glycoside hydrolase family 65 protein is an inverting phosphorylase that catalyzes the reversible phosphorolysis of alpha-glucosides; similar to Bacillus subtilis maltose phosphorylase
Glycosyl hydrolase family 65 central catalytic domain; This family of glycosyl hydrolases ...
323-696
0e+00
Glycosyl hydrolase family 65 central catalytic domain; This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface.
Pssm-ID: 281612 Cd Length: 387 Bit Score: 559.70 E-value: 0e+00
Glycosyl hydrolase family 65 central catalytic domain; This family of glycosyl hydrolases ...
323-696
0e+00
Glycosyl hydrolase family 65 central catalytic domain; This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The central domain is the catalytic domain, which binds a phosphate ion that is proximal the the highly conserved Glu. The arrangement of the phosphate and the glutamate is thought to cause nucleophilic attack on the anomeric carbon atom. The catalytic domain also forms the majority of the dimerization interface.
Pssm-ID: 281612 Cd Length: 387 Bit Score: 559.70 E-value: 0e+00
Glycosyl hydrolase family 65, N-terminal domain; This family of glycosyl hydrolases contains ...
16-266
1.61e-77
Glycosyl hydrolase family 65, N-terminal domain; This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. This domain is believed to be essential for catalytic activity although its precise function remains unknown.
Pssm-ID: 460999 [Multi-domain] Cd Length: 237 Bit Score: 249.79 E-value: 1.61e-77
Glycosyl hydrolase family 65, C-terminal domain; This family of glycosyl hydrolases contains ...
700-750
3.46e-16
Glycosyl hydrolase family 65, C-terminal domain; This family of glycosyl hydrolases contains vacuolar acid trehalase and maltose phosphorylase.Maltose phosphorylase (MP) is a dimeric enzyme that catalyzes the conversion of maltose and inorganic phosphate into beta-D-glucose-1-phosphate and glucose. The C-terminal domain forms a two layered jelly roll motif. This domain is situated at the base of the catalytic domain, however its function remains unknown.
Pssm-ID: 460997 [Multi-domain] Cd Length: 51 Bit Score: 72.82 E-value: 3.46e-16
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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