3-hydroxy-5-phosphonooxypentane-2,4-dione thiolase catalyzes the transfer of an acetyl moiety from 3-hydroxy-5-phosphonooxypentane-2,4-dione to CoA to form glycerone phosphate and acetyl-CoA
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ...
33-282
2.27e-102
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 441435 [Multi-domain] Cd Length: 259 Bit Score: 299.35 E-value: 2.27e-102
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ...
51-274
1.74e-87
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies.
Pssm-ID: 188645 [Multi-domain] Cd Length: 235 Bit Score: 260.99 E-value: 1.74e-87
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
51-259
3.92e-16
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: 75.50 E-value: 3.92e-16
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ...
33-282
2.27e-102
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; Fructose-bisphosphate aldolase class Ia, DhnA family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 441435 [Multi-domain] Cd Length: 259 Bit Score: 299.35 E-value: 2.27e-102
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ...
51-274
1.74e-87
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs) found in bacteria and archaea. Catalysis of the enzymes proceeds via a Schiff-base mechanism like other class I aldolases, although this subfamily is clearly divergent based on sequence similarity to other class I and class II (metal dependent) aldolase subfamilies.
Pssm-ID: 188645 [Multi-domain] Cd Length: 235 Bit Score: 260.99 E-value: 1.74e-87
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
52-253
6.28e-22
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: 90.85 E-value: 6.28e-22
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
51-259
3.92e-16
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: 75.50 E-value: 3.92e-16
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in ...
219-277
1.00e-03
PdxS is a subunit of the pyridoxal 5'-phosphate (PLP) synthase, an important enzyme in deoxyxylulose 5-phosphate (DXP)-independent pathway for de novo biosynthesis of PLP, present in some eubacteria, in archaea, fungi, plants, plasmodia, and some metazoa. Together with PdxT, PdxS forms the PLP synthase, a heteromeric glutamine amidotransferase (GATase), whereby PdxT produces ammonia from glutamine and PdxS combines ammonia with five- and three-carbon phosphosugars to form PLP. PLP is the biologically active form of vitamin B6, an essential cofactor in many biochemical processes. PdxS subunits form two hexameric rings.
Pssm-ID: 240078 Cd Length: 283 Bit Score: 39.92 E-value: 1.00e-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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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