Species | Peptostreptococcus russellii_A | |||||||||||
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Lineage | Bacteria; Firmicutes_A; Clostridia; Peptostreptococcales; Peptostreptococcaceae; Peptostreptococcus; Peptostreptococcus russellii_A | |||||||||||
CAZyme ID | MGYG000001601_00392 | |||||||||||
CAZy Family | GT81 | |||||||||||
CAZyme Description | Polyprenol monophosphomannose synthase | |||||||||||
CAZyme Property |
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Genome Property |
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Gene Location | Start: 17457; End: 18146 Strand: + |
Family | Start | End | Evalue | family coverage |
---|---|---|---|---|
GT81 | 4 | 184 | 3.7e-29 | 0.658703071672355 |
Cdd ID | Domain | E-Value | qStart | qEnd | sStart | sEnd | Domain Description |
---|---|---|---|---|---|---|---|
cd04179 | DPM_DPG-synthase_like | 1.71e-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. |
cd04188 | DPG_synthase | 4.56e-23 | 5 | 196 | 1 | 206 | 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 | 4.59e-23 | 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. |
cd06423 | CESA_like | 7.77e-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. |
cd00761 | Glyco_tranf_GTA_type | 6.90e-21 | 5 | 91 | 1 | 88 | Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold. Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities. |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End |
---|---|---|---|---|---|
QEZ70004.1 | 1.80e-101 | 2 | 227 | 4 | 229 |
CEK39207.1 | 2.56e-101 | 2 | 227 | 4 | 229 |
CEJ74759.1 | 2.56e-101 | 2 | 227 | 4 | 229 |
QYE97464.1 | 5.99e-100 | 2 | 227 | 4 | 229 |
AUN15364.1 | 3.45e-99 | 2 | 227 | 4 | 229 |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
3F1Y_A | 1.45e-08 | 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] |
6YV7_A | 5.23e-06 | 4 | 177 | 46 | 226 | 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 | 5.23e-06 | 4 | 177 | 45 | 225 | 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] |
Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
---|---|---|---|---|---|---|
Q58619 | 9.69e-12 | 5 | 198 | 21 | 218 | Uncharacterized protein MJ1222 OS=Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) OX=243232 GN=MJ1222 PE=4 SV=1 |
A2ELE6 | 5.01e-11 | 1 | 105 | 76 | 189 | Dolichyl-phosphate beta-glucosyltransferase ALG5C OS=Trichomonas vaginalis OX=5722 GN=ALG5C PE=1 SV=1 |
B3VA58 | 1.81e-10 | 5 | 161 | 8 | 183 | UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminyltransferase OS=Methanococcus voltae OX=2188 GN=aglK PE=1 SV=1 |
Q57964 | 6.95e-10 | 6 | 198 | 4 | 205 | 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 |
A2DSR8 | 1.85e-09 | 1 | 158 | 73 | 246 | Dolichyl-phosphate beta-glucosyltransferase ALG5E OS=Trichomonas vaginalis OX=5722 GN=ALG5E PE=1 SV=1 |
Other | SP_Sec_SPI | LIPO_Sec_SPII | TAT_Tat_SPI | TATLIP_Sec_SPII | PILIN_Sec_SPIII |
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0.999098 | 0.000943 | 0.000010 | 0.000002 | 0.000001 | 0.000002 |
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