RecName: Full=Mannosylglucosyl-3-phosphoglycerate synthase
Protein Classification
glycosyltransferase family protein( domain architecture ID 56)
glycosyltransferase family protein may 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
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| Glycosyltransferase_GTB-type super family | cl10013 | glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
8-317 | 5.77e-11 | |||||
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The actual alignment was detected with superfamily member cd03801: Pssm-ID: 471961 [Multi-domain] Cd Length: 366 Bit Score: 64.10 E-value: 5.77e-11
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| Name | Accession | Description | Interval | E-value | |||||
| GT4_PimA-like | cd03801 | phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
8-317 | 5.77e-11 | |||||
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 64.10 E-value: 5.77e-11
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| Name | Accession | Description | Interval | E-value | ||||||
| GT4_PimA-like | cd03801 | phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ... |
8-317 | 5.77e-11 | ||||||
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea. Pssm-ID: 340831 [Multi-domain] Cd Length: 366 Bit Score: 64.10 E-value: 5.77e-11
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| GT4_MtfB-like | cd03809 | glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ... |
13-318 | 1.99e-07 | ||||||
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide. Pssm-ID: 340838 [Multi-domain] Cd Length: 362 Bit Score: 53.14 E-value: 1.99e-07
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| Glycosyltransferase_GTB-type | cd01635 | glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ... |
225-336 | 1.95e-04 | ||||||
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. Pssm-ID: 340816 [Multi-domain] Cd Length: 235 Bit Score: 43.16 E-value: 1.95e-04
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| GT4_GT28_WabH-like | cd03811 | family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ... |
6-318 | 6.87e-03 | ||||||
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core. Pssm-ID: 340839 [Multi-domain] Cd Length: 351 Bit Score: 38.88 E-value: 6.87e-03
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