aspartyl/asparaginyl beta-hydroxylase domain-containing protein similar to Pseudomonas aeruginosa lipopolysaccharide biosynthetic protein LpxO, a Fe2+/alpha-ketoglutarate-dependent dioxygenase homolog
lipid A hydroxylase LpxO; Members of this family are LpxO, an enzyme that modifies one of the ...
16-297
0e+00
lipid A hydroxylase LpxO; Members of this family are LpxO, an enzyme that modifies one of the lipid chains in lipid A by hydroxylation, with resulting changes in resistance to the host immune response and to the antibiotic colistin. This family, as built, includes LpxO1 from Pseudomonas aeruginosa, but not its paralog LpxO2.
:
Pssm-ID: 468010 Cd Length: 297 Bit Score: 589.99 E-value: 0e+00
lipid A hydroxylase LpxO; Members of this family are LpxO, an enzyme that modifies one of the ...
16-297
0e+00
lipid A hydroxylase LpxO; Members of this family are LpxO, an enzyme that modifies one of the lipid chains in lipid A by hydroxylation, with resulting changes in resistance to the host immune response and to the antibiotic colistin. This family, as built, includes LpxO1 from Pseudomonas aeruginosa, but not its paralog LpxO2.
Pssm-ID: 468010 Cd Length: 297 Bit Score: 589.99 E-value: 0e+00
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
70-222
9.18e-62
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.
Pssm-ID: 461552 Cd Length: 157 Bit Score: 192.86 E-value: 9.18e-62
lipid A hydroxylase LpxO; Members of this family are LpxO, an enzyme that modifies one of the ...
16-297
0e+00
lipid A hydroxylase LpxO; Members of this family are LpxO, an enzyme that modifies one of the lipid chains in lipid A by hydroxylation, with resulting changes in resistance to the host immune response and to the antibiotic colistin. This family, as built, includes LpxO1 from Pseudomonas aeruginosa, but not its paralog LpxO2.
Pssm-ID: 468010 Cd Length: 297 Bit Score: 589.99 E-value: 0e+00
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases ...
70-222
9.18e-62
Aspartyl/Asparaginyl beta-hydroxylase; Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyze oxidative reactions in a range of metabolic processes. Proline 3-hydroxylase hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. The structure of proline 3-hydroxylase contains the conserved motifs present in other 2-OG oxygenases including a jelly roll strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. This family represent the arginine, asparagine and proline hydroxylases. The aspartyl/asparaginyl beta-hydroxylase (EC:1.14.11.16) specifically hydroxylates one aspartic or asparagine residue in certain epidermal growth factor-like domains of a number of proteins.
Pssm-ID: 461552 Cd Length: 157 Bit Score: 192.86 E-value: 9.18e-62
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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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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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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