Species | Helicobacter_C cinaedi | |||||||||||
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Lineage | Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Helicobacteraceae; Helicobacter_C; Helicobacter_C cinaedi | |||||||||||
CAZyme ID | MGYG000001432_01935 | |||||||||||
CAZy Family | GT2 | |||||||||||
CAZyme Description | Undecaprenyl-phosphate mannosyltransferase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 1820256; End: 1821029 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT2 | 27 | 194 | 3.4e-36 | 0.9823529411764705 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04179 | DPM_DPG-synthase_like | 2.23e-59 | 28 | 211 | 1 | 184 | 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. |
cd04188 | DPG_synthase | 2.12e-37 | 28 | 226 | 1 | 203 | 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. |
pfam00535 | Glycos_transf_2 | 4.95e-37 | 27 | 192 | 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. |
cd06442 | DPM1_like | 2.11e-36 | 28 | 252 | 1 | 223 | 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. |
cd04187 | DPM1_like_bac | 1.17e-33 | 28 | 202 | 1 | 171 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
BAM33153.1 | 1.45e-185 | 1 | 257 | 1 | 257 |
BBB20739.1 | 1.19e-184 | 1 | 257 | 1 | 257 |
QOQ91808.1 | 1.39e-163 | 28 | 257 | 1 | 230 |
QOQ97165.1 | 1.39e-163 | 28 | 257 | 1 | 230 |
BAM12879.1 | 6.78e-151 | 46 | 257 | 2 | 213 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5MLZ_A | 3.23e-17 | 26 | 238 | 25 | 236 | 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] |
6YV7_A | 2.85e-07 | 26 | 143 | 45 | 160 | MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548] |
6YV7_B | 2.85e-07 | 26 | 143 | 44 | 159 | MannosyltransferasePcManGT from Pyrobaculum calidifontis [Pyrobaculum calidifontis JCM 11548],6YV8_B Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP and Mn2+ [Pyrobaculum calidifontis JCM 11548],6YV9_A Mannosyltransferase PcManGT from Pyrobaculum calidifontis in complex with GDP-Man and Mn2+ [Pyrobaculum calidifontis JCM 11548] |
4Y6N_A | 6.76e-06 | 25 | 135 | 48 | 159 | Crystalstructure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-1 [Mycobacterium tuberculosis H37Rv],4Y6U_A Mycobacterial protein [Mycobacterium tuberculosis H37Rv],4Y7F_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and 3-(phosphonooxy)propanoic acid (PPA) - GpgS Mn2+ UDP-Glc PPA [Mycobacterium tuberculosis H37Rv],4Y7G_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and glycerol 3-phosphate (G3P) - GpgS Mn2+ UDP-Glc G3P [Mycobacterium tuberculosis H37Rv],4Y9X_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate-glucose (UDP-Glc) and phosphoglyceric acid (PGA) - GpgS Mn2+ UDP-Glc PGA-3 [Mycobacterium tuberculosis H37Rv],5JQX_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_B Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_C Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JQX_D Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with phosphoglyceric acid (PGA) - GpgS*PGA [Mycobacterium tuberculosis H37Ra],5JSX_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+ and uridine-diphosphate-glucose (UDP-Glc) [Mycobacterium tuberculosis H37Ra],5JT0_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate (UDP) and glucosyl-3-phosphoglycerate (GPG) - GpgS*GPG*UDP*Mn2+ [Mycobacterium tuberculosis H37Rv],5JUC_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with Mn2+, uridine-diphosphate (UDP) and glucosyl-3-phosphoglycerate (GPG) - GpgS*GPG*UDP*Mn2+_2 [Mycobacterium tuberculosis H37Rv],5JUD_A Crystal structure of glucosyl-3-phosphoglycerate synthase from Mycobacterium tuberculosis in complex with uridine-diphosphate (UDP) - GpgS*UDP [Mycobacterium tuberculosis variant bovis AF2122/97] |
3E25_A | 6.90e-06 | 25 | 135 | 44 | 155 | ChainA, Crystal structure of M. tuberculosis glucosyl-3-phosphoglycerate synthase [Mycobacterium tuberculosis],3E26_A Chain A, Crystal structure of M. tuberculosis glucosyl-3-phosphoglycerate synthase [Mycobacterium tuberculosis] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q8D342 | 5.20e-19 | 23 | 232 | 4 | 204 | Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase OS=Wigglesworthia glossinidia brevipalpis OX=36870 GN=arnC PE=3 SV=1 |
Q1JQ93 | 7.85e-19 | 27 | 236 | 28 | 240 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Bos taurus OX=9913 GN=DPM1 PE=2 SV=1 |
Q9VIU7 | 1.09e-18 | 24 | 236 | 6 | 221 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Drosophila melanogaster OX=7227 GN=Dpm1 PE=3 SV=1 |
Q9WU83 | 1.66e-18 | 27 | 236 | 34 | 246 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Cricetulus griseus OX=10029 GN=DPM1 PE=2 SV=1 |
Q9LM93 | 3.18e-18 | 27 | 236 | 16 | 226 | Dolichol-phosphate mannosyltransferase subunit 1 OS=Arabidopsis thaliana OX=3702 GN=DPMS1 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000069 | 0.000000 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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