L-fucose isomerase (FucIase) and L-arabinose isomerase (AI) family; composed of FucIase, AI ...
1-342
0e+00
L-fucose isomerase (FucIase) and L-arabinose isomerase (AI) family; composed of FucIase, AI and similar proteins. FucIase converts L-fucose, an aldohexose, to its ketose form, which prepares it for aldol cleavage (similar to the isomerization of glucose in glycolysis). L-fucose (or 6-deoxy-L-galactose) is found in various oligo- and polysaccharides in mammals, bacteria and plants. AI catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion to D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute.
The actual alignment was detected with superfamily member PRK02929:
Pssm-ID: 470007 [Multi-domain] Cd Length: 499 Bit Score: 625.32 E-value: 0e+00
L-Arabinose isomerase (AI) catalyzes the isomerization of L-arabinose to L-ribulose, the first ...
1-342
0e+00
L-Arabinose isomerase (AI) catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion into D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute.
Pssm-ID: 239619 Cd Length: 484 Bit Score: 545.73 E-value: 0e+00
L-arabinose isomerase; This is a family of L-arabinose isomerases, AraA, EC:5.3.1.4. These ...
1-226
2.86e-151
L-arabinose isomerase; This is a family of L-arabinose isomerases, AraA, EC:5.3.1.4. These enzymes catalyze the reaction: L-arabinose <=> L-ribulose. This reaction is the first step in the pathway of L-arabinose utilization as a carbon source after entering the cell L-arabinose is converted into L-ribulose by the L-arabinose isomerases enzyme.
Pssm-ID: 426873 Cd Length: 356 Bit Score: 429.22 E-value: 2.86e-151
L-Arabinose isomerase (AI) catalyzes the isomerization of L-arabinose to L-ribulose, the first ...
1-342
0e+00
L-Arabinose isomerase (AI) catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion into D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute.
Pssm-ID: 239619 Cd Length: 484 Bit Score: 545.73 E-value: 0e+00
L-arabinose isomerase; This is a family of L-arabinose isomerases, AraA, EC:5.3.1.4. These ...
1-226
2.86e-151
L-arabinose isomerase; This is a family of L-arabinose isomerases, AraA, EC:5.3.1.4. These enzymes catalyze the reaction: L-arabinose <=> L-ribulose. This reaction is the first step in the pathway of L-arabinose utilization as a carbon source after entering the cell L-arabinose is converted into L-ribulose by the L-arabinose isomerases enzyme.
Pssm-ID: 426873 Cd Length: 356 Bit Score: 429.22 E-value: 2.86e-151
L-fucose isomerase (FucIase) and L-arabinose isomerase (AI) family; composed of FucIase, AI ...
1-340
1.17e-121
L-fucose isomerase (FucIase) and L-arabinose isomerase (AI) family; composed of FucIase, AI and similar proteins. FucIase converts L-fucose, an aldohexose, to its ketose form, which prepares it for aldol cleavage (similar to the isomerization of glucose in glycolysis). L-fucose (or 6-deoxy-L-galactose) is found in various oligo- and polysaccharides in mammals, bacteria and plants. AI catalyzes the isomerization of L-arabinose to L-ribulose, the first reaction in its conversion to D-xylulose-5-phosphate, an intermediate in the pentose phosphate pathway, which allows L-arabinose to be used as a carbon source. AI can also convert D-galactose to D-tagatose at elevated temperatures in the presence of divalent metal ions. D-tagatose, rarely found in nature, is of commercial interest as a low-calorie sugar substitute.
Pssm-ID: 238323 [Multi-domain] Cd Length: 452 Bit Score: 357.74 E-value: 1.17e-121
L-arabinose isomerase C-terminal domain; This is a family of L-arabinose isomerases, AraA, EC: ...
229-342
2.29e-65
L-arabinose isomerase C-terminal domain; This is a family of L-arabinose isomerases, AraA, EC:5.3.1.4. These enzymes catalyze the reaction: L-arabinose <=> L-ribulose. This reaction is the first step in the pathway of L-arabinose utilization as a carbon source after entering the cell L-arabinose is converted into L-ribulose by the L-arabinose isomerases enzyme. This is a C-terminal non catalytic domain.
Pssm-ID: 432056 [Multi-domain] Cd Length: 114 Bit Score: 201.94 E-value: 2.29e-65
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,
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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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