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CAZyme Information: MGYG000000232_01120
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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 | Collinsella sp902364645 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Bacteria; Actinobacteriota; Coriobacteriia; Coriobacteriales; Coriobacteriaceae; Collinsella; Collinsella sp902364645 | |||||||||||
| CAZyme ID | MGYG000000232_01120 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | Putative glycosyltransferase EpsF | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | Start: 12124; End: 13236 Strand: - | |||||||||||
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| cd03812 | GT4_CapH-like | 4.58e-130 | 6 | 352 | 1 | 351 | capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1). |
| cd03807 | GT4_WbnK-like | 1.19e-51 | 6 | 364 | 1 | 360 | Shigella dysenteriae WbnK and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis. |
| cd03811 | GT4_GT28_WabH-like | 1.22e-45 | 6 | 305 | 1 | 300 | family 4 and family 28 glycosyltransferases similar to Klebsiella WabH. This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core. |
| cd03801 | GT4_PimA-like | 4.54e-44 | 6 | 329 | 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. |
| cd03808 | GT4_CapM-like | 5.09e-41 | 51 | 326 | 42 | 323 | capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins. This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| ALE35630.1 | 2.42e-156 | 4 | 361 | 31 | 391 |
| BAF40169.1 | 4.31e-153 | 4 | 361 | 21 | 375 |
| BAR04206.1 | 6.17e-151 | 4 | 365 | 2 | 363 |
| BAR02358.1 | 3.95e-149 | 4 | 364 | 21 | 378 |
| QSZ14380.1 | 4.72e-149 | 14 | 361 | 1 | 351 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 5D00_A | 2.13e-13 | 52 | 296 | 59 | 302 | Crystalstructure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D00_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate and UMP [Bacillus subtilis subsp. subtilis str. 168],5D01_A Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168],5D01_B Crystal structure of BshA from B. subtilis complexed with N-acetylglucosaminyl-malate [Bacillus subtilis subsp. subtilis str. 168] |
| 3C4Q_A | 1.47e-12 | 177 | 329 | 206 | 368 | 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 | 1.52e-12 | 177 | 329 | 226 | 388 | 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] |
| 3OKA_A | 4.10e-11 | 156 | 296 | 159 | 307 | 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 | 4.29e-11 | 156 | 296 | 159 | 307 | 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] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| P71055 | 1.66e-61 | 6 | 326 | 7 | 338 | Putative glycosyltransferase EpsF OS=Bacillus subtilis (strain 168) OX=224308 GN=epsF PE=2 SV=1 |
| Q4JSW2 | 4.10e-14 | 164 | 329 | 192 | 369 | D-inositol 3-phosphate glycosyltransferase OS=Corynebacterium jeikeium (strain K411) OX=306537 GN=mshA PE=3 SV=1 |
| Q1BEA6 | 4.41e-14 | 85 | 349 | 116 | 393 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium sp. (strain MCS) OX=164756 GN=mshA PE=3 SV=1 |
| A3PU84 | 4.41e-14 | 85 | 349 | 116 | 393 | D-inositol 3-phosphate glycosyltransferase OS=Mycobacterium sp. (strain JLS) OX=164757 GN=mshA PE=3 SV=1 |
| A1UAM8 | 4.41e-14 | 85 | 349 | 116 | 393 | 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 |
|---|---|---|---|---|---|
| 1.000070 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |