Species | Helicobacter_D canadensis | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Helicobacteraceae; Helicobacter_D; Helicobacter_D canadensis | |||||||||||
CAZyme ID | MGYG000001348_01244 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1256930; End: 1257652 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 4 | 136 | 2e-17 | 0.7529411764705882 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04188 | DPG_synthase | 1.05e-48 | 4 | 214 | 1 | 211 | DPG_synthase is involved in protein N-linked glycosylation. 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. |
cd04179 | DPM_DPG-synthase_like | 1.11e-33 | 4 | 193 | 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. |
PTZ00260 | PTZ00260 | 3.43e-30 | 2 | 233 | 72 | 316 | dolichyl-phosphate beta-glucosyltransferase; Provisional |
cd06442 | DPM1_like | 7.86e-30 | 4 | 231 | 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. |
PLN02726 | PLN02726 | 3.31e-18 | 33 | 232 | 41 | 240 | dolichyl-phosphate beta-D-mannosyltransferase |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QOQ96233.1 | 2.38e-81 | 1 | 231 | 6 | 246 |
QOQ90051.1 | 1.93e-80 | 1 | 231 | 6 | 246 |
BBB19399.1 | 1.93e-80 | 1 | 231 | 6 | 246 |
BAM31807.1 | 1.93e-80 | 1 | 231 | 6 | 246 |
BAM11821.1 | 1.93e-80 | 1 | 231 | 6 | 246 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5MLZ_A | 3.76e-09 | 2 | 232 | 25 | 247 | Dolichylphosphate 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
D4GUA0 | 9.59e-23 | 2 | 217 | 19 | 232 | Glycosyltransferase AglD OS=Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) OX=309800 GN=aglD PE=1 SV=1 |
A2DZE8 | 9.84e-20 | 2 | 217 | 75 | 294 | Dolichyl-phosphate beta-glucosyltransferase ALG5A OS=Trichomonas vaginalis OX=5722 GN=ALG5A PE=1 SV=1 |
A2EK20 | 2.91e-19 | 5 | 220 | 78 | 300 | Dolichyl-phosphate beta-glucosyltransferase ALG5B OS=Trichomonas vaginalis OX=5722 GN=ALG5B PE=1 SV=1 |
A2E3C6 | 9.85e-19 | 2 | 217 | 76 | 298 | Dolichyl-phosphate beta-glucosyltransferase ALG5D OS=Trichomonas vaginalis OX=5722 GN=ALG5D PE=1 SV=1 |
A5GFZ5 | 1.44e-18 | 3 | 217 | 27 | 240 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Sus scrofa OX=9823 GN=DPM1 PE=3 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000062 | 0.000001 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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