deoxyribose-phosphate aldolase (DERA) catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate.
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
50-242
3.24e-73
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction.
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Pssm-ID: 188646 Cd Length: 203 Bit Score: 223.18 E-value: 3.24e-73
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
50-242
3.24e-73
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction.
Pssm-ID: 188646 Cd Length: 203 Bit Score: 223.18 E-value: 3.24e-73
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
53-242
2.57e-38
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism of nucleotides and deoxyriibonucleotides. The catalytic process is as follows: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. It is found in both gram-postive and gram-negative bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
Pssm-ID: 272921 Cd Length: 211 Bit Score: 134.13 E-value: 2.57e-38
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
54-242
1.20e-19
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.
Pssm-ID: 460332 Cd Length: 230 Bit Score: 85.13 E-value: 1.20e-19
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate ...
50-242
3.24e-73
2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family; 2-deoxyribose-5-phosphate aldolase (DERA) of the DeoC family. DERA belongs to the class I aldolases and catalyzes a reversible aldol reaction between acetaldehyde and glyceraldehyde 3-phosphate to generate 2-deoxyribose 5-phosphate. DERA is unique in catalyzing the aldol reaction between two aldehydes, and its broad substrate specificity confers considerable utility as a biocatalyst, offering an environmentally benign alternative to chiral transition metal catalysis of the asymmetric aldol reaction.
Pssm-ID: 188646 Cd Length: 203 Bit Score: 223.18 E-value: 3.24e-73
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
54-242
1.29e-49
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 162.88 E-value: 1.29e-49
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism ...
53-242
2.57e-38
deoxyribose-phosphate aldolase; Deoxyribose-phosphate aldolase is involved in the catabolism of nucleotides and deoxyriibonucleotides. The catalytic process is as follows: 2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde. It is found in both gram-postive and gram-negative bacteria. [Purines, pyrimidines, nucleosides, and nucleotides, Other, Energy metabolism, Other]
Pssm-ID: 272921 Cd Length: 211 Bit Score: 134.13 E-value: 2.57e-38
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
54-242
1.20e-19
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes the enzyme deoxyribose-phosphate aldolase EC:4.1.2.4, which is involved in nucleotide metabolism. The family also includes a group of related bacterial proteins of unknown function, see examples Swiss:Q57843 and Swiss:P76143. The family also includes tagatose 1,6-diphosphate aldolase (EC:4.1.2.40) is part of the tagatose-6-phosphate pathway of galactose-6-phosphate degradation.
Pssm-ID: 460332 Cd Length: 230 Bit Score: 85.13 E-value: 1.20e-19
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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