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]; ...
204-772
3.35e-106
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: 341.83 E-value: 3.35e-106
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
71-197
1.53e-15
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
The actual alignment was detected with superfamily member COG1529:
Pssm-ID: 441138 [Multi-domain] Cd Length: 741 Bit Score: 80.66 E-value: 1.53e-15
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
204-772
3.35e-106
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: 341.83 E-value: 3.35e-106
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
71-197
1.53e-15
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: 80.66 E-value: 1.53e-15
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: 62.54 E-value: 7.35e-12
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
204-772
3.35e-106
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: 341.83 E-value: 3.35e-106
Aldehyde, CO or xanthine dehydrogenase, Mo-binding subunit [Energy production and conversion]; ...
71-197
1.53e-15
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: 80.66 E-value: 1.53e-15
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: 62.54 E-value: 7.35e-12
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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