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CAZyme Information: OON09385.1
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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 | Batrachochytrium salamandrivorans | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Lineage | Chytridiomycota; Chytridiomycetes; ; NA; Batrachochytrium; Batrachochytrium salamandrivorans | |||||||||||
| CAZyme ID | OON09385.1 | |||||||||||
| CAZy Family | GT4 | |||||||||||
| CAZyme Description | dolichol-phosphate mannosyltransferase subunit 1 | |||||||||||
| CAZyme Property |
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| Genome Property |
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| Gene Location | ||||||||||||
Enzyme Prediction help
| EC | 2.4.1.83:6 |
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CAZyme Signature Domains help
| Family | Start | End | Evalue | family coverage |
|---|---|---|---|---|
| GT2 | 45 | 214 | 1.6e-34 | 0.9823529411764705 |
CDD Domains download full data without filtering help
| Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
|---|---|---|---|---|---|---|---|
| 215385 | PLN02726 | 3.51e-146 | 34 | 275 | 1 | 241 | dolichyl-phosphate beta-D-mannosyltransferase |
| 133062 | DPM1_like | 3.99e-126 | 46 | 273 | 1 | 224 | DPM1_like represents putative enzymes similar to eukaryotic DPM1. Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily. |
| 133022 | DPM_DPG-synthase_like | 3.80e-67 | 46 | 234 | 1 | 185 | DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily. DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily. |
| 395426 | Glycos_transf_2 | 8.53e-35 | 45 | 212 | 1 | 164 | Glycosyl transferase family 2. Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids. |
| 133030 | DPM1_like_bac | 1.53e-31 | 46 | 218 | 1 | 165 | Bacterial DPM1_like enzymes are related to eukaryotic DPM1. A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily. |
CAZyme Hits help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
|---|---|---|---|---|---|
| 1.90e-123 | 40 | 277 | 22 | 259 | |
| 2.51e-123 | 40 | 274 | 10 | 244 | |
| 6.68e-123 | 30 | 274 | 18 | 262 | |
| 1.60e-122 | 37 | 274 | 20 | 257 | |
| 1.60e-122 | 37 | 274 | 20 | 257 |
PDB Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 8.02e-34 | 43 | 273 | 24 | 246 | Dolichyl phosphate mannose synthase in complex with GDP and Mg2+ [Pyrococcus furiosus DSM 3638],5MM0_A Dolichyl phosphate mannose synthase in complex with GDP-mannose and Mn2+ (donor complex) [Pyrococcus furiosus DSM 3638],5MM1_A Dolichyl phosphate mannose synthase in complex with GDP and dolichyl phosphate mannose [Pyrococcus furiosus DSM 3638] |
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| 1.41e-14 | 37 | 212 | 21 | 189 | Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKE_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (F215A mutant) [Synechocystis sp. PCC 6803 substr. Kazusa] |
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| 1.41e-14 | 37 | 212 | 21 | 189 | Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_B Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_C Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa],5EKP_D Structure of the polyisoprenyl-phosphate glycosyltransferase GtrB (WT) [Synechocystis sp. PCC 6803 substr. Kazusa] |
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| 3.50e-08 | 40 | 170 | 18 | 145 | Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H1J_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H1J_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H21_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H2N_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4F_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6H4M_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_A Chain A, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_B Chain B, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_C Chain C, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_D Chain D, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_E Chain E, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_F Chain F, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_G Chain G, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_H Chain H, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_I Chain I, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_O Chain O, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_P Chain P, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315],6HNQ_Q Chain Q, Probable ss-1,3-N-acetylglucosaminyltransferase [Staphylococcus aureus subsp. aureus N315] |
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| 1.01e-06 | 43 | 137 | 6 | 94 | Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343],3BCV_B Crystal structure of a putative glycosyltransferase from Bacteroides fragilis [Bacteroides fragilis NCTC 9343] |
Swiss-Prot Hits download full data without filtering help
| Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
|---|---|---|---|---|---|---|
| 2.85e-123 | 37 | 274 | 20 | 257 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Homo sapiens OX=9606 GN=DPM1 PE=1 SV=1 |
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| 3.51e-123 | 37 | 274 | 26 | 263 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Cricetulus griseus OX=10029 GN=DPM1 PE=2 SV=1 |
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| 2.33e-122 | 43 | 274 | 26 | 257 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Bos taurus OX=9913 GN=DPM1 PE=2 SV=1 |
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| 3.31e-122 | 37 | 274 | 20 | 257 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Mus musculus OX=10090 GN=Dpm1 PE=1 SV=1 |
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| 9.13e-122 | 43 | 274 | 25 | 256 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Sus scrofa OX=9823 GN=DPM1 PE=3 SV=1 |
SignalP and Lipop Annotations help
This protein is predicted as OTHER
| Other | SP_Sec_SPI | CS Position |
|---|---|---|
| 1.000046 | 0.000001 |