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This strain metabolized AF by a novel pathway involving its reduction to 1,5-anhydro-<jats:sc>d<\/jats:sc>-mannitol (AM) and the further conversion of AM to<jats:sc>d<\/jats:sc>-mannose by C-1 oxygenation. Growth studies showed that the AF metabolizing capability is not confined to<jats:italic>S. morelense<\/jats:italic>S-30.7.5 but is a more common feature among the<jats:italic>Rhizobiaceae<\/jats:italic>. The AF reducing enzyme was purified and characterized as a new NADPH-dependent monomeric reductase (AFR, EC 1.1.1.-) of 35.1 kDa. It catalyzed the stereoselective reduction of AF to AM and also the conversion of a number of 2-keto aldoses (osones) to the corresponding manno-configurated aldoses. In contrast, common aldoses and ketoses, as well as nonsugar aldehydes and ketones, were not reduced. A database search using the N-terminal AFR sequence retrieved a putative 35-kDa oxidoreductase encoded by the open reading frame<jats:italic>Smc04400<\/jats:italic>localized on the chromosome of<jats:italic>Sinorhizobium meliloti<\/jats:italic>1021. Based on sequence information for this locus, the<jats:italic>afr<\/jats:italic>gene was cloned from<jats:italic>S. morelense<\/jats:italic>S-30.7.5 and overexpressed in<jats:italic>Escherichia coli<\/jats:italic>. In addition to the oxidoreductase of<jats:italic>S. meliloti<\/jats:italic>1021, AFR showed high sequence similarities to putative oxidoreductases of<jats:italic>Mesorhizobium loti<\/jats:italic>,<jats:italic>Brucella suis<\/jats:italic>, and<jats:italic>B. melitensis<\/jats:italic>but not to any oxidoreductase with known functions. AFR could be assigned to the GFO\/IDH\/MocA family on the basis of highly conserved common structural features. His<jats:sub>6<\/jats:sub>-tagged AFR was used to demonstrate the utility of this enzyme for AF analysis and synthesis of AM, as well as related derivatives.<\/jats:p>","DOI":"10.1128\/aem.72.2.1248-1257.2006","type":"journal-article","created":{"date-parts":[[2006,2,3]],"date-time":"2006-02-03T21:18:24Z","timestamp":1139001504000},"page":"1248-1257","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":26,"title":["Catabolism of 1,5-Anhydro-<scp>d<\/scp>-Fructose in<i>Sinorhizobium morelense<\/i>S-30.7.5: Discovery, Characterization, and Overexpression of a New 1,5-Anhydro-<scp>d<\/scp>-Fructose Reductase and Its Application in Sugar Analysis and Rare Sugar Synthesis"],"prefix":"10.1128","volume":"72","author":[{"given":"Annette","family":"Ku\u0308hn","sequence":"first","affiliation":[{"name":"Lehrstuhl fu\u0308r Angewandte Mikrobiologie, Universita\u0308t des Saarlandes, 66123 Saarbru\u0308cken, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shukun","family":"Yu","sequence":"additional","affiliation":[{"name":"Danisco Innovation, Danisco A\/S, Langebrogade 1, P.O. 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