You are browsing environment: HUMAN GUT
CAZyme Information: MGYG000000133_00081
You are here: Home > Sequence: MGYG000000133_00081
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 | Blautia_A caecimuris | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Blautia_A; Blautia_A caecimuris | |||||||||||
| CAZyme ID | MGYG000000133_00081 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | D-inositol-3-phosphate glycosyltransferase | |||||||||||
| CAZyme Property |
|
|||||||||||
| Genome Property |
|
|||||||||||
| Gene Location | Start: 71170; End: 72456 Strand: + | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03801 | GT4_PimA-like | 1.05e-28 | 56 | 408 | 50 | 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 | 2.88e-28 | 71 | 413 | 66 | 380 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| pfam00534 | Glycos_transf_1 | 2.33e-22 | 222 | 389 | 2 | 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. |
| cd01635 | Glycosyltransferase_GTB-type | 1.72e-16 | 213 | 357 | 103 | 235 | glycosyltransferase family 1 and related proteins with GTB topology. 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. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common 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. |
| pfam13692 | Glyco_trans_1_4 | 3.32e-16 | 226 | 375 | 5 | 138 | Glycosyl transferases group 1. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| QRN85475.1 | 1.54e-122 | 1 | 411 | 1 | 419 |
| QII82417.1 | 8.35e-119 | 1 | 411 | 1 | 419 |
| QYF84824.1 | 2.16e-116 | 1 | 411 | 1 | 420 |
| AWE06762.1 | 2.62e-114 | 1 | 413 | 1 | 421 |
| QGV06202.1 | 9.85e-113 | 1 | 410 | 1 | 418 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5I45_A | 2.74e-07 | 223 | 410 | 29 | 212 | 1.35Angstrom Crystal Structure of C-terminal Domain of Glycosyl Transferase Group 1 Family Protein (LpcC) from Francisella tularensis. [Francisella tularensis subsp. tularensis SCHU S4] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P46915 | 3.96e-07 | 223 | 409 | 192 | 375 | Spore coat protein SA OS=Bacillus subtilis (strain 168) OX=224308 GN=cotSA PE=1 SV=1 |
| O05083 | 8.62e-07 | 236 | 387 | 194 | 334 | Uncharacterized glycosyltransferase HI_1698 OS=Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) OX=71421 GN=HI_1698 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 |
|---|---|---|---|---|---|
| 0.636766 | 0.362090 | 0.000485 | 0.000260 | 0.000180 | 0.000236 |