UDP-N-acetylglucosamine 2-epimerase [Aromatoleum aromaticum]
List of domain hits
Name | Accession | Description | Interval | E-value | ||
WecB super family | cl46823 | UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
30-94 | 6.08e-17 | ||
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; The actual alignment was detected with superfamily member COG0381: Pssm-ID: 481163 Cd Length: 366 Bit Score: 74.33 E-value: 6.08e-17
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Name | Accession | Description | Interval | E-value | ||
WecB | COG0381 | UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
30-94 | 6.08e-17 | ||
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440150 Cd Length: 366 Bit Score: 74.33 E-value: 6.08e-17
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Epimerase_2 | pfam02350 | UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
26-104 | 1.99e-15 | ||
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain. Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 69.87 E-value: 1.99e-15
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GTB_UDP-GlcNAc_2-Epimerase | cd03786 | UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
25-94 | 2.30e-14 | ||
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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: 340819 [Multi-domain] Cd Length: 365 Bit Score: 66.85 E-value: 2.30e-14
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Name | Accession | Description | Interval | E-value | ||
WecB | COG0381 | UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; |
30-94 | 6.08e-17 | ||
UDP-N-acetylglucosamine 2-epimerase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440150 Cd Length: 366 Bit Score: 74.33 E-value: 6.08e-17
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Epimerase_2 | pfam02350 | UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine ... |
26-104 | 1.99e-15 | ||
UDP-N-acetylglucosamine 2-epimerase; This family consists of UDP-N-acetylglucosamine 2-epimerases EC:5.1.3.14 this enzyme catalyzes the production of UDP-ManNAc from UDP-GlcNAc. Note that some of the enzymes is this family are bifunctional such as Swiss:O35826 and Swiss:Q9Z0P6 in this instance Pfam matches only the N-terminal half of the protein suggesting that the additional C-terminal part (when compared to mono-functional members of this family) is responsible for the UPD-N-acetylmannosamine kinase activity of these enzymes. This hypothesis is further supported by the assumption that the C-terminal part of Swiss:O35826 is the kinase domain. Pssm-ID: 426733 [Multi-domain] Cd Length: 336 Bit Score: 69.87 E-value: 1.99e-15
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GTB_UDP-GlcNAc_2-Epimerase | cd03786 | UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the ... |
25-94 | 2.30e-14 | ||
UDP-N-acetylglucosamine 2-epimerase and similar proteins; Bacterial members of the UDP-N-Acetylglucosamine (GlcNAc) 2-Epimerase family (EC 5.1.3.14) are known to catalyze the reversible interconversion of UDP-GlcNAc and UDP-N-acetylmannosamine (UDP-ManNAc). The enzyme serves to produce an activated form of ManNAc residues (UDP-ManNAc) for use in the biosynthesis of a variety of cell surface polysaccharides; The mammalian enzyme is bifunctional, catalyzing both the inversion of stereochemistry at C-2 and the hydrolysis of the UDP-sugar linkage to generate free ManNAc. It also catalyzes the phosphorylation of ManNAc to generate ManNAc 6-phosphate, a precursor to salic acids. In mammals, sialic acids are found at the termini of oligosaccharides in a large variety of cell surface glycoconjugates and are key mediators of cell-cell recognition events. Mutations in human members of this family have been associated with Sialuria, a rare disease caused by the disorders of sialic acid metabolism. This family belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic 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: 340819 [Multi-domain] Cd Length: 365 Bit Score: 66.85 E-value: 2.30e-14
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Blast search parameters | ||||
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