dTDP-4-dehydrorhamnose 3,5-epimerase family protein such as dTDP-4-keto-6-deoxy-D-glucose epimerase that converts dTDP-4-dehydro-6-deoxy-alpha-D-glucose into dTDP-4-dehydro-beta-L-rhamnose or dTDP-4-dehydro-6-deoxy-alpha-D-allose
dTDP-4-dehydrorhamnose 3,5-epimerase; This family catalyze the isomerization of ...
12-176
4.21e-110
dTDP-4-dehydrorhamnose 3,5-epimerase; This family catalyze the isomerization of dTDP-4-dehydro-6-deoxy -D-glucose with dTDP-4-dehydro-6-deoxy-L-mannose. The EC number of this enzyme is 5.1.3.13.
Pssm-ID: 459991 Cd Length: 164 Bit Score: 310.85 E-value: 4.21e-110
RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production; RmlC (deoxythymidine ...
4-171
3.78e-104
RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production; RmlC (deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-D-hexulose 3, 5-epimerase or dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase; also known as RfbC) is a carbohydrate epimerase involved in the production of dTDP-L-rhamnose, a precursor of the bacterial cell wall constituent, L-rhamnose. L-Rhamnose (6-deoxy-l-mannose) plays an important role in the cell-wall structure of many bacterial species. It has been found to contribute to the virulence of several species, including the Gram-negative Salmonella enterica and Vibrio cholerae, where it is present as a part of the O-antigen, and is essential for the growth of Gram-positive bacteria such as Streptococcus pyogenes. RmlC converts dTDP-6-deoxy-D-xylo-4-hexulose to dTDP-6-deoxy-L-xylo-hexulose by catalyzing the epimerization of the 5-methyl and 3-hydroxyl groups of hexulose, the third of four steps in the dTDP-L-rhamnose biosynthetic pathway. RmlC belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380337 Cd Length: 168 Bit Score: 295.87 E-value: 3.78e-104
dTDP-4-dehydrorhamnose 3,5-epimerase; This enzyme participates in the biosynthesis of ...
4-177
2.08e-98
dTDP-4-dehydrorhamnose 3,5-epimerase; This enzyme participates in the biosynthesis of dTDP-L-rhamnose, often as a precursor to LPS O-antigen [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 273510 Cd Length: 176 Bit Score: 281.98 E-value: 2.08e-98
dTDP-4-dehydrorhamnose 3,5-epimerase; This family catalyze the isomerization of ...
12-176
4.21e-110
dTDP-4-dehydrorhamnose 3,5-epimerase; This family catalyze the isomerization of dTDP-4-dehydro-6-deoxy -D-glucose with dTDP-4-dehydro-6-deoxy-L-mannose. The EC number of this enzyme is 5.1.3.13.
Pssm-ID: 459991 Cd Length: 164 Bit Score: 310.85 E-value: 4.21e-110
RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production; RmlC (deoxythymidine ...
4-171
3.78e-104
RmlC carbohydrate epimerase, involved in dTDP-L-rhamnose production; RmlC (deoxythymidine diphosphate (dTDP)-4-keto-6-deoxy-D-hexulose 3, 5-epimerase or dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase; also known as RfbC) is a carbohydrate epimerase involved in the production of dTDP-L-rhamnose, a precursor of the bacterial cell wall constituent, L-rhamnose. L-Rhamnose (6-deoxy-l-mannose) plays an important role in the cell-wall structure of many bacterial species. It has been found to contribute to the virulence of several species, including the Gram-negative Salmonella enterica and Vibrio cholerae, where it is present as a part of the O-antigen, and is essential for the growth of Gram-positive bacteria such as Streptococcus pyogenes. RmlC converts dTDP-6-deoxy-D-xylo-4-hexulose to dTDP-6-deoxy-L-xylo-hexulose by catalyzing the epimerization of the 5-methyl and 3-hydroxyl groups of hexulose, the third of four steps in the dTDP-L-rhamnose biosynthetic pathway. RmlC belongs to the cupin superfamily with a conserved "jelly roll-like" beta-barrel fold capable of homodimerization.
Pssm-ID: 380337 Cd Length: 168 Bit Score: 295.87 E-value: 3.78e-104
dTDP-4-dehydrorhamnose 3,5-epimerase; This enzyme participates in the biosynthesis of ...
4-177
2.08e-98
dTDP-4-dehydrorhamnose 3,5-epimerase; This enzyme participates in the biosynthesis of dTDP-L-rhamnose, often as a precursor to LPS O-antigen [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 273510 Cd Length: 176 Bit Score: 281.98 E-value: 2.08e-98
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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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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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
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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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