GenePage for the kduD gene of Escherichia coli K-12

Primary Gene Name: kduD
EcoGene Accession Number: EG12361
K-12 Gene Accession Number: ECK2840
MG1655 Gene Identifier: b2842
Gene Name Mnemonic: Ketodeoxygluconate utilization
Alternate Gene Symbols: ygeC; yqeD
Description: 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase; KDG oxidoreductase; DKII reductase; 20-ketosteroid reductase
  # bp Upstream # bp Downstream
MW: 27070.02 ---------253 aa Pre-Run BlastP UniProt
Pre-Run BlastP NR+Env
Left End: 2982497
Left Intergenic Region

Name: araE_kduD

Length: 314 bp gap

Orientation: Codirectional-

Left_end: 2982183

Right_end: 2982496

Centisome: 64.25

Genomic Address
Counterclockwise
Minute or Centisome (%) = 64.26
Right End: 2983258
Right Intergenic Region

Name: kduD_kduI

Length: 29 bp gap

Orientation: Codirectional-

Left_end: 2983259

Right_end: 2983287

Centisome: 64.27

Purified E. coli KduD is a 2-keto-3-deoxygluconate (KDG) oxidoreductase (2-deoxy-D-gluconate 3-dehydrogenase), also known as 2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase, with a KDG Km of 30 mM; O. Hantz, Ph.D. thesis, Claude Bernard University, 1977, as cited by Tubeleviciute et al. (Tubeleviciute, 2014). KduI and KduD activities were initially determined in Erwinia chrysanthemi where they are required for pectin catabolism (Condemine, 1991). KDG is derived from pectin, a common plant heteropolysaccharide, although E. coli K-12 does not secrete pectinases or uptake pectin oligosaccharides and has only the core KDG regulon as compared to plant pathogens like Erwinia chrysanthemi, whose extracellular pectate lyases and intacellular oligogalacturonate lyase breaks pectin down mainly into 5-keto-4-deoxyuronate (DKI) monomers and to a lesser extent polygalacturonase-generated galacturonate; in E. coli K-12 galacturonate uptake and degradation is mediated by the ExuT permease and the UxaABC catabolic enzymes producing KDG, respectively, and DKI is imported by the KdgR-regulated KDG importer KdgT and catabolized to KDG by the KdgR-regulated KduID enyzymes, also producing KDG; KDG is converted to pyruvate and glyceraldehyde-3-phosphate by KdsK and Eda(KdsA) (Rodionov, 2004; Hugouvieux-Cotte-Pattat, 1996). KduI and KduD activities were initially determined in Erwinia chrysanthemi where they are required for pectin catabolism; E. coli does not catabolize pectin (Condemine, 1991). The reversible KduD oxidoreductase converts DKII to KDG in vivo, displaying DKII reductase activity; the substrate for this reaction, 3-deoxy-D-glycero-2,5-hexodiulosonate (DKII), is also known as 3-deoxy-D-glycero-hexo-2,5-diulosonate, (4S)-4,6-dihydroxy-2,5-dioxohexanoate, or 2,5-diketo-3-deoxygluconate. KduI and KduD are inducible by galacturonate and glucuronate and are required for optimal utilization of galacturonate and glucuronate at high osmolarity, presumably substituting for salt-repressed UxaC; lactose catabolism generates intracellular hexuronates (Rothe, 2013). EC 1.1.1.125 (2-deoxy-D-gluconate 3-dehydrogenase) and EC 1.1.1.127 (2-dehydro-3-deoxy-D-gluconate 5-dehydrogenase) have 2-keto-3-deoxygluconate oxidoreductase and dehydrogenase as alternative names, respectively, leading to the previous misannotation of KduD as EC 1.1.1.125. KduD may be the hexuronate dehydrogenase required for hexuronate utilization at high osmolarity. KduD is a 20-ketosteroid reductase (a reversible 20-alpha-hydroxysteroid dehydrogenase, EC 1.1.1.149) that catalyzes the in vitro reduction of a carbonyl group at the C20 position of steroid substrates with a hydroxyl group at position C21 including 11-deoxycorticosterone (11-DOC), 11-deoxycortisol (Reichstein's Compound S, RSS), cortisol, corticosterone, cortisone, and 21-hydroxypregnenolone; physiologically relevant Km values were determined for 11-DOC (0.23 mM) and RSS (0.19 mM) as well as low affinity substrate activities using the sugar substrates D-gluconate and 5-keto-D-gluconate (Hannermann, 2007; Tubeleviciute, 2014).

Go to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePageGo to GenePage

BamHI EcoRI HindIII