 | 6 | 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 | 3.96e-50 | 29 | 431 | 14 | 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 | 3.21e-47 | 114 | 434 | 84 | 378 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| pfam00534 | Glycos_transf_1 | 1.13e-37 | 259 | 413 | 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. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QXW98101.1 | 5.36e-194 | 1 | 430 | 1 | 411 |
| ATF63583.1 | 7.89e-194 | 1 | 430 | 1 | 412 |
| BAI64356.1 | 3.08e-193 | 1 | 430 | 1 | 411 |
| BAS20452.1 | 3.08e-193 | 1 | 430 | 1 | 411 |
| VEI23806.1 | 7.06e-165 | 1 | 434 | 12 | 424 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3C4Q_A | 1.62e-56 | 10 | 434 | 3 | 406 | 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] |
| 3C48_A | 2.14e-56 | 10 | 434 | 23 | 426 | 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] |
| 6KIH_A | 5.48e-31 | 6 | 430 | 29 | 421 | 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] |
| 4N9W_A | 1.98e-14 | 234 | 432 | 173 | 366 | Crystalstructure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_A Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_B Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_C Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155],4NC9_D Crystal structure of phosphatidyl mannosyltransferase PimA [Mycolicibacterium smegmatis MC2 155] |
| 2GEJ_A | 2.15e-14 | 234 | 432 | 189 | 382 | CrystalStructure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP-Man [Mycolicibacterium smegmatis MC2 155],2GEK_A Crystal Structure of phosphatidylinositol mannosyltransferase (PimA) from Mycobacterium smegmatis in complex with GDP [Mycolicibacterium smegmatis MC2 155] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| A1R8N8 | 1.05e-66 | 14 | 434 | 5 | 400 | D-inositol 3-phosphate glycosyltransferase OS=Paenarthrobacter aurescens (strain TC1) OX=290340 GN=mshA PE=3 SV=1 |
| B8HCF8 | 1.44e-66 | 7 | 434 | 4 | 406 | D-inositol 3-phosphate glycosyltransferase OS=Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) OX=452863 GN=mshA PE=3 SV=1 |
| D1BD84 | 7.86e-66 | 10 | 433 | 8 | 417 | 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 |
| D2B9F4 | 3.20e-65 | 7 | 434 | 16 | 423 | D-inositol 3-phosphate glycosyltransferase OS=Streptosporangium roseum (strain ATCC 12428 / DSM 43021 / JCM 3005 / NI 9100) OX=479432 GN=mshA PE=3 SV=1 |
| C7R101 | 3.39e-65 | 10 | 431 | 10 | 413 | D-inositol 3-phosphate glycosyltransferase OS=Jonesia denitrificans (strain ATCC 14870 / DSM 20603 / BCRC 15368 / CIP 55.134 / JCM 11481 / NBRC 15587 / NCTC 10816 / Prevot 55134) OX=471856 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 |
|---|---|---|---|---|---|
| 1.000055 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |