3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) hydroxylase; This is a family of ...
19-282
1.62e-119
3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) hydroxylase; This is a family of 3-deoxy-D-manno-oct-2-ulosonic acid 3-hydroxylases, which catalyze the conversion of 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) to D-glycero-D-talo-oct-2-ulosonic acid (Ko). It contains a potential iron-binding motif, HXDX(n)H (n>40). Hydroxylation activity is iron-dependent.
The actual alignment was detected with superfamily member pfam11004:
Pssm-ID: 431597 Cd Length: 273 Bit Score: 343.51 E-value: 1.62e-119
3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) hydroxylase; This is a family of ...
19-282
1.62e-119
3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) hydroxylase; This is a family of 3-deoxy-D-manno-oct-2-ulosonic acid 3-hydroxylases, which catalyze the conversion of 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) to D-glycero-D-talo-oct-2-ulosonic acid (Ko). It contains a potential iron-binding motif, HXDX(n)H (n>40). Hydroxylation activity is iron-dependent.
Pssm-ID: 431597 Cd Length: 273 Bit Score: 343.51 E-value: 1.62e-119
3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) hydroxylase; This is a family of ...
19-282
1.62e-119
3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) hydroxylase; This is a family of 3-deoxy-D-manno-oct-2-ulosonic acid 3-hydroxylases, which catalyze the conversion of 3-deoxy-D-manno-oct-2-ulosonic acid (Kdo) to D-glycero-D-talo-oct-2-ulosonic acid (Ko). It contains a potential iron-binding motif, HXDX(n)H (n>40). Hydroxylation activity is iron-dependent.
Pssm-ID: 431597 Cd Length: 273 Bit Score: 343.51 E-value: 1.62e-119
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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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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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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