xanthine dehydrogenase family protein molybdopterin-binding subunit is part of an oxidase/dehydrogenase complex acting on one or more of a variety of substrates
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
182-744
5.03e-99
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
:
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 322.18 E-value: 5.03e-99
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
182-744
5.03e-99
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 322.18 E-value: 5.03e-99
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
48-167
2.43e-22
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 102.62 E-value: 2.43e-22
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.
Pssm-ID: 214971 [Multi-domain] Cd Length: 107 Bit Score: 74.09 E-value: 5.64e-16
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
182-744
5.03e-99
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 322.18 E-value: 5.03e-99
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
48-167
2.43e-22
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 102.62 E-value: 2.43e-22
Aldehyde oxidase and xanthine dehydrogenase, a/b hammerhead domain; Aldehyde oxidase catalyses the conversion of an aldehyde in the presence of oxygen and water to an acid and hydrogen peroxide. The enzyme is a homodimer, and requires FAD, molybdenum and two 2FE-2S clusters as cofactors. Xanthine dehydrogenase catalyses the hydrogenation of xanthine to urate, and also requires FAD, molybdenum and two 2FE-2S clusters as cofactors. This activity is often found in a bifunctional enzyme with xanthine oxidase activity too. The enzyme can be converted from the dehydrogenase form to the oxidase form irreversibly by proteolysis or reversibly through oxidation of sulphydryl groups.
Pssm-ID: 214971 [Multi-domain] Cd Length: 107 Bit Score: 74.09 E-value: 5.64e-16
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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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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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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