You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000001486_01175
You are here: Home > Sequence: MGYG000001486_01175
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 | Mobilicoccus massiliensis | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Actinomycetia; Actinomycetales; Dermatophilaceae; Mobilicoccus; Mobilicoccus massiliensis | |||||||||||
| CAZyme ID | MGYG000001486_01175 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 298312; End: 300426 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03800 | GT4_sucrose_synthase | 1.06e-130 | 2 | 385 | 1 | 397 | 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 | 2.18e-67 | 26 | 388 | 18 | 365 | 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 | 2.32e-58 | 1 | 394 | 1 | 380 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| cd05006 | SIS_GmhA | 1.27e-55 | 418 | 561 | 4 | 147 | Phosphoheptose isomerase is a member of the SIS (Sugar ISomerase) superfamily. Phosphoheptose isomerase catalyzes the isomerization of sedoheptulose 7-phosphate into D-glycero-D-mannoheptose 7-phosphate. This is the first step of the biosynthesis of gram-negative bacteria inner core lipopolysaccharide precursor, L-glycero-D-mannoheptose (Gmh). |
| PRK13937 | PRK13937 | 1.54e-54 | 414 | 563 | 4 | 154 | phosphoheptose isomerase; Provisional |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| VEI49879.1 | 9.22e-236 | 1 | 563 | 1 | 561 |
| QCY33177.1 | 9.22e-236 | 1 | 563 | 1 | 561 |
| VEH43018.1 | 1.31e-235 | 1 | 563 | 1 | 561 |
| QCU79393.1 | 3.97e-212 | 1 | 562 | 1 | 567 |
| AVM63326.1 | 2.41e-210 | 1 | 563 | 1 | 569 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6KIH_A | 5.90e-67 | 3 | 393 | 33 | 426 | 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] |
| 3C4Q_A | 2.72e-45 | 1 | 393 | 1 | 407 | 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 | 3.49e-45 | 1 | 393 | 21 | 427 | 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] |
| 5I01_A | 3.42e-30 | 431 | 550 | 31 | 149 | Structureof phosphoheptose isomerase GmhA from Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090],5I01_B Structure of phosphoheptose isomerase GmhA from Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090],5I01_C Structure of phosphoheptose isomerase GmhA from Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090],5I01_D Structure of phosphoheptose isomerase GmhA from Neisseria gonorrhoeae [Neisseria gonorrhoeae FA 1090] |
| 5LTZ_A | 1.02e-27 | 442 | 561 | 42 | 161 | GmhA_mutantQ175E [Burkholderia pseudomallei K96243],5LTZ_B GmhA_mutant Q175E [Burkholderia pseudomallei K96243],5LTZ_C GmhA_mutant Q175E [Burkholderia pseudomallei K96243],5LTZ_D GmhA_mutant Q175E [Burkholderia pseudomallei K96243] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D1BZ82 | 1.17e-67 | 2 | 397 | 8 | 416 | D-inositol 3-phosphate glycosyltransferase OS=Xylanimonas cellulosilytica (strain DSM 15894 / CECT 5975 / LMG 20990 / XIL07) OX=446471 GN=mshA PE=3 SV=1 |
| A0LQY9 | 2.37e-54 | 2 | 396 | 28 | 436 | D-inositol 3-phosphate glycosyltransferase OS=Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B) OX=351607 GN=mshA PE=3 SV=1 |
| A8LDJ8 | 2.37e-54 | 2 | 395 | 22 | 430 | D-inositol 3-phosphate glycosyltransferase OS=Frankia sp. (strain EAN1pec) OX=298653 GN=mshA PE=3 SV=1 |
| D7C367 | 2.79e-54 | 2 | 392 | 38 | 444 | D-inositol 3-phosphate glycosyltransferase OS=Streptomyces bingchenggensis (strain BCW-1) OX=749414 GN=mshA PE=3 SV=1 |
| C9ZH13 | 4.16e-53 | 2 | 403 | 27 | 444 | D-inositol 3-phosphate glycosyltransferase OS=Streptomyces scabiei (strain 87.22) OX=680198 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 |
|---|---|---|---|---|---|
| 1.000017 | 0.000024 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |