Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
725-993
5.22e-30
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
:
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 120.00 E-value: 5.22e-30
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes ...
37-458
2.93e-17
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes glycoside hydrolase family 55 (GH55) domains, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching, found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Also included in this family is SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E, a secreted protein encoded by SACTE_4363. Structural studies reveal an extended substrate-binding cleft with six or more subsites for sugar binding formed at the interface of two right handed beta-helical domains. Mutation studies support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base. Trichoderma harzianum and T. viride LamA1 have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A, Chaetomium thermophilum CtLam55, as well as SacteLam55A, are exo-acting enzymes.
The actual alignment was detected with superfamily member cd23668:
Pssm-ID: 483971 [Multi-domain] Cd Length: 623 Bit Score: 86.80 E-value: 2.93e-17
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
725-993
5.22e-30
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 120.00 E-value: 5.22e-30
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
37-458
2.93e-17
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.
Pssm-ID: 467840 [Multi-domain] Cd Length: 623 Bit Score: 86.80 E-value: 2.93e-17
Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure ...
45-217
4.68e-14
Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
Pssm-ID: 403800 [Multi-domain] Cd Length: 213 Bit Score: 72.35 E-value: 4.68e-14
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
905-993
3.37e-11
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.
Pssm-ID: 462480 [Multi-domain] Cd Length: 246 Bit Score: 64.59 E-value: 3.37e-11
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
730-955
1.17e-06
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 51.17 E-value: 1.17e-06
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
725-993
5.22e-30
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 120.00 E-value: 5.22e-30
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family ...
37-458
2.93e-17
fungal glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes fungal glycoside hydrolase family 55 (GH55) proteins, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Trichoderma harzianum BGN13.1 and T. viride LamA1 in this family have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A and Chaetomium thermophilum CtLam55 are exo-acting enzymes. The CtLam55 substrate binding cleft exhibits restricted access on one side, thus rendering the enzyme as an exo-beta-1,3-glucanase; this has been confirmed by thin layer chromatography experiments. Also, a binding pocket was identified that could explain binding of branched laminarin and accumulation of laminaritriose. A similar binding pocket has been observed in T. chrysosporium Lam55A through structural studies and site-directed mutagenesis; both support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base.
Pssm-ID: 467840 [Multi-domain] Cd Length: 623 Bit Score: 86.80 E-value: 2.93e-17
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes ...
43-614
8.81e-15
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes glycoside hydrolase family 55 (GH55) domains, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching, found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Also included in this family is SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E, a secreted protein encoded by SACTE_4363. Structural studies reveal an extended substrate-binding cleft with six or more subsites for sugar binding formed at the interface of two right handed beta-helical domains. Mutation studies support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base. Trichoderma harzianum and T. viride LamA1 have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A, Chaetomium thermophilum CtLam55, as well as SacteLam55A, are exo-acting enzymes.
Pssm-ID: 467839 [Multi-domain] Cd Length: 564 Bit Score: 78.58 E-value: 8.81e-15
Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure ...
45-217
4.68e-14
Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
Pssm-ID: 403800 [Multi-domain] Cd Length: 213 Bit Score: 72.35 E-value: 4.68e-14
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in ...
905-993
3.37e-11
SMP-30/Gluconolactonase/LRE-like region; This family describes a region that is found in proteins expressed by a variety of eukaryotic and prokaryotic species. These proteins include various enzymes, such as senescence marker protein 30 (SMP-30), gluconolactonase and luciferin-regenerating enzyme (LRE). SMP-30 is known to hydrolyse diisopropyl phosphorofluoridate in the liver, and has been noted as having sequence similarity, in the region described in this family, with PON1 and LRE.
Pssm-ID: 462480 [Multi-domain] Cd Length: 246 Bit Score: 64.59 E-value: 3.37e-11
Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure ...
378-431
3.51e-11
Pectate lyase superfamily protein; This family of proteins possesses a beta helical structure like Pectate lyase. This family is most closely related to glycosyl hydrolase family 28.
Pssm-ID: 403800 [Multi-domain] Cd Length: 213 Bit Score: 63.88 E-value: 3.51e-11
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
730-955
1.17e-06
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 51.17 E-value: 1.17e-06
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
714-782
1.17e-04
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 45.00 E-value: 1.17e-04
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ...
908-996
9.32e-04
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271328 [Multi-domain] Cd Length: 300 Bit Score: 42.25 E-value: 9.32e-04
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ...
908-966
9.86e-04
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 42.31 E-value: 9.86e-04
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ...
716-789
1.13e-03
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 41.80 E-value: 1.13e-03
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes ...
18-100
1.34e-03
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes glycoside hydrolase family 55 (GH55) domains, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching, found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Also included in this family is SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E, a secreted protein encoded by SACTE_4363. Structural studies reveal an extended substrate-binding cleft with six or more subsites for sugar binding formed at the interface of two right handed beta-helical domains. Mutation studies support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base. Trichoderma harzianum and T. viride LamA1 have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A, Chaetomium thermophilum CtLam55, as well as SacteLam55A, are exo-acting enzymes.
Pssm-ID: 467839 [Multi-domain] Cd Length: 564 Bit Score: 42.37 E-value: 1.34e-03
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes ...
380-452
2.70e-03
glycoside hydrolase family 55 (GH55) family domains and similar proteins; This family includes glycoside hydrolase family 55 (GH55) domains, which contains both endo- (EC 3.2.1.39) and exo-beta-1,3-glucanases (EC 3.2.1.58), based on the hydrolysis position. These enzymes hydrolyze beta-1,3-glucan bonds via inversion of stereochemistry at the anomeric carbon. GH55 is also called laminarinase due to its ability to hydrolyze laminarin, a beta-1,3-glucan with occasional beta-1,6 branching, found in brown algae such as Laminaria digitata. They have also been shown to react with the beta-1,3-glucans from fungal and plant cell walls. Also included in this family is SacteLam55A from the highly cellulolytic Streptomyces sp. SirexAA-E, a secreted protein encoded by SACTE_4363. Structural studies reveal an extended substrate-binding cleft with six or more subsites for sugar binding formed at the interface of two right handed beta-helical domains. Mutation studies support a critical glutamate as a catalytic acid and a proton relay network that activates water to serve as the catalytic base. Trichoderma harzianum and T. viride LamA1 have been characterized as endo-acting enzymes while Phanerochaete chrysosporium Lam55A, Chaetomium thermophilum CtLam55, as well as SacteLam55A, are exo-acting enzymes.
Pssm-ID: 467839 [Multi-domain] Cd Length: 564 Bit Score: 41.60 E-value: 2.70e-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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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