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bifunctional 5-dehydro-2-deoxygluconokinase/5-dehydro-2-deoxyphosphogluconate aldolase
2-deoxy-5-keto-D-gluconate 6-phosphate aldolase domain-containing protein
This domain, previously known as DUF2090, is identified as a new type of 2-deoxy-5-keto-D-gluconate 6-phosphate aldolase, unrelated to IolJ from Bacillus subtilis, based on its requirement for myo-inositol utilization.
PfkB family carbohydrate kinase
This family includes a variety of carbohydrate and pyrimidine kinases. [1]. 9519409. Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis. Petersen LA, Downs DM;. J Bacteriol 1997;179:4894-4900. (from Pfam)
5-dehydro-2-deoxygluconokinase
5-dehydro-2-deoxygluconokinase catalyzes the phosphorylation of 5-dehydro-2-deoxy-D-gluconate (2-deoxy-5-keto-D-gluconate or DKG) to 6-phospho-5-dehydro-2-deoxy-D-gluconate (DKGP); contains a C-terminal DUF2090 domain
All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by Pfam model PF09863.
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