3-deoxy-8-phosphooctulonate synthase catalyzes the condensation reaction between arabinose 5-phosphate and phosphoenolpyruvate to synthesize 3-deoxy-D-manno-octulosonate-8-phosphate (KDO8P), the precursor of the 8-carbon sugar KDO, which is an essential component of gram-negative bacterial lipopolysaccharides
3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope biogenesis]; 3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 442124 Cd Length: 265 Bit Score: 505.34 E-value: 0e+00
3-deoxy-8-phosphooctulonate synthase; This model describes 3-deoxy-8-phosphooctulonate ...
17-273
2.05e-152
3-deoxy-8-phosphooctulonate synthase; This model describes 3-deoxy-8-phosphooctulonate synthase. Alternate names include 2-dehydro-3-deoxyphosphooctonate aldolase, 3-deoxy-d-manno-octulosonic acid 8-phosphate and KDO-8 phosphate synthetase. It catalyzes the aldol condensation of phosphoenolpyruvate with D-arabinose 5-phosphate: phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate In Gram-negative bacteria, this is the first step in the biosynthesis of 3-deoxy-D-manno-octulosonate, part of the oligosaccharide core of lipopolysaccharide. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 130429 Cd Length: 258 Bit Score: 426.01 E-value: 2.05e-152
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino ...
15-273
3.09e-84
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino acid biosynthesis from chorismate. E-coli has three related synthetases, which are inhibited by different aromatic amino acids. This family also includes KDSA which has very similar catalytic activity but is involved in the first step of liposaccharide biosynthesis. The enzyme is also part of the shikimate pathway, EC:2.5.1.54.
Pssm-ID: 395641 Cd Length: 271 Bit Score: 253.78 E-value: 3.09e-84
3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase [Cell wall/membrane/envelope biogenesis]; 3-deoxy-D-manno-octulosonic acid (KDO) 8-phosphate synthase is part of the Pathway/BioSystem: Lipid A biosynthesis
Pssm-ID: 442124 Cd Length: 265 Bit Score: 505.34 E-value: 0e+00
3-deoxy-8-phosphooctulonate synthase; This model describes 3-deoxy-8-phosphooctulonate ...
17-273
2.05e-152
3-deoxy-8-phosphooctulonate synthase; This model describes 3-deoxy-8-phosphooctulonate synthase. Alternate names include 2-dehydro-3-deoxyphosphooctonate aldolase, 3-deoxy-d-manno-octulosonic acid 8-phosphate and KDO-8 phosphate synthetase. It catalyzes the aldol condensation of phosphoenolpyruvate with D-arabinose 5-phosphate: phosphoenolpyruvate + D-arabinose 5-phosphate + H2O = 2-dehydro-3-deoxy-D-octonate 8-phosphate + phosphate In Gram-negative bacteria, this is the first step in the biosynthesis of 3-deoxy-D-manno-octulosonate, part of the oligosaccharide core of lipopolysaccharide. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 130429 Cd Length: 258 Bit Score: 426.01 E-value: 2.05e-152
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino ...
15-273
3.09e-84
DAHP synthetase I family; Members of this family catalyze the first step in aromatic amino acid biosynthesis from chorismate. E-coli has three related synthetases, which are inhibited by different aromatic amino acids. This family also includes KDSA which has very similar catalytic activity but is involved in the first step of liposaccharide biosynthesis. The enzyme is also part of the shikimate pathway, EC:2.5.1.54.
Pssm-ID: 395641 Cd Length: 271 Bit Score: 253.78 E-value: 3.09e-84
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and ...
63-267
5.49e-22
3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase [Amino acid transport and metabolism]; 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) synthase is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 442123 Cd Length: 283 Bit Score: 92.44 E-value: 5.49e-22
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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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,
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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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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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