You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000001668_01225
You are here: Home > Sequence: MGYG000001668_01225
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 | UBA1259 sp900760875 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia_A; Christensenellales; Borkfalkiaceae; UBA1259; UBA1259 sp900760875 | |||||||||||
| CAZyme ID | MGYG000001668_01225 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 3198; End: 4394 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03825 | GT4_WcaC-like | 1.10e-98 | 82 | 398 | 41 | 361 | putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis. |
| cd03801 | GT4_PimA-like | 1.18e-36 | 2 | 367 | 1 | 330 | 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 | 1.58e-27 | 82 | 398 | 73 | 374 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| cd03823 | GT4_ExpE7-like | 2.06e-25 | 35 | 367 | 35 | 324 | glycosyltransferase ExpE7 and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II). |
| PRK10125 | PRK10125 | 2.34e-23 | 93 | 398 | 95 | 402 | colanic acid biosynthesis glycosyltransferase WcaC. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| AGY54104.1 | 2.40e-145 | 1 | 398 | 1 | 395 |
| QPS12772.1 | 6.41e-144 | 1 | 398 | 1 | 393 |
| QMW73962.1 | 6.41e-144 | 1 | 398 | 1 | 393 |
| QUA54041.1 | 1.08e-141 | 1 | 398 | 6 | 400 |
| ANQ53651.1 | 2.43e-129 | 1 | 398 | 1 | 396 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 6KIH_A | 1.06e-09 | 174 | 367 | 184 | 386 | 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] |
| 3OKA_A | 1.13e-07 | 176 | 360 | 135 | 334 | Crystalstructure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum],3OKA_B Crystal structure of Corynebacterium glutamicum PimB' in complex with GDP-Man (triclinic crystal form) [Corynebacterium glutamicum] |
| 3OKC_A | 1.17e-07 | 176 | 360 | 135 | 334 | Crystalstructure of Corynebacterium glutamicum PimB' bound to GDP (orthorhombic crystal form) [Corynebacterium glutamicum],3OKP_A Crystal structure of Corynebacterium glutamicum PimB' bound to GDP-Man (orthorhombic crystal form) [Corynebacterium glutamicum] |
| 6TVP_A | 1.58e-07 | 198 | 364 | 164 | 354 | 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] |
| 2IV7_A | 4.48e-06 | 227 | 352 | 186 | 318 | CrystalStructure of WaaG, a glycosyltransferase involved in lipopolysaccharide biosynthesis [Escherichia coli str. K-12 substr. W3110] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P71237 | 1.36e-19 | 93 | 398 | 95 | 402 | Putative colanic acid biosynthesis glycosyl transferase WcaC OS=Escherichia coli (strain K12) OX=83333 GN=wcaC PE=4 SV=2 |
| D6Y4U7 | 4.11e-09 | 208 | 356 | 199 | 366 | D-inositol 3-phosphate glycosyltransferase OS=Thermobispora bispora (strain ATCC 19993 / DSM 43833 / CBS 139.67 / JCM 10125 / KCTC 9307 / NBRC 14880 / R51) OX=469371 GN=mshA PE=3 SV=1 |
| A0QQZ8 | 4.17e-09 | 208 | 372 | 201 | 376 | D-inositol 3-phosphate glycosyltransferase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=mshA PE=1 SV=1 |
| B1MHQ0 | 4.25e-09 | 208 | 352 | 208 | 363 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543) OX=561007 GN=mshA PE=3 SV=1 |
| D6Z995 | 7.62e-09 | 183 | 352 | 199 | 382 | D-inositol 3-phosphate glycosyltransferase OS=Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578) OX=640132 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 |
|---|---|---|---|---|---|
| 1.000054 | 0.000002 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |