Gene Ontology annotation through association of InterPro records with GO terms
Combined Automated Annotation using Multiple IEA Methods
UniProtKB entry for Pseudomonas putida KT2440 XdhA (Q88F21)
Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization.
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The purified strain-86 enzyme oxidized hypoxanthine and xanthine with NAD+ as preferred electron acceptor.
"oxidation of hypoxanthine, xanthine, purine, and some aromatic aldehydes, using"
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The enzyme contained distinct large and small subunits and spectroscopically detected FAD and two iron-sulfur centers.
"XDH from P. putida 86 consists of 91.0 kDa and 46.2 kDa"
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Similar potentials of the molybdenum, FeSI, and FAD centers support their role as a coupled electron-transfer chain.
"The midpoint potentials determined for the molybdenum, FeSI and FAD redox couples are close to each other"
Identification of a chemoreceptor that specifically mediates chemotaxis toward metabolizable purine derivatives.
OpenScientist deep-research report for Pseudomonas putida KT2440 xdhA
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The report correctly distinguishes the XdhA electron-transfer subunit from the XdhB catalytic molybdenum subunit.
"Importantly, XdhA is **not** the molybdenum-cofactor catalytic subunit"
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It explicitly identifies the target-specific evidence gap.
"No direct biochemical study of the KT2440 protein."