Species | Peptostreptococcus russellii | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|
Lineage | Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Peptostreptococcus; Peptostreptococcus russellii | |||||||||||
CAZyme ID | MGYG000001618_00251 | |||||||||||
CAZy Family | GT81 | |||||||||||
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: 315694; End: 316383 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT81 | 4 | 185 | 7.1e-29 | 0.6621160409556314 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04179 | DPM_DPG-synthase_like | 3.62e-34 | 5 | 178 | 1 | 181 | 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. |
PRK13915 | PRK13915 | 3.74e-23 | 4 | 183 | 34 | 228 | putative glucosyl-3-phosphoglycerate synthase; Provisional |
cd04188 | DPG_synthase | 1.50e-22 | 5 | 115 | 1 | 117 | 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. |
cd06423 | CESA_like | 2.91e-22 | 5 | 90 | 1 | 88 | CESA_like is the cellulose synthase superfamily. The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan. |
pfam00535 | Glycos_transf_2 | 2.17e-20 | 4 | 160 | 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. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEZ70004.1 | 9.44e-104 | 2 | 227 | 4 | 229 |
CEI73683.1 | 1.10e-102 | 2 | 227 | 4 | 229 |
CEK39207.1 | 4.45e-102 | 2 | 227 | 4 | 229 |
CEJ74759.1 | 4.45e-102 | 2 | 227 | 4 | 229 |
QYE97464.1 | 2.56e-101 | 2 | 227 | 4 | 229 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
5EKE_A | 3.79e-06 | 4 | 168 | 29 | 197 | Structureof 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] |
5EKP_A | 3.79e-06 | 4 | 168 | 29 | 197 | Structureof 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] |
3F1Y_A | 9.87e-06 | 4 | 182 | 97 | 291 | Mannosyl-3-phosphoglyceratesynthase from Rubrobacter xylanophilus [synthetic construct],3F1Y_C Mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus [synthetic construct],3KIA_A Crystal structure of mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus [synthetic construct],3KIA_C Crystal structure of mannosyl-3-phosphoglycerate synthase from Rubrobacter xylanophilus [synthetic construct],3O3P_A Crystal structure of R. xylanophilus MpgS in complex with GDP-Mannose [Rubrobacter xylanophilus],3O3P_B Crystal structure of R. xylanophilus MpgS in complex with GDP-Mannose [Rubrobacter xylanophilus] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
A2ELE6 | 1.70e-10 | 1 | 90 | 76 | 174 | Dolichyl-phosphate beta-glucosyltransferase ALG5C OS=Trichomonas vaginalis OX=5722 GN=ALG5C PE=1 SV=1 |
B3VA58 | 1.18e-09 | 5 | 161 | 8 | 183 | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase OS=Methanococcus voltae OX=2188 GN=aglK PE=1 SV=1 |
Q54J42 | 8.49e-09 | 1 | 90 | 74 | 174 | Dolichyl-phosphate beta-glucosyltransferase OS=Dictyostelium discoideum OX=44689 GN=alg5 PE=2 SV=1 |
Q57964 | 1.60e-08 | 6 | 225 | 4 | 221 | Uncharacterized protein MJ0544 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ0544 PE=4 SV=1 |
A0QZ12 | 2.13e-08 | 3 | 200 | 24 | 232 | Polyprenol monophosphomannose synthase OS=Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) OX=246196 GN=ppm1 PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
---|---|---|---|---|---|
1.000031 | 0.000014 | 0.000000 | 0.000000 | 0.000000 | 0.000000 |
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