TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate ...
1-237
2.85e-144
TIM-like beta/alpha barrel domains; A large family of domains similar to triose phosphate isomerase (TIM) which, in general, share an eight beta/alpha closed barrel structure.
The actual alignment was detected with superfamily member TIGR02134:
Pssm-ID: 473867 [Multi-domain] Cd Length: 236 Bit Score: 402.74 E-value: 2.85e-144
transaldolase; This small family of proteins is a member of the transaldolase sybfamily ...
1-237
2.85e-144
transaldolase; This small family of proteins is a member of the transaldolase sybfamily represented by pfam00923. Coxiella and Staphylococcus lack members of the known transaldolase equivalog families and appear to require a transaldolase activity for completion of the pentose phosphate pathway. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 131189 [Multi-domain] Cd Length: 236 Bit Score: 402.74 E-value: 2.85e-144
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
7-231
6.63e-75
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea, which are member of the MipB/TalC subfamily of class I aldolases. FSA catalyze an aldol cleavage of fructose 6-phosphate and do not utilize fructose, fructose 1-phosphate, fructose 1,6-phosphate, or dihydroxyacetone phosphate. The enzymes belong to the transaldolase family that serves in transfer reactions in the pentose phosphate cycle, and are more distantly related to fructose 1,6-bisphosphate aldolase.
Pssm-ID: 188643 [Multi-domain] Cd Length: 211 Bit Score: 225.92 E-value: 6.63e-75
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
6-231
3.36e-63
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439946 [Multi-domain] Cd Length: 214 Bit Score: 196.06 E-value: 3.36e-63
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
8-236
4.12e-49
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 160.78 E-value: 4.12e-49
transaldolase; This small family of proteins is a member of the transaldolase sybfamily ...
1-237
2.85e-144
transaldolase; This small family of proteins is a member of the transaldolase sybfamily represented by pfam00923. Coxiella and Staphylococcus lack members of the known transaldolase equivalog families and appear to require a transaldolase activity for completion of the pentose phosphate pathway. [Energy metabolism, Pentose phosphate pathway]
Pssm-ID: 131189 [Multi-domain] Cd Length: 236 Bit Score: 402.74 E-value: 2.85e-144
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; ...
7-231
6.63e-75
Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea; Transaldolase-like fructose-6-phosphate aldolases (FSA) found in bacteria and archaea, which are member of the MipB/TalC subfamily of class I aldolases. FSA catalyze an aldol cleavage of fructose 6-phosphate and do not utilize fructose, fructose 1-phosphate, fructose 1,6-phosphate, or dihydroxyacetone phosphate. The enzymes belong to the transaldolase family that serves in transfer reactions in the pentose phosphate cycle, and are more distantly related to fructose 1,6-bisphosphate aldolase.
Pssm-ID: 188643 [Multi-domain] Cd Length: 211 Bit Score: 225.92 E-value: 6.63e-75
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; ...
6-231
3.36e-63
Transaldolase/fructose-6-phosphate aldolase [Carbohydrate transport and metabolism]; Transaldolase/fructose-6-phosphate aldolase is part of the Pathway/BioSystem: Pentose phosphate pathway
Pssm-ID: 439946 [Multi-domain] Cd Length: 214 Bit Score: 196.06 E-value: 3.36e-63
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose ...
8-236
4.12e-49
Transaldolase/Fructose-6-phosphate aldolase; Transaldolase (TAL) is an enzyme of the pentose phosphate pathway (PPP) found almost ubiquitously in the three domains of life (Archaea, Bacteria, and Eukarya). TAL shares a high degree of structural similarity and sequence identity with fructose-6-phosphate aldolase (FSA). They both belong to the class I aldolase family. Their protein structures have been revealed.
Pssm-ID: 395737 [Multi-domain] Cd Length: 226 Bit Score: 160.78 E-value: 4.12e-49
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose ...
7-231
1.01e-08
Transaldolase; Transaldolase. Enzymes found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates.
Pssm-ID: 188631 [Multi-domain] Cd Length: 252 Bit Score: 54.28 E-value: 1.01e-08
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants ...
27-184
1.64e-08
Transaldolase-like proteins from plants and bacteria; Transaldolase-like proteins from plants and bacteria. Transaldolase is found in the non-oxidative branch of the pentose phosphate pathway, that catalyze the reversible transfer of a dihydroxyacetone group from fructose-6-phosphate to erythrose-4-phosphate yielding sedoheptulose-7-phosphate and glyceraldehyde-3-phosphate. They are members of the class I aldolases, who are characterized by using a Schiff-base mechanism for stabilization of the reaction intermediates.
Pssm-ID: 188642 [Multi-domain] Cd Length: 338 Bit Score: 53.87 E-value: 1.64e-08
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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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.
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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.
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(labeled illustration) Four types of hits can be shown, as available,
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