alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
1-392
0e+00
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
The actual alignment was detected with superfamily member PRK04200:
Pssm-ID: 474031 Cd Length: 395 Bit Score: 520.20 E-value: 0e+00
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ...
2-393
1.92e-166
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate transport and metabolism]; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 442852 Cd Length: 398 Bit Score: 471.55 E-value: 1.92e-166
proposed homoserine kinase; The genes in this family are largely adjacent to genes involved in ...
1-392
7.77e-162
proposed homoserine kinase; The genes in this family are largely adjacent to genes involved in the biosynthesis of threonine (aspartate kinase, homoserine dehydrogenase and threonine synthase) in genomes which are lacking any other known homoserine kinase, and in which the presence of a homoserine kinase would indicate a complete pathway for the biosynthesis of threonine. These genes are a member of the (now subfamily, formerly equivalog) TIGR00306 model describing the archaeal form of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. All of these are members of a superfamily (pfam01676) of metalloenzyme also including phosphopentomutase alkaline phosphatases and sulfatases. The proposal that this family encodes a kinase is based on analogy to phosphomutases which are intramolecular phosphotransferases. A mutase active site could evolve to bring together homoserine and a phosphate donor such as phosphoenolpyruvate resulting in a kinase activity.
Pssm-ID: 274183 Cd Length: 396 Bit Score: 459.92 E-value: 7.77e-162
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
1-393
2.14e-142
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).
Pssm-ID: 293735 Cd Length: 368 Bit Score: 409.55 E-value: 2.14e-142
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; This family represents 2, ...
40-201
6.97e-53
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), a metalloenzyme found particularly in archaea and some eubacteria, which catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in the reaction: [(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate] (EC 5.4.2.12).
Pssm-ID: 462961 [Multi-domain] Cd Length: 171 Bit Score: 173.42 E-value: 6.97e-53
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate ...
2-393
1.92e-166
2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type [Carbohydrate transport and metabolism]; 2,3-bisphosphoglycerate-independent phosphoglycerate mutase, archeal type is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 442852 Cd Length: 398 Bit Score: 471.55 E-value: 1.92e-166
proposed homoserine kinase; The genes in this family are largely adjacent to genes involved in ...
1-392
7.77e-162
proposed homoserine kinase; The genes in this family are largely adjacent to genes involved in the biosynthesis of threonine (aspartate kinase, homoserine dehydrogenase and threonine synthase) in genomes which are lacking any other known homoserine kinase, and in which the presence of a homoserine kinase would indicate a complete pathway for the biosynthesis of threonine. These genes are a member of the (now subfamily, formerly equivalog) TIGR00306 model describing the archaeal form of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. All of these are members of a superfamily (pfam01676) of metalloenzyme also including phosphopentomutase alkaline phosphatases and sulfatases. The proposal that this family encodes a kinase is based on analogy to phosphomutases which are intramolecular phosphotransferases. A mutase active site could evolve to bring together homoserine and a phosphate donor such as phosphoenolpyruvate resulting in a kinase activity.
Pssm-ID: 274183 Cd Length: 396 Bit Score: 459.92 E-value: 7.77e-162
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate ...
1-393
2.14e-142
uncharacterized subfamily of alkaline phosphatase, homologous to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) and bacterial phosphopentomutases; The proteins in this subfamily of alkaline phosphatase are not characterized. Their sequences show similarity to 2 3 bisphosphoglycerate independent phosphoglycerate mutase (iPGM) which catalyzes the interconversion of 3-phosphoglycerate to 2-phosphoglycerate, and to bacterial phosphopentomutases (PPMs) which interconvert alpha-D-ribose 5-phosphate (ribose 5-phosphate) and alpha-D-ribose 1-phosphate (ribose 1-phosphate).
Pssm-ID: 293735 Cd Length: 368 Bit Score: 409.55 E-value: 2.14e-142
phosphoglycerate mutase (2,3-diphosphoglycerate-independent), archaeal form; Experimentally characterized in archaea as 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This model describes a set of proteins in the Archaea (two each in Methanococcus jannaschii, Methanobacterium thermoautotrophicum, and Archaeoglobus fulgidus) and in Aquifex aeolicus (1 member). [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 273005 Cd Length: 396 Bit Score: 304.01 E-value: 1.33e-100
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; This family represents 2, ...
40-201
6.97e-53
2,3-bisphosphoglycerate-independent phosphoglycerate mutase; This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), a metalloenzyme found particularly in archaea and some eubacteria, which catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in the reaction: [(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate] (EC 5.4.2.12).
Pssm-ID: 462961 [Multi-domain] Cd Length: 171 Bit Score: 173.42 E-value: 6.97e-53
Metalloenzyme superfamily; This family includes phosphopentomutase and 2, ...
1-379
1.30e-39
Metalloenzyme superfamily; This family includes phosphopentomutase and 2,3-bisphosphoglycerate-independent phosphoglycerate mutase. This family is also related to pfam00245. The alignment contains the most conserved residues that are probably involved in metal binding and catalysis.
Pssm-ID: 396305 Cd Length: 410 Bit Score: 145.62 E-value: 1.30e-39
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and ...
282-365
7.59e-04
alkaline phosphatases and sulfatases; This family includes alkaline phosphatases and sulfatases. Alkaline phosphatases are non-specific phosphomonoesterases that catalyze the hydrolysis reaction via a phosphoseryl intermediate to produce inorganic phosphate and the corresponding alcohol, optimally at high pH. Alkaline phosphatase exists as a dimer, each monomer binding 2 zinc atoms and one magnesium atom, which are essential for enzymatic activity. Sulfatases catalyze the hydrolysis of sulfate esters from wide range of substrates, including steroids, carbohydrates and proteins. Sulfate esters may be formed from various alcohols and amines. The biological roles of sulfatase includes the cycling of sulfur in the environment, in the degradation of sulfated glycosaminoglycans and glycolipids in the lysosome, and in remodeling sulfated glycosaminoglycans in the extracellular space. Both alkaline phosphatase and sulfatase are essential for human metabolism. Deficiency of individual enzyme cause genetic diseases.
Pssm-ID: 293732 [Multi-domain] Cd Length: 237 Bit Score: 40.87 E-value: 7.59e-04
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- ...
280-363
4.97e-03
2 3 bisphosphoglycerate independent phosphoglycerate mutase iPGM; The 2,3-diphosphoglycerate- independent phosphoglycerate mutase (iPGM) catalyzes the interconversion of 3-phosphoglycerate (3PGA) and 2-phosphoglycerate (2PGA). They are the predominant PGM in plants and some other bacteria, including endospore forming Gram-positive bacteria and their close relatives. The two steps catalysis is a phosphatase reaction removing the phosphate from 2- or 3-phosphoglycerate, generating an enzyme-bound phosphoserine intermediate, followed by a phosphotransferase reaction as the phosphate is transferred from the enzyme back to the glycerate moiety. The iPGM exists as a dimer, each monomer binding 2 magnesium atoms, which are essential for enzymatic activity.
Pssm-ID: 293734 Cd Length: 503 Bit Score: 38.94 E-value: 4.97e-03
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.
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