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CAZyme Information: MGYG000002650_00233
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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 | ||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Verrucomicrobiota; Lentisphaeria; Victivallales; UBA1829; UBA11452; | |||||||||||
| CAZyme ID | MGYG000002650_00233 | |||||||||||
| 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: 13039; End: 14127 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03804 | GT4_WbaZ-like | 8.83e-153 | 3 | 356 | 1 | 356 | mannosyltransferase WbaZ and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity. |
| cd03801 | GT4_PimA-like | 9.65e-36 | 3 | 360 | 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 | 1.95e-29 | 1 | 360 | 1 | 375 | Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]. |
| cd05844 | GT4-like | 2.20e-27 | 159 | 327 | 147 | 329 | glycosyltransferase family 4 proteins. 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 glycosyltransferase family 4 (GT4). 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. |
| pfam00534 | Glycos_transf_1 | 5.91e-27 | 199 | 344 | 2 | 156 | 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 |
|---|---|---|---|---|---|
| AVM45637.1 | 9.73e-130 | 3 | 359 | 21 | 374 |
| SPP97677.1 | 1.95e-127 | 3 | 361 | 2 | 358 |
| SDT58273.1 | 4.68e-122 | 3 | 356 | 2 | 353 |
| SHG29984.1 | 5.08e-122 | 3 | 356 | 2 | 353 |
| VVC55695.1 | 5.94e-121 | 3 | 360 | 2 | 358 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 3C4Q_A | 1.88e-10 | 206 | 346 | 230 | 389 | 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 | 1.93e-10 | 206 | 346 | 250 | 409 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| D2Q1C4 | 1.39e-16 | 154 | 346 | 175 | 401 | D-inositol 3-phosphate glycosyltransferase OS=Kribbella flavida (strain DSM 17836 / JCM 10339 / NBRC 14399) OX=479435 GN=mshA PE=3 SV=1 |
| B1MHQ0 | 9.96e-14 | 154 | 346 | 181 | 397 | 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 |
| Q1BEA6 | 1.36e-12 | 154 | 346 | 176 | 392 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium sp. (strain MCS) OX=164756 GN=mshA PE=3 SV=1 |
| A3PU84 | 1.36e-12 | 154 | 346 | 176 | 392 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium sp. (strain JLS) OX=164757 GN=mshA PE=3 SV=1 |
| A1UAM8 | 1.36e-12 | 154 | 346 | 176 | 392 | 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 |
|---|---|---|---|---|---|
| 1.000077 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |