class I fructose-bisphosphate aldolase catalyzes the conversion of beta-D-fructose 1,6-bisphosphate to D-glyceraldehyde 3-phosphate and dihydroxyacetone phosphate
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ...
48-350
3.22e-93
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: 278.55 E-value: 3.22e-93
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ...
68-343
2.30e-91
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: 272.93 E-value: 2.30e-91
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
68-326
9.80e-76
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: 233.05 E-value: 9.80e-76
Fructose-bisphosphate aldolase class Ia, DhnA family [Carbohydrate transport and metabolism]; ...
48-350
3.22e-93
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: 278.55 E-value: 3.22e-93
Class I fructose-1,6-bisphosphate (FBP) aldolases of the archaeal type (DhnA homologs); Class ...
68-343
2.30e-91
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: 272.93 E-value: 2.30e-91
DeoC/LacD family aldolase; This family includes diverse aldolase enzymes. This family includes ...
68-326
9.80e-76
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: 233.05 E-value: 9.80e-76
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ...
70-320
6.09e-26
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: 102.79 E-value: 6.09e-26
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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of your query sequence and the protein sequences used to curate the domain model,
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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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.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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Domains are color coded according to superfamilies
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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