N-acetyl-beta-D-glucosaminidase [Streptococcus sp. HMSC061D10]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||
| GH20_GcnA-like | cd06565 | Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ... |
86-398 | 4.06e-115 | |||||
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. : Pssm-ID: 119335 Cd Length: 301 Bit Score: 345.73 E-value: 4.06e-115
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| Glyco_H_20C_C | pfam18088 | Glycoside Hydrolase 20C C-terminal domain; This is the C-terminal domain of Glycoside ... |
417-604 | 5.36e-72 | |||||
Glycoside Hydrolase 20C C-terminal domain; This is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. The C-terminal domain is commonly known as Domain III is important in dimerization as it forms the primary interface of the dimer. However, there is presently no evidence supporting dimerization as being necessary for catalysis. Domain III is unusual among structurally characterized GH20 enzymes but in GH20 enzymes possessing domain III, dimerization seems to be a conserved feature. : Pssm-ID: 465644 Cd Length: 194 Bit Score: 230.19 E-value: 5.36e-72
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| GcnA_N | pfam18229 | N-acetyl-beta-D-glucosaminidase N-terminal domain; This is the N-terminal domain found in ... |
3-80 | 9.46e-37 | |||||
N-acetyl-beta-D-glucosaminidase N-terminal domain; This is the N-terminal domain found in N-acetyl-beta-D-glucosaminidase (GcnA) present in Streptococcus gordonii. GcnA is a family 20 glycosidase that cleaves N-acetyl-beta-D-glucosamine and N-acetyl-beta-D-galactosamine from 4-methylumbelliferylated substrates. Similar N-terminal domains have been observed in all family 20 glycosidases although the number of beta-sheet strands may vary from five. : Pssm-ID: 408053 Cd Length: 78 Bit Score: 131.57 E-value: 9.46e-37
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| Name | Accession | Description | Interval | E-value | |||||
| GH20_GcnA-like | cd06565 | Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ... |
86-398 | 4.06e-115 | |||||
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Pssm-ID: 119335 Cd Length: 301 Bit Score: 345.73 E-value: 4.06e-115
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| Glyco_H_20C_C | pfam18088 | Glycoside Hydrolase 20C C-terminal domain; This is the C-terminal domain of Glycoside ... |
417-604 | 5.36e-72 | |||||
Glycoside Hydrolase 20C C-terminal domain; This is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. The C-terminal domain is commonly known as Domain III is important in dimerization as it forms the primary interface of the dimer. However, there is presently no evidence supporting dimerization as being necessary for catalysis. Domain III is unusual among structurally characterized GH20 enzymes but in GH20 enzymes possessing domain III, dimerization seems to be a conserved feature. Pssm-ID: 465644 Cd Length: 194 Bit Score: 230.19 E-value: 5.36e-72
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| GcnA_N | pfam18229 | N-acetyl-beta-D-glucosaminidase N-terminal domain; This is the N-terminal domain found in ... |
3-80 | 9.46e-37 | |||||
N-acetyl-beta-D-glucosaminidase N-terminal domain; This is the N-terminal domain found in N-acetyl-beta-D-glucosaminidase (GcnA) present in Streptococcus gordonii. GcnA is a family 20 glycosidase that cleaves N-acetyl-beta-D-glucosamine and N-acetyl-beta-D-galactosamine from 4-methylumbelliferylated substrates. Similar N-terminal domains have been observed in all family 20 glycosidases although the number of beta-sheet strands may vary from five. Pssm-ID: 408053 Cd Length: 78 Bit Score: 131.57 E-value: 9.46e-37
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| Name | Accession | Description | Interval | E-value | ||||||
| GH20_GcnA-like | cd06565 | Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, ... |
86-398 | 4.06e-115 | ||||||
Glycosyl hydrolase family 20 (GH20) catalytic domain of N-acetyl-beta-D-glucosaminidase (GcnA, also known as BhsA) and related proteins. GcnA is an exoglucosidase which cleaves N-acetyl-beta-D-galactosamine (NAG) and N-acetyl-beta-D-galactosamine residues from 4-methylumbelliferylated (4MU) substrates, as well as cleaving NAG from chito-oligosaccharides (i.e. NAG polymers). In contrast, sulfated forms of the substrate are unable to be cleaved and act instead as mild competitive inhibitors. Additionally, the enzyme is known to be poisoned by several first-row transition metals as well as by mercury. GcnA forms a homodimer with subunits comprised of three domains, an N-terminal zincin-like domain, this central catalytic GH20 domain, and a C-terminal alpha helical domain. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Pssm-ID: 119335 Cd Length: 301 Bit Score: 345.73 E-value: 4.06e-115
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| GH20_hexosaminidase | cd02742 | Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of ... |
85-398 | 1.00e-87 | ||||||
Beta-N-acetylhexosaminidases of glycosyl hydrolase family 20 (GH20) catalyze the removal of beta-1,4-linked N-acetyl-D-hexosamine residues from the non-reducing ends of N-acetyl-beta-D-hexosaminides including N-acetylglucosides and N-acetylgalactosides. These enzymes are broadly distributed in microorganisms, plants and animals, and play roles in various key physiological and pathological processes. These processes include cell structural integrity, energy storage, cellular signaling, fertilization, pathogen defense, viral penetration, the development of carcinomas, inflammatory events and lysosomal storage disorders. The GH20 enzymes include the eukaryotic beta-N-acetylhexosaminidases A and B, the bacterial chitobiases, dispersin B, and lacto-N-biosidase. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by the solvent or the enzyme, but by the substrate itself. Pssm-ID: 119331 [Multi-domain] Cd Length: 303 Bit Score: 275.08 E-value: 1.00e-87
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| Glyco_H_20C_C | pfam18088 | Glycoside Hydrolase 20C C-terminal domain; This is the C-terminal domain of Glycoside ... |
417-604 | 5.36e-72 | ||||||
Glycoside Hydrolase 20C C-terminal domain; This is the C-terminal domain of Glycoside hydrolase 20 C (GH20C) present in S. pneumoniae. GH20C possesses the ability to hydrolyze the beta-linkages joining either N-acetylglucosamine or N-acetylgalactosamine to a wide variety of aglycon residues. The C-terminal domain is commonly known as Domain III is important in dimerization as it forms the primary interface of the dimer. However, there is presently no evidence supporting dimerization as being necessary for catalysis. Domain III is unusual among structurally characterized GH20 enzymes but in GH20 enzymes possessing domain III, dimerization seems to be a conserved feature. Pssm-ID: 465644 Cd Length: 194 Bit Score: 230.19 E-value: 5.36e-72
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| GcnA_N | pfam18229 | N-acetyl-beta-D-glucosaminidase N-terminal domain; This is the N-terminal domain found in ... |
3-80 | 9.46e-37 | ||||||
N-acetyl-beta-D-glucosaminidase N-terminal domain; This is the N-terminal domain found in N-acetyl-beta-D-glucosaminidase (GcnA) present in Streptococcus gordonii. GcnA is a family 20 glycosidase that cleaves N-acetyl-beta-D-glucosamine and N-acetyl-beta-D-galactosamine from 4-methylumbelliferylated substrates. Similar N-terminal domains have been observed in all family 20 glycosidases although the number of beta-sheet strands may vary from five. Pssm-ID: 408053 Cd Length: 78 Bit Score: 131.57 E-value: 9.46e-37
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| GH20_DspB_LnbB-like | cd06564 | Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase ... |
104-286 | 1.29e-07 | ||||||
Glycosyl hydrolase family 20 (GH20) catalytic domain of dispersin B (DspB), lacto-N-biosidase (LnbB) and related proteins. Dispersin B is a soluble beta-N-acetylglucosamidase found in bacteria that hydrolyzes the beta-1,6-linkages of PGA (poly-beta-(1,6)-N-acetylglucosamine), a major component of the extracellular polysaccharide matrix. Lacto-N-biosidase hydrolyzes lacto-N-biose (LNB) type I oligosaccharides at the nonreducing terminus to produce lacto-N-biose as part of the GNB/LNB (galacto-N-biose/lacto-N-biose I) degradation pathway. The lacto-N-biosidase from Bifidobacterium bifidum has this GH20 domain, a carbohydrate binding module 32, and a bacterial immunoglobulin-like domain 2, as well as a YSIRK signal peptide and a G5 membrane anchor at the N and C termini, respectively. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Pssm-ID: 119334 Cd Length: 326 Bit Score: 53.83 E-value: 1.29e-07
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| GH20_chitobiase-like | cd06563 | The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl ... |
88-225 | 7.04e-03 | ||||||
The chitobiase of Serratia marcescens is a beta-N-1,4-acetylhexosaminidase with a glycosyl hydrolase family 20 (GH20) domain that hydrolyzes the beta-1,4-glycosidic linkages in oligomers derived from chitin. Chitin is degraded by a two step process: i) a chitinase hydrolyzes the chitin to oligosaccharides and disaccharides such as di-N-acetyl-D-glucosamine and chitobiose, ii) chitobiase then further degrades these oligomers into monomers. This GH20 domain family includes an N-acetylglucosamidase (GlcNAcase A) from Pseudoalteromonas piscicida and an N-acetylhexosaminidase (SpHex) from Streptomyces plicatus. SpHex lacks the C-terminal PKD (polycystic kidney disease I)-like domain found in the chitobiases. The GH20 hexosaminidases are thought to act via a catalytic mechanism in which the catalytic nucleophile is not provided by solvent or the enzyme, but by the substrate itself. Pssm-ID: 119333 Cd Length: 357 Bit Score: 39.10 E-value: 7.04e-03
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